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G3V8Q9

- G3V8Q9_RAT

UniProt

G3V8Q9 - G3V8Q9_RAT

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Protein
Submitted name:

Adenomatosis polyposis coli, isoform CRA_a

Gene

Apc

Organism
Rattus norvegicus (Rat)
Status
Unreviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. protein kinase regulator activity Source: Ensembl

GO - Biological processi

  1. anterior/posterior pattern specification Source: Ensembl
  2. axis specification Source: Ensembl
  3. axonogenesis Source: Ensembl
  4. canonical Wnt signaling pathway involved in negative regulation of apoptotic process Source: Ensembl
  5. canonical Wnt signaling pathway involved in positive regulation of apoptotic process Source: Ensembl
  6. cell cycle arrest Source: InterPro
  7. cell migration Source: Ensembl
  8. cellular response to DNA damage stimulus Source: InterPro
  9. chromosome organization Source: Ensembl
  10. cytoplasmic microtubule organization Source: Ensembl
  11. dorsal/ventral pattern formation Source: Ensembl
  12. hair follicle development Source: Ensembl
  13. kidney development Source: Ensembl
  14. metaphase/anaphase transition of mitotic cell cycle Source: Ensembl
  15. mitotic cytokinesis Source: Ensembl
  16. mitotic spindle assembly checkpoint Source: Ensembl
  17. muscle cell cellular homeostasis Source: Ensembl
  18. negative regulation of canonical Wnt signaling pathway Source: Ensembl
  19. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: Ensembl
  20. negative regulation of epithelial cell proliferation involved in prostate gland development Source: Ensembl
  21. negative regulation of MAPK cascade Source: Ensembl
  22. negative regulation of microtubule depolymerization Source: Ensembl
  23. negative regulation of odontogenesis Source: Ensembl
  24. positive regulation of cell adhesion Source: Ensembl
  25. positive regulation of cell division Source: Ensembl
  26. positive regulation of cell migration Source: Ensembl
  27. positive regulation of epithelial cell differentiation Source: Ensembl
  28. positive regulation of microtubule polymerization Source: Ensembl
  29. positive regulation of protein catabolic process Source: Ensembl
  30. positive regulation of pseudopodium assembly Source: Ensembl
  31. protein complex assembly Source: Ensembl
  32. proximal/distal pattern formation Source: Ensembl
  33. regulation of attachment of spindle microtubules to kinetochore Source: Ensembl
  34. regulation of nitrogen compound metabolic process Source: Ensembl
  35. regulation of osteoblast differentiation Source: Ensembl
  36. regulation of osteoclast differentiation Source: Ensembl
  37. retina development in camera-type eye Source: Ensembl
  38. somatic stem cell maintenance Source: Ensembl
  39. T cell differentiation in thymus Source: Ensembl
  40. thymus development Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_214025. deactivation of the beta-catenin transactivating complex.
REACT_216976. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_232045. truncations of AMER1 destabilize the destruction complex.
REACT_234350. Beta-catenin phosphorylation cascade.
REACT_237110. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_238778. Apoptotic cleavage of cellular proteins.
REACT_242544. T41 mutants of beta-catenin aren't phosphorylated.
REACT_245397. APC truncation mutants are not K63 polyubiquitinated.
REACT_248040. S37 mutants of beta-catenin aren't phosphorylated.
REACT_249104. APC truncation mutants have impaired AXIN binding.
REACT_250136. S33 mutants of beta-catenin aren't phosphorylated.
REACT_251328. S45 mutants of beta-catenin aren't phosphorylated.
REACT_257365. Degradation of beta-catenin by the destruction complex.
REACT_260559. AXIN missense mutants destabilize the destruction complex.

Names & Taxonomyi

Protein namesi
Submitted name:
Adenomatosis polyposis coli, isoform CRA_aImported
Submitted name:
Adenomatous polyposis coli proteinImported
Gene namesi
Name:ApcImported
ORF Names:rCG_49353Imported
OrganismiRattus norvegicus (Rat)Imported
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 18

Organism-specific databases

RGDi2123. Apc.

Subcellular locationi

GO - Cellular componenti

  1. axonal growth cone Source: Ensembl
  2. beta-catenin destruction complex Source: Ensembl
  3. cell-cell adherens junction Source: Ensembl
  4. centrosome Source: Ensembl
  5. cytoplasmic microtubule Source: Ensembl
  6. kinetochore Source: Ensembl
  7. lamellipodium Source: Ensembl
  8. lateral plasma membrane Source: Ensembl
  9. microtubule plus-end Source: Ensembl
  10. nucleus Source: Ensembl
  11. ruffle membrane Source: Ensembl
  12. tight junction Source: Ensembl
Complete GO annotation...

Family & Domainsi

Phylogenomic databases

GeneTreeiENSGT00530000063749.
KOiK02085.
OMAiIEDCPIN.
OrthoDBiEOG7BCN9S.
TreeFamiTF106496.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR026836. APC.
IPR009240. APC_15aa_rpt.
IPR009234. APC_basic_dom.
IPR009223. APC_Cys-rich_rpt.
IPR026831. APC_dom.
IPR026818. Apc_fam.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR009232. EB1-bd.
IPR009224. SAMP.
[Graphical view]
PANTHERiPTHR12607. PTHR12607. 1 hit.
PTHR12607:SF11. PTHR12607:SF11. 1 hit.
PfamiPF05972. APC_15aa. 4 hits.
PF05956. APC_basic. 1 hit.
PF05923. APC_crr. 7 hits.
PF00514. Arm. 3 hits.
PF05937. EB1_binding. 1 hit.
PF05924. SAMP. 3 hits.
PF11414. Suppressor_APC. 1 hit.
[Graphical view]
SMARTiSM00185. ARM. 6 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50176. ARM_REPEAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

G3V8Q9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTELETE ASNMKEVLKQ
60 70 80 90 100
LQGSIEDETM TSGQIDLLER LKEFNLDSNF PGVKLRSKMS LRSYGSREGS
110 120 130 140 150
VSSRSGECSP VPMGSFPRRA FVNGSRESTG YLEELEKERS LLLADLDKEE
160 170 180 190 200
KEKDWYYAQL QNLTKRIDSL PLTENFSLQT DMTRRQLEYE ARQIRAAMEE
210 220 230 240 250
QLGTCQDMEK RAQRRIARIQ QIEKDILRVR QLLQSQAAEA ERSSQSKHET
260 270 280 290 300
ASHEAERQLE GQGVAESNLA TSGSGQSSAA RVDHETAGVL SSSGTHSAPR
310 320 330 340 350
RLTSHLGTKV EMVYSLLSML GTHDKDDMSR TLLAMSSSQD SCISMRQSGC
360 370 380 390 400
LPLLIQLLHG NDKDSVLLGN SRGSKEARAR ASAALHNIIH SQPDDKRGRR
410 420 430 440 450
EIRVLHLLEQ IRAYCETCWE WQEAHEQGMD QDKNPMPAPV EHQICPAVCV
460 470 480 490 500
LMKLSFDEEH RHAMNELGGL QAIAELLQVD CEMHGLTDDH YSVTLRRYAG
510 520 530 540 550
MALTNLTFGD VANKATLCSM KGCMRALVAQ LKSESEDLQQ VIASVLRNLS
560 570 580 590 600
WRADVNSKKT LREVGSVKAL MECALEVKKE STLKSVLSAL WNLSAHCTEN
610 620 630 640 650
KADICAVDGA LAFLVGTLTY RSQTNTLAII ESGGGILRNV SSLIATNEDH
660 670 680 690 700
RQILRENNCL QTLLQHLKSH SLTIVSNACG TLWNLSARNP KDQEALWDMG
710 720 730 740 750
AVSMLKNLIH SKHKMIAMGS AAALRNLMAN RPAKYKDANI MSPGSSLPSL
760 770 780 790 800
HVRKQKALEA ELDAQHLSET FDNIDNLSPK ASHRSKQRHK QNLYGDYVFD
810 820 830 840 850
ASRHDDNRSD NFNTGNMTVL SPYLNTTVLP SSSSSRGSLD SSRSEKDRSL
860 870 880 890 900
ERERGIGLST YHSATENPGT SSKRGLQLSA TAAQIAKVME EVSALHTSQD
910 920 930 940 950
DRSPASAAEL HCVAEERTAA RRSSASHTHP NTHNFAKSES SNRTCSMPYA
960 970 980 990 1000
KVEYKRSSND SLNSVTSSDG YGKRGQMKPS VESYSEDDEG KFCSYGQYPA
1010 1020 1030 1040 1050
DLAHKIHSAN HMDDNGGELD TPINYSLKYS DEQLNSGRQS PSQNERWARP
1060 1070 1080 1090 1100
KHVIEDEIKQ NEQRQSRSQN TNFPVYSENT DDKHLKFQQH FGQQECVSPY
1110 1120 1130 1140 1150
RSRGTNGSET NRMGSSHAVN QNVNQSLCQE DDYEDDKPTN YSERYSEEEQ
1160 1170 1180 1190 1200
HEEEERPTNY SIKYNEEKHH VDQPIDYSLK YATDISSSQK PSFSFSKTPS
1210 1220 1230 1240 1250
VQGTKTEHNS PSSEAASAPS SNAKRQSQLH PSSAQRNGQT PKGTACKVPS
1260 1270 1280 1290 1300
INQETMQTYC VEDTPICFSR CSSLSSLSSA EDEIGCDQTT QEADSANTLQ
1310 1320 1330 1340 1350
IAEIKENDVT RSAQDPASDV PAVSQSTRTK PSRLQASGLA SESARHKAVE
1360 1370 1380 1390 1400
FSSGAKSPSK SGAQTPKSPP EHYVQETPLV FSRCTSVSSL DSFESRSIAS
1410 1420 1430 1440 1450
SVQSEPCSGM VSGIVSPSDL PDSPGQTMPP SRSKTPPPPP PPQPVQTKRE
1460 1470 1480 1490 1500
VPKTKVPAAE QREGGPKQTA VSAAVQRVQV LPDADTLLHF ATESTPDGFS
1510 1520 1530 1540 1550
CSSSLSALSL DEPFIQKDVE LRIMPPVQEN DNGNETEPEQ PEESNENQDK
1560 1570 1580 1590 1600
EVEKPDSEKD LLDDSDDDDI EILEECIISA MPTKSSRKAK KLAQTASKLP
1610 1620 1630 1640 1650
PPVARKPSQL PVYKLLPSQS RLQAQKHVSF TPGDDVPRVY CVEGTPINFS
1660 1670 1680 1690 1700
TATSLSDLTI ESPPNELAAG DGVRASVQSG EFEKRDTIPT EGRSTDEAQR
1710 1720 1730 1740 1750
GKVSSIAIPD LDGSKAEEGD ILAECINSAL PKGRSHKPFR VKKIMDQVQQ
1760 1770 1780 1790 1800
ASMTSSGTNK NQIDTKKKKP TSPVKPMPQN TEYRTRVRKN TDSKVNVNTE
1810 1820 1830 1840 1850
ETFSDNKDSK KQSLKNNPKD LNDKLPDNED RVRGGFTFDS PHHYTPIEGT
1860 1870 1880 1890 1900
PYCFSRNDSL SSLDFDDDDV DLSREKAELR KGKESKDSEA KVTCHTEPSS
1910 1920 1930 1940 1950
SQQSARKAQA STKHPVNRGP SKPLLQEQPT FPQSSKDVPD RGAATDEKLQ
1960 1970 1980 1990 2000
NFAIENTPVC FSRNSSLSSL SDVDQENNNN EETGPVRDAE PANAQGQPGK
2010 2020 2030 2040 2050
PQASGYAPKS FHVEDTPVCF SRNSSLSSLS IDSEDDLLQE CISSAMPKKR
2060 2070 2080 2090 2100
RPSRLKGEGE RQSPRKVGSV LAEDLTLDLK DIQRPESEHG LSPDSENFDW
2110 2120 2130 2140 2150
KAIQEGANSI VSSLHQAAAA AACLSRQASS DSDSILSLKS GVSLGSPFHL
2160 2170 2180 2190 2200
TPDQEEKPFT SHKGPRILKP GEKSTLEAKK IESENKGIKG GKKVYKSLIT
2210 2220 2230 2240 2250
GKIRSNSEIS SQMKQPLQTN MPSISRGRTM IHIPGVRNSS SSTSPVSKKG
2260 2270 2280 2290 2300
PPLKTPASKS PSEGPVATTS PRGTKPAVKS ELSPITRQTS HISGSNKGPS
2310 2320 2330 2340 2350
RSGSRDSTPS RPTQQPLSRP MQSPGRNSIS PGRNGISTPN KLSQLPRTSS
2360 2370 2380 2390 2400
PSTASTKSSG SGKMSYTSPG RQLSQQNLSK QTGLSKNASS IPRSESASKG
2410 2420 2430 2440 2450
LNQMNNSNGS NKKVELSRMS STKSSGSESD RSERPALVRQ STFIKEAPSP
2460 2470 2480 2490 2500
TLRRKLEESA SFESLSPSSR PDSPTRSQAQ TPVLSPSLPD MSLSTHPSVQ
2510 2520 2530 2540 2550
AGGWRKLPPN LSPTIEYSDG RPSKRHDIAR SHSESPSRLP VNRAGTWKRE
2560 2570 2580 2590 2600
HSKHSSSLPR VSTWRRTGSS SSILSASSES SEKAKSEDEK HVNSVPGPRQ
2610 2620 2630 2640 2650
MKENQVPTKG TWRKIKESEI SPTNTVSQTT SSGAASGAES KTLIYQMAPA
2660 2670 2680 2690 2700
VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSISEKG NPSIKDSKDT
2710 2720 2730 2740 2750
QGKQSVGSGS PVQTVGLENR LNSFIQVEAP EQKGTETKAG QSSPAPVAET
2760 2770 2780 2790 2800
GETCMAERTP FSSSSSSKHS SPSGTVAARV TPFNYNPSPR KSSADSTSAR
2810 2820 2830 2840
PSQIPTPVGS STKKRDSKTD STESSGAQSP KRHSGSYLVT SV
Length:2,842
Mass (Da):310,507
Last modified:November 16, 2011 - v1
Checksum:iF2A2B2083E31C4BD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06094556 Genomic DNA. No translation available.
AABR06094557 Genomic DNA. No translation available.
CH473974 Genomic DNA. Translation: EDL76212.1.
CH473974 Genomic DNA. Translation: EDL76213.1.
CH473974 Genomic DNA. Translation: EDL76216.1.
CH473974 Genomic DNA. Translation: EDL76217.1.
RefSeqiXP_006254573.1. XM_006254511.2.
UniGeneiRn.156346.
Rn.88057.

Genome annotation databases

EnsembliENSRNOT00000027691; ENSRNOP00000027691; ENSRNOG00000020423.
GeneIDi24205.
KEGGirno:24205.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06094556 Genomic DNA. No translation available.
AABR06094557 Genomic DNA. No translation available.
CH473974 Genomic DNA. Translation: EDL76212.1 .
CH473974 Genomic DNA. Translation: EDL76213.1 .
CH473974 Genomic DNA. Translation: EDL76216.1 .
CH473974 Genomic DNA. Translation: EDL76217.1 .
RefSeqi XP_006254573.1. XM_006254511.2.
UniGenei Rn.156346.
Rn.88057.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000027691 ; ENSRNOP00000027691 ; ENSRNOG00000020423 .
GeneIDi 24205.
KEGGi rno:24205.

Organism-specific databases

CTDi 324.
RGDi 2123. Apc.

Phylogenomic databases

GeneTreei ENSGT00530000063749.
KOi K02085.
OMAi IEDCPIN.
OrthoDBi EOG7BCN9S.
TreeFami TF106496.

Enzyme and pathway databases

Reactomei REACT_214025. deactivation of the beta-catenin transactivating complex.
REACT_216976. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_232045. truncations of AMER1 destabilize the destruction complex.
REACT_234350. Beta-catenin phosphorylation cascade.
REACT_237110. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_238778. Apoptotic cleavage of cellular proteins.
REACT_242544. T41 mutants of beta-catenin aren't phosphorylated.
REACT_245397. APC truncation mutants are not K63 polyubiquitinated.
REACT_248040. S37 mutants of beta-catenin aren't phosphorylated.
REACT_249104. APC truncation mutants have impaired AXIN binding.
REACT_250136. S33 mutants of beta-catenin aren't phosphorylated.
REACT_251328. S45 mutants of beta-catenin aren't phosphorylated.
REACT_257365. Degradation of beta-catenin by the destruction complex.
REACT_260559. AXIN missense mutants destabilize the destruction complex.

Miscellaneous databases

NextBioi 35584209.
PROi G3V8Q9.

Family and domain databases

Gene3Di 1.25.10.10. 2 hits.
InterProi IPR026836. APC.
IPR009240. APC_15aa_rpt.
IPR009234. APC_basic_dom.
IPR009223. APC_Cys-rich_rpt.
IPR026831. APC_dom.
IPR026818. Apc_fam.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000225. Armadillo.
IPR009232. EB1-bd.
IPR009224. SAMP.
[Graphical view ]
PANTHERi PTHR12607. PTHR12607. 1 hit.
PTHR12607:SF11. PTHR12607:SF11. 1 hit.
Pfami PF05972. APC_15aa. 4 hits.
PF05956. APC_basic. 1 hit.
PF05923. APC_crr. 7 hits.
PF00514. Arm. 3 hits.
PF05937. EB1_binding. 1 hit.
PF05924. SAMP. 3 hits.
PF11414. Suppressor_APC. 1 hit.
[Graphical view ]
SMARTi SM00185. ARM. 6 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50176. ARM_REPEAT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  2. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  3. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  4. "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
    Hoffert J.D., Pisitkun T., Wang G., Shen R.F., Knepper M.A.
    Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Ensembl
    Submitted (SEP-2011) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiG3V8Q9_RAT
AccessioniPrimary (citable) accession number: G3V8Q9
Entry historyi
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: November 26, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteomeImported

External Data

Dasty 3