In Japanese,
Nature Genetics
参考にしての
vol 38 nu 8 august 2006 の 論文を
RIKEN FAMSBASE の使い方
In English,
Using examples of RIKEN FAMSBASE
Genetics
for Nature
vol 38 nu 8 august 2006
1 (Department of Biomolecular Design, School of Pharmaceutical Sciences, Kitasato
University)
2 (Protein Function Team, Protein Research Group, RIKEN Genomic Sciences Center)
3 (In-Silico Sciences Inc.)
Mitsuo Iwadate 1,2 , Kazuhiko Kanou 1, Daisuke Takaya 1, Genki Terashi 1, Mayuko
Takeda-Shitaka 1,2, Kinji Fuchikami 1,3, Katsuichiro Komatsu 1,3 and Hideaki
Umeyama 1,2
nature genetics vol 38 nu 8 august 2006
全遺伝子ネットワーク構成要素であるタンパク質複合体の立体構造モデリング
Protein complex 3-dimensional modeling database based upon all the genes networks
p862 From worm genetic networks to complex human deseases
a network of 350 interactions
p896
Systematic mapping of genetic interactions in Caenorhabditis
isentifies commmon modifiers
of diverse signaling pathways
Talbe 1 Synthetic genetic enhancer screens
lin-3 elegans mamalian ortholog EGR
elegans
let-23 elegans mamalian ortholog EGR receptor
etc.
lin-3 elegans
http://www.ncbi.nlm.nih.gov/
protein
lin-3 elegans
1: CAA48207 Reports
BLink, Links
Lin-3 [Caenorhabditis elegans]
gi|6776|emb|CAA48207.1|[6776]
1: CAA48207. Reports Lin-3 [Caenorhabd...[gi:6776] BLink, Links
FeaturesSequenceLOCUS
linear
CAA48207
438 aa
INV 03-DEC-1993
DEFINITION Lin-3 [Caenorhabditis elegans].
ACCESSION
VERSION
CAA48207
CAA48207.1 GI:6776
DBSOURCE
embl locus CELIN3A, accession X68070.1
KEYWORDS
.
SOURCE
Caenorhabditis elegans
ORGANISM Caenorhabditis elegans
Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
REFERENCE
AUTHORS
TITLE
1 (residues 1 to 438)
Hill,R.J. and Sternberg,P.W.
The gene lin-3 encodes an inductive signal for vulval development
in C. elegans
JOURNAL
PUBMED
FEATURES
source
Nature 358 (6386), 470-476 (1992)
1641037
Location/Qualifiers
1..438
/organism="Caenorhabditis elegans"
/strain="Bristol N2"
/db_xref="taxon:6239"
/chromosome="IVC"
/clone="cDNA clones pRH39 and pRH40"
/clone_lib="lambda Zap of R. Barstead. (Ref. JBC vol. 264
10177-10185. 1989)"
Protein
1..438
/product="Lin-3"
/function="lin-3 is necessary for C. elegans vulval
induction. Lin-3 is a putative nematode homologue of the
EGF group of growth factors."
1: CAA48207. Reports Lin-3 [Caenorhabd...[gi:6776] BLink, Links
>gi|6776|emb|CAA48207.1| Lin-3 [Caenorhabditis elegans]
MRKMLLFCILLLFMPQFTVSESCLPSWFRQERSAPEQLQSAENAAENSGSVPPDTS
RNSLETNEIGDAPS
STSTPETPTETTISEAGDDEKRTEEVAKELIEKEAEYEGEYEDEKVDEEVEEALKYN
EDATQDATSTLKP
AVRKEIEKLKEAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCDRH
YVQAFYAPINGRYN
VRLSTMSSTAQLLVQQSSTSAIPAFAFLIVMLIMFITIVVYAYRRMSKRSDDMTYTMS
HMCPPEAFNVLK
TPNGRHIPVHQIPSCSYTIPTPGTVPPNISSTPGSRIPTRQQAIRNNEQARNNFFSILR
SQGTIPSRSIN
DDDTPKHYKSVPRVEVSAINYSGHIDFSTVSYQSTESEVSKASVTCPPPAHTVINIEL
DSADTNFRSPSR
SSGEQGSPATCEPMIRHT
9: Q03345 Reports
BLink, Links
Protein lin-3 precursor (Abnormal cell lineage protein 3) (Lethal protein 94)
gi|417248|sp|Q03345|LIN3_CAEEL[417248]
1: Q03345. Reports Protein lin-3 pre...[gi:417248] BLink, Links
CommentFeaturesSequenceLOCUS
linear
Q03345
438 aa
INV 04-APR-2006
DEFINITION Protein lin-3 precursor (Abnormal cell lineage protein 3) (Lethal
protein 94).
ACCESSION
VERSION
DBSOURCE
Q03345
Q03345 GI:417248
swissprot: locus LIN3_CAEEL, accession Q03345;
class: standard.
created: Oct 1, 1993.
sequence updated: Oct 1, 1993.
annotation updated: Apr 4, 2006.
xrefs: X68070.1, CAA48207.1, Z68760.2, CAA92997.2, AL032641.1,
CAD27623.1, CAD30434.1, CAA21649.2, CAD27613.1, CAD30455.1,
D88826,
S28263
COMMENT
On or before Jun 21, 2005 this sequence version replaced
gi:25354067, gi:283549.
[FUNCTION] Essential for induction of vulval development. Ligand
for the let-23 receptor. The lin-3/let-23 pair is a simplified
version of the mammalian neuregulin-erbb network.
[SUBCELLULAR LOCATION] Membrane; single-pass type I membrane
protein.
[ALTERNATIVE PRODUCTS] Event=Alternative splicing; Named
isoforms=3; Comment=Experimental confirmation may be lacking for
some isoforms; Name=A; IsoId=Q03345-1; Sequence=Displayed; Name=B;
IsoId=Q03345-2; Sequence=VSP_001396; Name=C; IsoId=Q03345-3;
Sequence=VSP_001397.
[SIMILARITY] Contains 1 EGF-like domain.
FEATURES
source
Location/Qualifiers
1..438
/organism="Caenorhabditis elegans"
/db_xref="taxon:6239"
gene
1..438
/gene="lin-3"
/locus_tag="F36H1.4"
/note="synonym: let-94"
Protein
1..438
/gene="lin-3"
/locus_tag="F36H1.4"
/product="Protein lin-3 precursor"
Region
1..13
/gene="lin-3"
/locus_tag="F36H1.4"
/region_name="Signal"
/inference="non-experimental evidence, no additional
details recorded"
/note="Potential."
1: Q03345. Reports Protein lin-3 pre...[gi:417248] BLink, Links
>gi|417248|sp|Q03345|LIN3_CAEEL Protein lin-3 precursor (Abnormal cell lineage
protein 3) (Lethal protein 94)
MRKMLLFCILLLFMPQFTVSESCLPSWFRQERSAPEQLQSAENAAENSGSVPPDTS
RNSLETNEIGDAPS
STSTPETPTETTISEAGDDEKRTEEVAKELIEKEAEYEGEYEDEKVDEEVEEALKYN
EDATQDATSTLKP
AVRKEIEKLKEAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCDRH
YVQAFYAPINGRYN
VRLSTMSSTAQLLVQQSSTSAIPAFAFLIVMLIMFITIVVYAYRRMSKRSDDMTYTMS
HMCPPEAFNVLK
TPNGRHIPVHQIPSCSYTIPTPGTVPPNISSTPGSRIPTRQQAIRNNEQARNNFFSILR
SQGTIPSRSIN
DDDTPKHYKSVPRVEVSAINYSGHIDFSTVSYQSTESEVSKASVTCPPPAHTVINIEL
DSADTNFRSPSR
SSGEQGSPATCEPMIRHT
Disclaimer | Write to the Help Desk
NCBI | NLM | NIH
http://gtof.gsc.riken.jp/SP277/blast/bSp277.php 15sec
Query= gi|417248|sp|Q03345|LIN3_CAEEL Protein lin-3 precursor
(Abnormal cell lineage protein 3) (Lethal protein 94)
(437 letters)
Database: sp277model.tfa
1,401,339 sequences; 311,159,872 total letters
Searching..................................................done
Score
Sequences producing significant alignments:
E
(bits) Value
CAD30455.1_1_1_1 cele0 151-194 7e-04 2 F36H1.4c wormpep113 ...
132
2e-29
CAD27613.1_1_1_1 cele0 149-192 8e-04 2 F36H1.4b wormpep113 ...
132
2e-29
CAA21649.2_1_1_1 cele0 151-194 8e-04 2 F36H1.4a wormpep113 ...
132
2e-29
>CAD30455.1_1_1_1 cele0 151-194 7e-04 2 F36H1.4c wormpep113 "lin-3 growth factor
precursor"
Length = 44
Score = 132 bits (280), Expect = 2e-29
Identities = 44/44 (100%), Positives = 44/44 (100%)
Query: 150 EAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCD 193
EAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCD
Sbjct: 1
EAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCD 44
>CAD27613.1_1_1_1 cele0 149-192 8e-04 2 F36H1.4b wormpep113 "lin-3 growth factor
precursor"
Length = 44
Score = 132 bits (280), Expect = 2e-29
Identities = 44/44 (100%), Positives = 44/44 (100%)
Query: 150 EAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCD 193
EAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCD
Sbjct: 1
EAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCD 44
>CAA21649.2_1_1_1 cele0 151-194 8e-04 2 F36H1.4a wormpep113 "lin-3 growth factor
precursor"
Length = 44
Score = 132 bits (280), Expect = 2e-29
Identities = 44/44 (100%), Positives = 44/44 (100%)
Query: 150 EAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCD 193
EAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCD
Sbjct: 1
EAKCKDYCHHNATCHVEVIFREDRVSAVVPSCHCPQGWEGTRCD 44
http://mammalia.gsc.riken.jp/human/search.php 5sec
http://mammalia.gsc.riken.jp/eukaryote/search.php
let-23 elegans
5: P24348 Reports
BLink, Conserved Domains, Links
Receptor tyrosine-protein kinase let-23 precursor (Lethal protein 23)
gi|110825728|sp|P24348|LET23_CAEEL[110825728]
1: P24348. Reports Receptor tyrosine...[gi:110825728] BLink, Conserved Domains,
Links
CommentFeaturesSequenceLOCUS
linear
P24348
1323 aa
INV 25-JUL-2006
DEFINITION Receptor tyrosine-protein kinase let-23 precursor (Lethal protein
23).
ACCESSION
VERSION
DBSOURCE
P24348
P24348 GI:110825728
swissprot: locus LET23_CAEEL, accession P24348;
class: standard.
created: Mar 1, 1992.
sequence updated: Jul 25, 2006.
annotation updated: Jul 25, 2006.
COMMENT
On Jul 28, 2006 this sequence version replaced gi:27923985.
[FUNCTION] Tyrosine kinase receptor required for the induction of
vulval differentiation. Possible receptor for the inductive signal
required for vulval development. Activated by lin-3 and acts by way
of let-60 RAS. The lin-3/let-23 pair is a simplified version of the
mammalian neuregulin-ERBB network.
[CATALYTIC ACTIVITY] ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate.
[SUBCELLULAR LOCATION] Cell membrane; apical cell membrane;
single-pass type I membrane protein. Cell membrane; basolateral
cell membrane; single-pass type I membrane protein. Basolateral and
apical membrane of cell junctions in epithelial vulval precursor
cells.
[TISSUE SPECIFICITY] Vulval precursor cells.
[DEVELOPMENTAL STAGE] Expressed during L2 and L3 larval stages.
[SIMILARITY] Belongs to the Tyr protein kinase family. EGF receptor
subfamily.
[SIMILARITY] Contains 1 protein kinase domain.
[CAUTION] Ref.2 sequence differs from that shown due to erroneous
gene model prediction.
FEATURES
source
Location/Qualifiers
1..1323
/organism="Caenorhabditis elegans"
/db_xref="taxon:6239"
gene
1..1323
/gene="let-23"
/locus_tag="ZK1067.1"
/note="synonym: kin-7"
Protein
1..1323
/gene="let-23"
/locus_tag="ZK1067.1"
/product="Receptor tyrosine-protein kinase let-23
precursor"
/EC_number="2.7.10.1"
1: P24348. Reports Receptor tyrosine...[gi:110825728] BLink, Conserved Domains,
Links
>gi|110825728|sp|P24348|LET23_CAEEL Receptor tyrosine-protein kinase let-23
precursor (Lethal protein 23)
MRYPPSIGSILLIIPIFLTFFGNSNAQLWKRCVSPQDCLCSGTTNGISRYGTGNILEDL
ETMYRGCRRVY
GNLEITWIEANEIKKWRESTNSTVDPKNEDSPLKSINFFDNLEEIRGSLIIYRANIQKI
SFPRLRVIYGD
EVFHDNALYIHKNDKVHEVVMRELRVIRNGSVTIQDNPKMCYIGDKIDWKELLYDP
DVQKVETTNSHQHC
YQNGKSMAKCHESCNDKCWGSGDNDCQRVYRSVCPKSCSQCFYSNSTSSYECCDS
ACLGGCTGHGPKNCI
ACSKYELDGICIETCPSRKIFNHKTGRLVFNPDGRYQNGNHCVKECPPELLIENDVC
VRHCSDGHHYDAT
KDVRECEKCRSSSCPKICTVDGHLTNETLKNLEGCEQIDGHLIIEHAFTYEQLKVLE
TVKIVSEYITIVQ
QNFYDLKFLKNLQIIEGRKLHNVRWALAIYQCDDLEELSLNSLKLIKTGAVLIMKNH
RLCYVSKIDWSSI
ITSKGKDNKPSLAIAENRDSKLCETEQRVCDKNCNKRGCWGKEPEDCLECKTWKS
VGTCVEKCDTKGFLR
NQTSMKCERCSPECETCNGLGELDCLTCRHKTLYNSDFGNRMECVHDCPVSHFPT
QKNVCEKCHPTCYDN
GCTGPDSNLGYGGCKQCKYAVKYENDTIFCLQSSGMNNVCVENDLPNYYISTYDTE
GVIETHCEKCSISC
KTCSSAGRNVVQNKCVCKHVEYQPNPSERICMDQCPVNSFMVPDTNNTVCKKCH
HECDQNYHCANGQSTG
CQKCKNFTVFKGDIAQCVSECPKNLPFSNPANGECLDYDIASRQRKTRMVIIGSVLF
GFAVMFLFILLVY
WRCQRIGKKLKIAEMVDMPELTPIDASVRPNMSRICLIPSSELQTKLDKKLGAGAFG
TVFAGIYYPKRAK
NVKIPVAIKVFQTDQSQTDEMLEEATNMFRLRHDNLLKIIGFCMHDDGLKIVTIYRP
LGNLQNFLKLHKE
NLGAREQVLYCYQIASGMQYLEKQRVVHRDLATRNVLVKKFNHVEITDFGLSKILK
HDADSITIKSGKVA
IKWLAIEIFSKHCYTHASDVWAFGVTCWEIITFGQSPYQGMSTDSIHNFLKDGNRLS
QPPNCSQDLYQEL
LRCWMADPKSRPGFEILYERFKEFCKVPQLFLENSNKISESDLSAEERFQTERIREM
FDGNIDPQMYFDQ
GSLPSMPSSPTSMATFTIPHGDLMNRMQSVNSSRYKTEPFDYGSTAQEDNSYLIPKT
KEVQQSAVLYTAV
TNEDGQTELSPSNGDYYNQPNTPSSSSGYYNEPHLKTKKPETSEEAEAVQYENEEV
SQKETCL
http://gtof.gsc.riken.jp/SP277/blast/bSp277.php 5sec
Query= gi|110825728|sp|P24348|LET23_CAEEL Receptor
tyrosine-protein kinase let-23 precursor (Lethal protein 23)
(1322 letters)
Database: sp277model.tfa
1,401,339 sequences; 311,159,872 total letters
Searching..................................................done
Score
E
Sequences producing significant alignments:
(bits) Value
CAA93882.3_1_1_1 cele0 870-1153 1e-83 42 ZK1067.1 wormpep11...
749
0.0
CAA93882.3_1_4_1 cele0 878-1158 2e-77 31 ZK1067.1 wormpep11...
739
0.0
CAA93882.3_1_3_1 cele0 878-1149 2e-77 34 ZK1067.1 wormpep11...
717
0.0
CAA93882.3_1_5_1 cele0 878-1144 2e-76 35 ZK1067.1 wormpep11...
702
0.0
CAA93882.3_1_2_1 cele0 878-1143 4e-79 30 ZK1067.1 wormpep11...
699
0.0
>CAA93882.3_1_1_1 cele0 870-1153 1e-83 42 ZK1067.1 wormpep113 "tyrosine-protein
kinase
(Epidermal growth factor.."
Length = 284
Score = 749 bits (1621), Expect = 0.0
Identities = 284/284 (100%), Positives = 284/284 (100%)
http://mammalia.gsc.riken.jp/human/search.php 15sec
Query= gi|110825728|sp|P24348|LET23_CAEEL Receptor
tyrosine-protein kinase let-23 precursor (Lethal protein 23)
(1322 letters)
Database: sp277model.tfa
1,401,339 sequences; 311,159,872 total letters
Searching..................................................done
Score
E
Sequences producing significant alignments:
(bits) Value
CAA93882.3_1_1_1 cele0 870-1153 1e-83 42 ZK1067.1 wormpep11...
749
0.0
CAA93882.3_1_4_1 cele0 878-1158 2e-77 31 ZK1067.1 wormpep11...
739
0.0
CAA93882.3_1_3_1 cele0 878-1149 2e-77 34 ZK1067.1 wormpep11...
717
0.0
CAA93882.3_1_5_1 cele0 878-1144 2e-76 35 ZK1067.1 wormpep11...
702
0.0
CAA93882.3_1_2_1 cele0 878-1143 4e-79 30 ZK1067.1 wormpep11...
699
0.0
>CAA93882.3_1_1_1 cele0 870-1153 1e-83 42 ZK1067.1 wormpep113 "tyrosine-protein
kinase
(Epidermal growth factor.."
Length = 284
Score = 749 bits (1621), Expect = 0.0
Identities = 284/284 (100%), Positives = 284/284 (100%)
> NP_001973.1 hsap2 ERBB3 v-erb-b2 erythroblastic leukemia viral oncogene homolog
3
Length = 1342
Score = 284 bits (727), Expect = 9e-76
Identities = 190/653 (29%), Positives = 286/653 (43%), Gaps = 98/653 (15%
==================================================================
Other nature genetics papers
nature genetics vol 38 nu 8 august 2006 p873
ATM mutations that cause ataxia-telangiectasia are breast cancer susceptibility alleles
8: Q13315 Reports
BLink, Conserved Domains, Links
Serine-protein kinase ATM (Ataxia telangiectasia mutated) (A-T, mutated)
gi|13878337|sp|Q13315|ATM_HUMAN[13878337]
1:
Q13315. Reports
Links
Serine-protein ki...[gi:13878337]
BLink, Conserved Domains,
CommentFeaturesSequenceLOCUS
linear
Q13315
3056 aa
PRI 25-JUL-2006
DEFINITION Serine-protein kinase ATM (Ataxia telangiectasia mutated) (A-T,
mutated).
ACCESSION
VERSION
DBSOURCE
Q13315
Q13315 GI:13878337
swissprot: locus ATM_HUMAN, accession Q13315;
class: standard.
extra
accessions:O15429,Q12758,Q16551,Q93007,Q9NP02,Q9UCX7,created:
Apr 27, 2001.
sequence updated: Nov 1, 1996.
annotation updated: Jul 25, 2006.
COMMENT
On Mar 15, 2005 this sequence version replaced gi:1082236.
[FUNCTION] Serine/threonine protein kinase which activates
checkpoint signaling upon double strand breaks (DSBs), apoptosis
and genotoxic stresses such as ionizing ultraviolet A light (UVA),
thereby acting as a DNA damage sensor. Recognizes the substrate
consensus sequence [S/T-Q]. Phosphorylates Ser-139 of histone
variant H2AX/H2AFX at double strand breaks (DSBs), thereby
regulating DNA damage response mechanism. Also involved in signal
transduction and cell cycle control. May function as a tumor
suppressor. Necessary for activation of ABL1 and SAPK.
Phosphorylates p53/TP53, FANCD2, NFKBIA, BRCA1, CTIP, nibrin
(NBN),
TERF1, RAD9 and DCLRE1C. May play a role in vesicle and/or protein
transport. Could play a role in T-cell development, gonad and
neurological function.
[CATALYTIC ACTIVITY] ATP + a protein = ADP + a phosphoprotein.
[ENZYME REGULATION] Inhibited by wortmannin.
[SUBUNIT] Exists in monomeric and tetrameric state. Binds DNA ends,
p53/TP53, ABL1, BRCA1, NBN/nibrin and TERF1. Part of the
BRCA1-associated genome surveillance complex (BASC), which contains
BRCA1,
MSH2,
MSH6,
MLH1,
ATM,
BLM,
PMS2
and
the
RAD50-MRE11-NBN
protein complex. This association could be a dynamic process
changing throughout the cell cycle and within subnuclear domains.
DNA damage promotes association with RAD17. Interacts with EEF1E1.
This interaction, which takes place independently of TP53, is
induced by DNA damage that may occur during genotoxic stress or
cell growth. Interacts with DCLRE1C. Interacts with MYST1.
Interacts with HTATIP.
[INTERACTION]
Q14676:MDC1;
NbExp=1;
IntAct=EBI-495465,
EBI-495453.
[SUBCELLULAR LOCATION] Nucleus. Cytoplasmic vesicle. Primarily
nuclear. Found also in endocytic vesicles in association with
beta-adaptin.
[TISSUE SPECIFICITY] Found in pancreas, kidney, skeletal muscle,
liver, lung, placenta, brain, heart, spleen, thymus, testis, ovary,
small intestine, colon and leukocytes.
[INDUCTION] By ionizing radiation.
[DOMAIN] The FATC domain is required for interaction with HTATIP.
[PTM] Phosphorylated by ARK5. Autophosphorylated on Ser-1981 upon
DNA damage.
[PTM] Acetylated by HTATIP upon DNA damage; which is required for
autophosphorylation and subsequent activation.
[DISEASE] Defects in ATM are the cause of ataxia talangiectasia
(AT) [MIM:208900]; also known as Louis-Bar syndrome, which includes
four complementation groups: A, C, D and E. This rare recessive
disorder is characterized by progressive cerebellar ataxia,
dilation of the blood vessels in the conjunctiva and eyeballs,
immunodeficiency, growth retardation and sexual immaturity. AT
patients have a strong predisposition to cancer; about 30% of
patients develop tumors, particularly lymphomas and leukemias.
Cells from affected individuals are highly sensitive to damage by
ionizing radiation and resistant to inhibition of DNA synthesis
following irradiation.
[DISEASE] Defects in ATM contribute to T-cell acute lymphoblastic
leukemia (TALL) and T-prolymphocytic leukemia (TPLL). TPLL is
characterized by a high white blood cell count, with a predominance
of prolymphocytes, marked splenomegaly, lymphadenopathy, skin
lesions and serous effusion. The clinical course is highly
aggressive, with poor response to chemotherapy and short survival
time. TPLL occurs both in adults as a sporadic disease and in
younger AT patients.
[DISEASE] Defects in ATM contribute to B-cell non-Hodgkin lymphomas
(BNHL), including mantle cell lymphoma (MCL).
[DISEASE] Defects in ATM contribute to B-cell chronic lymphocytic
leukemia (BCLL). BCLL is the commonest form of leukemia in the
elderly. It is characterized by the accumulation of mature CD5+ B
lymphocytes, lymphadenopathy, immunodeficiency and bone marrow
failure.
[SIMILARITY] Belongs to the PI3/PI4-kinase family. ATM subfamily.
[SIMILARITY] Contains 1 FAT domain.
[SIMILARITY] Contains 1 FATC domain.
[SIMILARITY] Contains 1 PI3K/PI4K domain.
WEB RESOURCE: NAME=Ataxia talangiectasia mutation db;
URL='http://benaroyaresearch.org/investigators/concannon_patrick/at
m.htm'.
WEB RESOURCE: NAME=Atlas Genet. Cytogenet. Oncol. Haematol.;
URL='http://www.infobiogen.fr/services/chromcancer/Genes/ATM123.htm
l'.
WEB RESOURCE: NAME=GeneReviews;
URL='http://www.genetests.org/query?gene=ATM'.
FEATURES
source
Location/Qualifiers
1..3056
/organism="Homo sapiens"
/db_xref="taxon:9606"
gene
1..3056
/gene="ATM"
Protein
1..3056
/gene="ATM"
/product="Serine-protein kinase ATM"
/EC_number="2.7.11.
1:
Q13315. Reports
Links
Serine-protein ki...[gi:13878337]
BLink, Conserved Domains,
>gi|13878337|sp|Q13315|ATM_HUMAN
Serine-protein
kinase
ATM
(Ataxia
telangiectasia mutated) (A-T, mutated)
MSLVLNDLLICCRQLEHDRATERKKEVEKFKRLIRDPETIKHLDRHSDSKQGKYLN
WDAVFRFLQKYIQK
ETECLRIAKPNVSASTQASRQKKMQEISSLVKYFIKCANRRAPRLKCQELLNYIMDT
VKDSSNGAIYGAD
CSNILLKDILSVRKYWCEISQQQWLELFSVYFRLYLKPSQDVHRVLVARIIHAVTKGC
CSQTDGLNSKFL
DFFSKAIQCARQEKSSSGLNHILAALTIFLKTLAVNFRIRVCELGDEILPTLLYIWTQH
RLNDSLKEVII
ELFQLQIYIHHPKGAKTQEKGAYESTKWRSILYNLYDLLVNEISHIGSRGKYSSGFRN
IAVKENLIELMA
DICHQVFNEDTRSLEISQSYTTTQRESSDYSVPCKRKKIELGWEVIKDHLQKSQNDF
DLVPWLQIATQLI
SKYPASLPNCELSPLLMILSQLLPQQRHGERTPYVLRCLTEVALCQDKRSNLESSQK
SDLLKLWNKIWCI
TFRGISSEQIQAENFGLLGAIIQGSLVEVDREFWKLFTGSACRPSCPAVCCLTLALTTS
IVPGAVKMGIE
QNMCEVNRSFSLKESIMKWLLFYQLEGDLENSTEVPPILHSNFPHLVLEKILVSLTM
KNCKAAMNFFQSV
PECEHHQKDKEELSFSEVEELFLQTTFDKMDFLTIVRECGIEKHQSSIGFSVHQNLK
ESLDRCLLGLSEQ
LLNNYSSEITNSETLVRCSRLLVGVLGCYCYMGVIAEEEAYKSELFQKANSLMQCAG
ESITLFKNKTNEE
FRIGSLRNMMQLCTRCLSNCTKKSPNKIASGFFLRLLTSKLMNDIADICKSLASFIKK
PFDRGEVESMED
DTNGNLMEVEDQSSMNLFNDYPDSSVSDANEPGESQSTIGAINPLAEEYLSKQDLL
FLDMLKFLCLCVTT
AQTNTVSFRAADIRRKLLMLIDSSTLEPTKSLHLHMYLMLLKELPGEEYPLPMEDV
LELLKPLSNVCSLY
RRDQDVCKTILNHVLHVVKNLGQSNMDSENTRDAQGQFLTVIGAFWHLTKERKYI
FSVRMALVNCLKTLL
EADPYSKWAILNVMGKDFPVNEVFTQFLADNHHQVRMLAAESINRLFQDTKGDSS
RLLKALPLKLQQTAF
ENAYLKAQEGMREMSHSAENPETLDEIYNRKSVLLTLIAVVLSCSPICEKQALFALC
KSVKENGLEPHLV
KKVLEKVSETFGYRRLEDFMASHLDYLVLEWLNLQDTEYNLSSFPFILLNYTNIEDF
YRSCYKVLIPHLV
IRSHFDEVKSIANQIQEDWKSLLTDCFPKILVNILPYFAYEGTRDSGMAQQRETATKV
YDMLKSENLLGK
QIDHLFISNLPEIVVELLMTLHEPANSSASQSTDLCDFSGDLDPAPNPPHFPSHVIKA
TFAYISNCHKTK
LKSILEILSKSPDSYQKILLAICEQAAETNNVYKKHRILKIYHLFVSLLLKDIKSGLGG
AWAFVLRDVIY
TLIHYINQRPSCIMDVSLRSFSLCCDLLSQVCQTAVTYCKDALENHLHVIVGTLIPLV
YEQVEVQKQVLD
LLKYLVIDNKDNENLYITIKLLDPFPDHVVFKDLRITQQKIKYSRGPFSLLEEINHFL
SVSVYDALPLTR
LEGLKDLRRQLELHKDQMVDIMRASQDNPQDGIMVKLVVNLLQLSKMAINHTGEK
EVLEAVGSCLGEVGP
IDFSTIAIQHSKDASYTKALKLFEDKELQWTFIMLTYLNNTLVEDCVKVRSAAVTCL
KNILATKTGHSFW
EIYKMTTDPMLAYLQPFRTSRKKFLEVPRFDKENPFEGLDDINLWIPLSENHDIWIK
TLTCAFLDSGGTK
CEILQLLKPMCEVKTDFCQTVLPYLIHDILLQDTNESWRNLLSTHVQGFFTSCLRHF
SQTSRSTTPANLD
SESEHFFRCCLDKKSQRTMLAVVDYMRRQKRPSSGTIFNDAFWLDLNYLEVAKVAQ
SCAAHFTALLYAEI
YADKKSMDDQEKRSLAFEEGSQSTTISSLSEKSKEETGISLQDLLLEIYRSIGEPDSL
YGCGGGKMLQPI
TRLRTYEHEAMWGKALVTYDLETAIPSSTRQAGIIQALQNLGLCHILSVYLKGLDYE
NKDWCPELEELHY
QAAWRNMQWDHCTSVSKEVEGTSYHESLYNALQSLRDREFSTFYESLKYARVKEV
EEMCKRSLESVYSLY
PTLSRLQAIGELESIGELFSRSVTHRQLSEVYIKWQKHSQLLKDSDFSFQEPIMALRT
VILEILMEKEMD
NSQRECIKDILTKHLVELSILARTFKNTQLPERAIFQIKQYNSVSCGVSEWQLEEAQV
FWAKKEQSLALS
ILKQMIKKLDASCAANNPSLKLTYTECLRVCGNWLAETCLENPAVIMQTYLEKAVEV
AGNYDGESSDELR
NGKMKAFLSLARFSDTQYQRIENYMKSSEFENKQALLKRAKEEVGLLREHKIQTNR
YTVKVQRELELDEL
ALRALKEDRKRFLCKAVENYINCLLSGEEHDMWVFRLCSLWLENSGVSEVNGMMK
RDGMKIPTYKFLPLM
YQLAARMGTKMMGGLGFHEVLNNLISRISMDHPHHTLFIILALANANRDEFLTKPE
VARRSRITKNVPKQ
SSQLDEDRTEAANRIICTIRSRRPQMVRSVEALCDAYIILANLDATQWKTQRKGINIP
ADQPITKLKNLE
DVVVPTMEIKVDHTGEYGNLVTIQSFKAEFRLAGGVNLPKIIDCVGSDGKERRQLVK
GRDDLRQDAVMQQ
VFQMCNTLLQRNTETRKRKLTICTYKVVPLSQRSGVLEWCTGTVPIGEFLVNNEDG
AHKRYRPNDFSAFQ
CQKKMMEVQKKSFEEKYEVFMDVCQNFQPVFRYFCMEKFLDPAIWFEKRLAYTRS
VATSSIVGYILGLGD
RHVQNILINEQSAELVHIDLGVAFEQGKILPTPETVPFRLTRDIVDGMGITGVEGVFR
RCCEKTMEVMRN
SQETLLTIVEVLLYDPLFDWTMNPLKALYLQQRPEDETELHPTLNADDQECKRNLS
DIDQSFDKVAERVL
MRLQEKLKGVEEGTVLSVGGQVNLLIQQAIDPKNLSRLFPGWKAWV
nature genetics vol 38 nu 8 august 2006 p910
Mutations in genes encoding ribonuclease H2 subunits cause Aicrdi-Goutieres
syndrome aand mimic congenital viral brain infection
gout 痛風 プリン代謝異常
5: Q2TBT5 Reports
Aicrdi 神経科医の名前
BLink, Conserved Domains, Links
Ribonuclease HI large subunit (RNase HI large subunit) (Ribonuclease H2) (RNase H2)
gi|110816412|sp|Q2TBT5|RNHL_BOVIN[110816412]
1: Q2TBT5. Reports Ribonuclease HI l...[gi:110816412] BLink, Conserved Domains,
Links
>gi|110816412|sp|Q2TBT5|RNHL_BOVIN Ribonuclease HI large subunit (RNase HI
large subunit) (Ribonuclease H2) (RNase H2)
MDLSELERDNTGRCRLSSPVPPVCLKEPCVLGVDEAGRGPVLGPMVYAICYCPLSR
LEDLEALKVADSKT
LSESERDRLFAKMEEDGDFVGWALDVLSPNLISTSMLGRVKYNLNALSHDTATGLV
QFALDQGVNVAQVF
VDTVGLPETYQERLQQRFPGIEVTVKAKADALYPVVSAASICAKVARDQAVKNWKF
VEKLQDLDTDYGSG
YPNDPKTKAWLRKHVDPVFGFPQFVRFSWRTAQSILESEAEDVKWEDSETGDPKG
PGKIKSYFSESPQTC
LRLPHRYFQERGLESATVL
6: Q5U209 Reports
BLink, Conserved Domains, Links
Ribonuclease HI large subunit (RNase HI large subunit) (Ribonuclease H2) (RNase H2)
gi|81889649|sp|Q5U209|RNHL_RAT[81889649]
1: Q5U209. Reports Ribonuclease HI l...[gi:81889649] BLink, Conserved Domains,
Links
>gi|81889649|sp|Q5U209|RNHL_RAT Ribonuclease HI large subunit (RNase HI
large subunit) (Ribonuclease H2) (RNase H2)
MDLSELERDNTGRCRLSSPVPAVCLKEPCVLGVDEAGRGPVLGPMVYAICYCPLSRL
ADLEALKVADSKT
LTENERERLFAKMEEDGDFVGWALDILSPNLISTSMLGRVKYNLNSMSHDTAAGLI
QHAMDQNVKVTQVF
VDTVGMPETYQARLQQRFPGIEVTVKAKADSLFPVVSAASIIAKVARDQAVKNWQFV
ESLQGLDSDYGSG
YPNDPKTKAWLRKHVDPVFGFPQFVRFSWSTAQAILEKEAESVTWEDSAAEEDPEG
PGRITSYFSQGPQA
CRPQVSHKYFQERGLETATSL
http://mammalia.gsc.riken.jp/human/search.php 3sec
http://mammalia.gsc.riken.jp/eukaryote/
7: O75792 Reports
BLink, Conserved Domains, Links
Ribonuclease HI large subunit (RNase HI large subunit) (Ribonuclease H2) (RNase H2)
(RNase H(35))
gi|20981704|sp|O75792|RNHL_HUMAN[20981704]
1: O75792. Reports Ribonuclease HI l...[gi:20981704] BLink, Conserved Domains,
Links
>gi|20981704|sp|O75792|RNHL_HUMAN Ribonuclease HI large subunit (RNase HI
large subunit) (Ribonuclease H2) (RNase H2) (RNase H(35))
MDLSELERDNTGRCRLSSPVPAVCRKEPCVLGVDEAGRGPVLGPMVYAICYCPLPRL
ADLEALKVADSKT
LLESERERLFAKMEDTDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTATGLIQY
ALDQGVNVTQVFV
DTVGMPETYQARLQQSFPGIEVTVKAKADALYPVVSAASICAKVARDQAVKKWQFV
EKLQDLDTDYGSGY
PNDPKTKAWLKEHVEPVFGFPQFVRFSWRTAQTILEKEAEDVIWEDSASENQEGLR
KITSYFLNEGSQAR
PRSSHRYFLERGLESATSL
8: Q9CWY8 Reports
BLink, Conserved Domains, Links
Ribonuclease HI large subunit (RNase HI large subunit) (Ribonuclease H2) (RNase H2)
gi|85541053|sp|Q9CWY8|RNHL_MOUSE[85541053]
1: Q9CWY8. Reports Ribonuclease HI l...[gi:85541053] BLink, Conserved Domains,
Links
>gi|85541053|sp|Q9CWY8|RNHL_MOUSE Ribonuclease HI large subunit (RNase HI
large subunit) (Ribonuclease H2) (RNase H2)
MDLSELERDNTGRCRLSSPVPAVCLKEPCVLGVDEAGRGPVLGPMVYAICYCPLSRL
ADLEALKVADSKT
LTENERERLFAKMEEDGDFVGWALDVLSPNLISTSMLGRVKYNLNSLSHDTAAGLI
QYALDQNVNVTQVF
VDTVGMPETYQARLQQHFPGIEVTVKAKADSLFPVVSAASIFAKVARDKAVKNWQF
VENLQDLDSDYGSG
YPNDPKTKAWLRKHVDPVFGFPQFVRFSWSTAQAILEKEAEDVIWEDSEAEEDPER
PGKITSYFSQGPQT
CRPQAPHRYFQERGLEAASSL
nature genetics vol 38 nu 8 august 2006 p917
Mutations in the gene encoding the 3'-5' DNA exonuclease TREX1 cause
Aicrdi-Goutieres syndrome at the AGS1 locus
7: Q9NSU2 Reports
BLink, Conserved Domains, Links
Three prime repair exonuclease 1 (3'-5' exonuclease TREX1) (DNase III)
gi|47606216|sp|Q9NSU2|TREX1_HUMAN[47606216]
1: Q9NSU2. Reports Three prime repai...[gi:47606216] BLink, Conserved Domains,
Links
CommentFeaturesSequenceLOCUS
linear
Q9NSU2
369 aa
PRI 13-JUN-2006
DEFINITION Three prime repair exonuclease 1 (3'-5' exonuclease TREX1) (DNase
III).
ACCESSION
VERSION
DBSOURCE
Q9NSU2
Q9NSU2 GI:47606216
swissprot: locus TREX1_HUMAN, accession Q9NSU2;
class: standard.
extra accessions:Q8TEU2,Q9BPW1,Q9Y4X2,created: May 24, 2004.
sequence updated: Oct 1, 2000.
annotation updated: Jun 13, 2006.
FEATURES
source
Location/Qualifiers
1..369
/organism="Homo sapiens"
/db_xref="taxon:9606"
gene
1..369
/gene="TREX1"
Protein
1..369
/gene="TREX1"
/product="Three prime repair exonuclease 1"
/EC_number="3.1.11.2"
Region
1..369
/gene="TREX1"
1: Q9NSU2. Reports Three prime repai...[gi:47606216] BLink, Conserved Domains,
Links
>gi|47606216|sp|Q9NSU2|TREX1_HUMAN Three prime repair exonuclease 1 (3'-5'
exonuclease TREX1) (DNase III)
MGPGARRQGRIVQGRPEMCFCPPPTPLPPLRILTLGTHTPTPCSSPGSAAGTYPTMG
SQALPPGPMQTLI
FFDMEATGLPFSQPKVTELCLLAVHRCALESPPTSQGPPPTVPPPPRVVDKLSLCVA
PGKACSPAASEIT
GLSTAVLAAHGRQCFDDNLANLLLAFLRRQPQPWCLVAHNGDRYDFPLLQAELAML
GLTSALDGAFCVDS
ITALKALERASSPSEHGPRKSYSLGSIYTRLYGQSPPDSHTAEGDVLALLSICQWRPQ
ALLRWVDAHARP
FGTIRPMYGVTASARTKPRPSAVTTTAHLATTRNTSPSLGESRGTKDLPPVKDPGALS
REGLLAPLGLLA
ILTLAVATLYGLSLATPGE
http://mammalia.gsc.riken.jp/human/
http://mammalia.gsc.riken.jp/human/search.php 4sec
> HIT000026033.1 hsap1 HIX0003286.1.5
Length = 369
Score = 560 bits (1442), Expect = e-159
Identities = 368/368 (100%), Positives = 368/368 (100%)
8: Q91XB0 Reports
BLink, Conserved Domains, Links
Three prime repair exonuclease 1 (3'-5' exonuclease TREX1)
gi|47606196|sp|Q91XB0|TREX1_MOUSE[47606196]
1: Q91XB0. Reports Three prime repai...[gi:47606196] BLink, Conserved Domains,
Links
CommentFeaturesSequenceLOCUS
linear
Q91XB0
314 aa
ROD 13-JUN-2006
DEFINITION Three prime repair exonuclease 1 (3'-5' exonuclease TREX1).
ACCESSION
VERSION
DBSOURCE
Q91XB0
Q91XB0 GI:47606196
swissprot: locus TREX1_MOUSE, accession Q91XB0;
class: standard.
extra accessions:Q3TAD7,Q9D6W2,Q9R1B0,created: May 24, 2004.
sequence updated: May 24, 2004.
annotation updated: Jun 13, 2006.
FEATURES
source
Location/Qualifiers
1..314
/organism="Mus musculus"
/db_xref="taxon:10090"
gene
1..314
/gene="Trex1"
Protein
1..314
/gene="Trex1"
/product="Three prime repair exonuclease 1"
/EC_number="3.1.11.2"
Region
1..314
/gene="Trex1"
1: Q91XB0. Reports Three prime repai...[gi:47606196] BLink, Conserved Domains,
Links
>gi|47606196|sp|Q91XB0|TREX1_MOUSE Three prime repair exonuclease 1 (3'-5'
exonuclease TREX1)
MGSQTLPHGHMQTLIFLDLEATGLPSSRPEVTELCLLAVHRRALENTSISQGHPPPV
PRPPRVVDKLSLC
IAPGKACSPGASEITGLSKAELEVQGRQRFDDNLAILLRAFLQRQPQPCCLVAHNGD
RYDFPLLQTELAR
LSTPSPLDGTFCVDSIAALKALEQASSPSGNGSRKSYSLGSIYTRLYWQAPTDSHTAE
GDVLTLLSICQW
KPQALLQWVDEHARPFSTVKPMYGTPATTGTTNLRPHAATATTPLATANGSPSNGR
SRRPKSPPPEKVPE
APSQEGLLAPLSLLTLLTLAIATLYGLFLASPGQ
10: Q9BG99 Reports
BLink, Conserved Domains, Links
Three prime repair exonuclease 1 (3'-5' exonuclease TREX1)
gi|47606205|sp|Q9BG99|TREX1_BOVIN[47606205]
1: Q9BG99. Reports Three prime repai...[gi:47606205] BLink, Conserved Domains,
Links
CommentFeaturesSequenceLOCUS
linear
Q9BG99
315 aa
MAM 27-JUN-2006
DEFINITION Three prime repair exonuclease 1 (3'-5' exonuclease TREX1).
ACCESSION
VERSION
DBSOURCE
Q9BG99
Q9BG99 GI:47606205
swissprot: locus TREX1_BOVIN, accession Q9BG99;
class: standard.
created: May 24, 2004.
sequence updated: Jun 1, 2001.
annotation updated: Jun 27, 2006.
FEATURES
source
Location/Qualifiers
1..315
/organism="Bos taurus"
/db_xref="taxon:9913"
gene
1..315
/gene="TREX1"
Protein
1..315
/gene="TREX1"
1: Q9BG99. Reports Three prime repai...[gi:47606205] BLink, Conserved Domains,
Links
>gi|47606205|sp|Q9BG99|TREX1_BOVIN Three prime repair exonuclease 1 (3'-5'
exonuclease TREX1)
MGSRALPPGPVQTLIFLDLEATGLPFSQPKITELCLLAVHRYALEGLSAPQGPSPTAP
VPPRVLDKLSLC
VAPGKVCSPAASEITGLSTAVLAAHGRRAFDADLVNLIRTFLQRQPQPWCLVAHNGD
RYDFPLLRAELAL
LGLASALDDAFCVDSIAALKALEPTGSSSEHGPRKSYSLGSVYTRLYGQAPPDSHTA
EGDVLALLSVCQW
RPRALLRWVDAHAKPFSTVKPMYVITTSTGTNPRPSAVTATVPLARASDTGPNLRGD
RSPKPAPSPKMCP
GAPPGEGLLAPLGLLAFLTLAVAMLYGLSLAMPGQ
38: Q9BQ50 Reports
BLink, Conserved Domains, Links
Three prime repair exonuclease 2 (3'-5' exonuclease TREX2)
gi|47606206|sp|Q9BQ50|TREX2_HUMAN[47606206]
1: Q9BQ50. Reports Three prime repai...[gi:47606206] BLink, Conserved Domains,
Links
CommentFeaturesSequenceLOCUS
linear
Q9BQ50
279 aa
PRI 27-JUN-2006
DEFINITION Three prime repair exonuclease 2 (3'-5' exonuclease TREX2).
ACCESSION
VERSION
DBSOURCE
Q9BQ50
Q9BQ50 GI:47606206
swissprot: locus TREX2_HUMAN, accession Q9BQ50;
FEATURES
source
Location/Qualifiers
1..279
/organism="Homo sapiens"
/db_xref="taxon:9606"
gene
1..279
/gene="TREX2"
Protein
1..279
/gene="TREX2"
/product="Three prime repair exonuclease 2"
/EC_number="3.1.11.2"
Region
1..279
/gene="TREX2"
1: Q9BQ50. Reports Three prime repai...[gi:47606206] BLink, Conserved Domains,
Links
>gi|47606206|sp|Q9BQ50|TREX2_HUMAN Three prime repair exonuclease 2 (3'-5'
exonuclease TREX2)
MGRAGSPLPRSSWPRMDDCGSRSRCSPTLCSSLRTCYPRGNITMSEAPRAETFVFL
DLEATGLPSVEPEI
AELSLFAVHRSSLENPEHDESGALVLPRVLDKLTLCMCPERPFTAKASEITGLSSEGL
ARCRKAGFDGAV
VRTLQAFLSRQAGPICLVAHNGFDYDFPLLCAELRRLGARLPRDTVCLDTLPALRGL
DRAHSHGTRARGR
QGYSLGSLFHRYFRAEPSAAHSAEGDVHTLLLIFLHRAAELLAWADEQARGWAHIE
PMYLPPDDPSLEA
nature genetics vol 38 nu 8 august 2006 p921
A functional SNP in PSMA6 confers risk of myocardial infarction in the Japanes
population
myocardial 心筋の
14: P60900 Reports
infarction 梗塞形成
confer 与える、授ける
BLink, Conserved Domains, Links
Proteasome subunit alpha type 6 (Proteasome iota chain) (Macropain iota chain)
(Multicatalytic endopeptidase complex iota chain) (27 kDa prosomal protein) (PROS-27)
(p27K)
gi|46397659|sp|P60900|PSA6_HUMAN[46397659]
1: P60900. Reports Proteasome subuni...[gi:46397659] BLink, Conserved Domains,
Links
CommentFeaturesSequenceLOCUS
P60900
246 aa
linear
PRI 13-JUN-2006
DEFINITION Proteasome subunit alpha type 6 (Proteasome iota chain) (Macropain
iota chain) (Multicatalytic endopeptidase complex iota chain) (27
kDa prosomal protein) (PROS-27) (p27K).
ACCESSION
VERSION
DBSOURCE
P60900
P60900 GI:46397659
swissprot: locus PSA6_HUMAN, accession P60900;
class: standard.
extra accessions:P34062,Q6IB60,created: Apr 13, 2004.
sequence updated: Apr 13, 2004.
annotation updated: Jun 13, 2006.
[SIMILARITY] Belongs to the peptidase T1A family.
COMMENT
On Mar 15, 2005 this sequence version replaced gi:418785.
[FUNCTION] The proteasome is a multicatalytic proteinase complex
which is characterized by its ability to cleave peptides with Arg,
Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or
slightly basic pH. The proteasome has an ATP-dependent proteolytic
activity.
[CATALYTIC ACTIVITY] Cleavage of peptide bonds with very broad
specificity.
[PATHWAY] Involved in an ATP/ubiquitin-dependent non-lysosomal
proteolytic pathway.
[SUBUNIT] The proteasome is composed of at least 15 non identical
subunits which form a highly ordered ring-shaped structure.
[INTERACTION]
P25788:PSMA3;
NbExp=1;
EBI-348380.
[SUBCELLULAR LOCATION] Cytoplasm. Nucleus.
[SIMILARITY] Belongs to the peptidase T1A family.
FEATURES
source
Location/Qualifiers
1..246
/organism="Homo sapiens"
/db_xref="taxon:9606"
gene
1..246
/gene="PSMA6"
IntAct=EBI-357793,
/note="synonym: PROS27"
Protein
1..246
/gene="PSMA6"
/product="Proteasome subunit alpha type 6"
/EC_number="3.4.25.1"
Region
1..246
/gene="PSMA6"
1: P60900. Reports Proteasome subuni...[gi:46397659] BLink, Conserved Domains,
Links
>gi|46397659|sp|P60900|PSA6_HUMAN
Proteasome
subunit
alpha
type
6
(Proteasome iota chain) (Macropain iota chain) (Multicatalytic endopeptidase complex
iota chain) (27 kDa prosomal protein) (PROS-27) (p27K)
MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPD
KLLDSSTVTHLF
KITENIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYT
QNAEMRPLGCCMIL
IGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVE
TAITCLSTVLSIDF
KPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD
Query= gi|46397659|sp|P60900|PSA6_HUMAN Proteasome subunit
alpha type 6 (Proteasome iota chain) (Macropain iota chain)
(Multicatalytic endopeptidase complex iota chain) (27 kDa prosomal
protein) (PROS-27) (p27K)
(245 letters)
Database: /ntc3/human_famsbase/20050902/SEQs/human
102,470 sequences; 47,066,789 total letters
Searching..................................................done
Score
Sequences producing significant alignments:
ENSP00000261479 hsap0 ENSG00000100902 transcript_id
e-140
E
(bits) Value
494
HIT000039494.1 hsap1 HIX0011598.1.2
494
e-140
HIT000038178.1 hsap1 HIX0011598.1.1
494
e-140
HIT000031331.1 hsap1 HIX0011598.1.3
494
e-140
NP_002782.1 hsap2 PSMA6 proteasome alpha 6 subunit
e-140
> ENSP00000261479 hsap0 ENSG00000100902 transcript_id
Length = 246
Score = 494 bits (1272), Expect = e-140
Identities = 245/245 (100%), Positives = 245/245 (100%)
494
15: Q9QUM9 Reports
BLink, Conserved Domains, Links
Proteasome subunit alpha type 6 (Proteasome iota chain) (Macropain iota chain)
(Multicatalytic endopeptidase complex iota chain)
gi|9910829|sp|Q9QUM9|PSA6_MOUSE[9910829]
1: Q9QUM9. Reports Proteasome subuni...[gi:9910829] BLink, Conserved Domains,
Links
CommentFeaturesSequenceLOCUS
linear
Q9QUM9
246 aa
ROD 13-JUN-2006
DEFINITION Proteasome subunit alpha type 6 (Proteasome iota chain) (Macropain
iota chain) (Multicatalytic endopeptidase complex iota chain).
ACCESSION
VERSION
DBSOURCE
Q9QUM9
Q9QUM9 GI:9910829
swissprot: locus PSA6_MOUSE, accession Q9QUM9;
class: standard.
extra accessions:Q3U6Y2,created: Dec 1, 2000.
sequence updated: May 1, 2000.
annotation updated: Jun 13, 2006.
FEATURES
source
Location/Qualifiers
1..246
/organism="Mus musculus"
/db_xref="taxon:10090"
gene
1..246
/gene="Psma6"
Protein
1..246
/gene="Psma6"
/product="Proteasome subunit alpha type 6"
/EC_number="3.4.25.1"
Region
1..246
/gene="Psma6"
1: Q9QUM9. Reports Proteasome subuni...[gi:9910829] BLink, Conserved Domains,
Links
>gi|9910829|sp|Q9QUM9|PSA6_MOUSE
Proteasome
subunit
alpha
type
6
(Proteasome iota chain) (Macropain iota chain) (Multicatalytic endopeptidase complex
iota chain)
MSRGSSAGFDRHITIFSPEGRLYQVEYAFKAINQGGLTSVAVRGKDCAVIVTQKKVPD
KLLDSSTVTHLF
KITESIGCVMTGMTADSRSQVQRARYEAANWKYKYGYEIPVDMLCKRIADISQVYT
QNAEMRPLGCCMIL
IGIDEEQGPQVYKCDPAGYYCGFKATAAGVKQTESTSFLEKKVKKKFDWTFEQTVE
TAITCLSTVLSIDF
KPSEIEVGVVTVENPKFRILTEAEIDAHLVALAERD
nature genetics vol 38 nu 8 august 2006 p926
A functional switch from lung cancer resistance to susceptibility at the Pas1 locus in
Kras2LA2 mice
Pulmonary adenoma susceptibility 1(Pas1) mouse
Kras2 is a common target of somatic mutation in chemically induced mouse lung tumors
3: P32883 Reports
BLink, Conserved Domains, Links
GTPase KRas (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras)
gi|417590|sp|P32883|RASK_MOUSE[417590]
1: P32883. Reports GTPase KRas (K-Ra...[gi:417590] BLink, Conserved Domains,
Links
CommentFeaturesSequenceLOCUS
linear
P32883
189 aa
ROD 27-JUN-2006
DEFINITION GTPase KRas (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras).
ACCESSION
VERSION
DBSOURCE
P32883
P32883 GI:417590
swissprot: locus RASK_MOUSE, accession P32883;
class: standard.
extra accessions:P04200,P08643,created: Mar 20, 1987.
sequence updated: Aug 13, 1987.
annotation updated: Jun 27, 2006.
xrefs: X02452.1, CAA26295.1, X02453.1, X02454.1, X02456.1,
X02455.1, CAA26296.1, BC004642.1, AAH04642.1, BC010202.1,
AAH10202.1, K01927.1, AAA40037.1, X00485.1, CAA25160.1, TVMSK,
TVMS2K
FEATURES
source
Location/Qualifiers
1..189
/organism="Mus musculus"
/db_xref="taxon:10090"
gene
1..189
/gene="Kras"
/note="synonym: Kras2"
Protein
1..189
/gene="Kras"
/product="GTPase KRas"
Region
1..189
/gene="Kras"
1: P32883. Reports GTPase KRas (K-Ra...[gi:417590] BLink, Conserved Domains,
Links
>gi|417590|sp|P32883|RASK_MOUSE GTPase KRas (K-Ras 2) (Ki-Ras) (c-K-ras)
(c-Ki-ras)
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILD
TAGQEEYSAMRDQ
YMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVD
TKQAQELARSYGIP
FIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCVIM