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O88907

- PIAS1_MOUSE

UniProt

O88907 - PIAS1_MOUSE

Protein

E3 SUMO-protein ligase PIAS1

Gene

Pias1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (07 Dec 2004)
      Previous versions | rss
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    Functioni

    Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA By similarity. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Together with PRMT1, may repress STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation.By similarity1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri320 – 39778SP-RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. SUMO ligase activity Source: Ensembl
    4. transcription corepressor activity Source: MGI
    5. ubiquitin protein ligase binding Source: BHF-UCL
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. JAK-STAT cascade Source: MGI
    2. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    3. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: UniProtKB
    4. positive regulation of protein sumoylation Source: UniProtKB
    5. positive regulation of smooth muscle cell differentiation Source: Ensembl
    6. positive regulation of transcription, DNA-templated Source: Ensembl
    7. protein-DNA complex assembly Source: Ensembl
    8. protein sumoylation Source: UniProtKB
    9. regulation of cell proliferation Source: UniProtKB
    10. spermatogenesis Source: Ensembl
    11. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198645. Regulation of IFNG signaling.
    UniPathwayiUPA00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 SUMO-protein ligase PIAS1 (EC:6.3.2.-)
    Alternative name(s):
    DEAD/H box-binding protein 1
    Protein inhibitor of activated STAT protein 1
    Gene namesi
    Name:Pias1
    Synonyms:Ddxbp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1913125. Pias1.

    Subcellular locationi

    Nucleus speckle By similarity. NucleusPML body 2 Publications
    Note: Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton.By similarity

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB-SubCell
    2. nucleus Source: MGI
    3. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi346 – 3461C → G: Loss of promotion of EKLF sumoylation; when associated with G-351 and A-356. 1 Publication
    Mutagenesisi351 – 3511C → G: Loss of promotion of EKLF sumoylation; when associated with G-346 and A-356. 1 Publication
    Mutagenesisi356 – 3561C → A: Loss of promotion of EKLF sumoylation; when associated with G-346 and G-351. 1 Publication
    Mutagenesisi363 – 3631I → S: Loss of promotion of EKLF sumoylation. 1 Publication
    Mutagenesisi372 – 3721W → A: Loss of promotion of NCOA2 sumoylation. 1 Publication
    Mutagenesisi375 – 3762PV → AA: Loss of promotion of EKLF sumoylation.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 651650E3 SUMO-protein ligase PIAS1PRO_0000218975Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei303 – 3031Asymmetric dimethylarginine; by PRMT1By similarity
    Modified residuei485 – 4851Phosphoserine1 Publication
    Modified residuei487 – 4871Phosphothreonine1 Publication
    Modified residuei503 – 5031PhosphoserineBy similarity
    Modified residuei510 – 5101PhosphoserineBy similarity
    Modified residuei522 – 5221PhosphoserineBy similarity

    Post-translational modificationi

    Sumoylated.By similarity
    Dimethylated by PRMT1 at Arg-303 in the late phase of interferon gamma (IFN-gamma) signaling, leading to preferential interaction with STAT1 and thus resulting in release of STAT1 from its target gene.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO88907.
    PRIDEiO88907.

    PTM databases

    PhosphoSiteiO88907.

    Expressioni

    Tissue specificityi

    Expressed in kidney, heart, spleen, brain and cerebellum; weak expression, if any, in liver and lung.1 Publication

    Developmental stagei

    Expressed as early as 7.6 dpc. Expression remains high through 15.5 dpc.1 Publication

    Gene expression databases

    ArrayExpressiO88907.
    BgeeiO88907.
    CleanExiMM_PIAS1.
    GenevestigatoriO88907.

    Interactioni

    Subunit structurei

    Interacts with STAT1 By similarity. Interacts with NR2C1; the interaction promotes its sumoylation. Interacts with DDX21, CSRP2, AXIN1, JUN, SATB2, PLAG1, TP53 and STAT1 (dimer), following IFNA1-stimulation. Interacts with SP3 (preferentially when SUMO-modified). Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase By similarity. Interacts with CHUK/IKKA; this interaction induces PIAS1 phosphorylation. Interacts with PTK2/FAK1; the interaction promotes its sumoylation By similarity. Interacts with SUMO1, UBE2I, NCOA2 and AR. Interacts with NR2C1; the interaction promotes its sumoylation. Interacts with DDX5. Interacts with MTA1 By similarity. Interacts with PML (isoform PML-12).By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SufuQ9Z0P73EBI-3508327,EBI-3508336

    Protein-protein interaction databases

    BioGridi208005. 34 interactions.
    DIPiDIP-29277N.
    IntActiO88907. 16 interactions.
    MINTiMINT-4107556.

    Structurei

    3D structure databases

    ProteinModelPortaliO88907.
    SMRiO88907. Positions 1-65, 135-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 4535SAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini124 – 288165PINITPROSITE-ProRule annotationAdd
    BLAST
    Repeati520 – 52341
    Repeati557 – 56042
    Repeati598 – 60143; approximate
    Repeati612 – 61544; approximate

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni462 – 47312SUMO1-bindingBy similarityAdd
    BLAST
    Regioni520 – 615964 X 4 AA repeats of N-T-S-LAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi19 – 235LXXLL motif
    Motifi56 – 649Nuclear localization signalSequence Analysis
    Motifi368 – 38013Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi577 – 63458Ser-richAdd
    BLAST

    Domaini

    The LXXLL motif is a transcriptional coregulator signature.
    The SP-RING-type domain is required for promoting EKLF sumoylation.

    Sequence similaritiesi

    Belongs to the PIAS family.Curated
    Contains 1 PINIT domain.PROSITE-ProRule annotation
    Contains 1 SAP domain.PROSITE-ProRule annotation
    Contains 1 SP-RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri320 – 39778SP-RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG125513.
    HOGENOMiHOG000230594.
    HOVERGENiHBG053598.
    InParanoidiO88907.
    KOiK04706.
    OMAiGRTYSMA.
    OrthoDBiEOG7HF1JB.
    PhylomeDBiO88907.
    TreeFamiTF323787.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    InterProiIPR027227. PIAS1.
    IPR023321. PINIT.
    IPR003034. SAP_dom.
    IPR004181. Znf_MIZ.
    [Graphical view]
    PANTHERiPTHR10782:SF11. PTHR10782:SF11. 1 hit.
    PfamiPF14324. PINIT. 1 hit.
    PF02891. zf-MIZ. 1 hit.
    [Graphical view]
    SMARTiSM00513. SAP. 1 hit.
    [Graphical view]
    PROSITEiPS51466. PINIT. 1 hit.
    PS50800. SAP. 1 hit.
    PS51044. ZF_SP_RING. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O88907-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS    50
    PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPPTLS PSTIPQLTYD 100
    GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL 150
    IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL 200
    RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI 250
    NITSLVRLST TVPNTIVVSW TAEIGRTYSM AVYLVKQLSS TVLLQRLRAK 300
    GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT 350
    CSHLQCFDAT LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT 400
    DCDEIQFKED GSWAPMRSKK EVQEVTASYN GVDGCLSSTL EHQVASHNQS 450
    SNKNKKVEVI DLTIDSSSDE EEEEPPAKRT CPSLSPTSPL SNKGILSLPH 500
    QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL QGLDFFPFLS 550
    GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 600
    LPATNGSSSG SNSSLVSSNS LRESHGHGVA SRSSADTASI FGIIPDIISL 650
    D 651
    Length:651
    Mass (Da):71,618
    Last modified:December 7, 2004 - v2
    Checksum:i8844364E8FEE4F7F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti320 – 3201P → S in AAC36701. (PubMed:9724754)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077950 mRNA. Translation: AAC36701.1.
    AK075708 mRNA. Translation: BAC35902.1.
    BC051417 mRNA. Translation: AAH51417.1.
    CCDSiCCDS40665.1.
    RefSeqiNP_062637.2. NM_019663.3.
    UniGeneiMm.431253.
    Mm.491651.

    Genome annotation databases

    EnsembliENSMUST00000098651; ENSMUSP00000096248; ENSMUSG00000032405.
    GeneIDi56469.
    KEGGimmu:56469.
    UCSCiuc009qas.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077950 mRNA. Translation: AAC36701.1 .
    AK075708 mRNA. Translation: BAC35902.1 .
    BC051417 mRNA. Translation: AAH51417.1 .
    CCDSi CCDS40665.1.
    RefSeqi NP_062637.2. NM_019663.3.
    UniGenei Mm.431253.
    Mm.491651.

    3D structure databases

    ProteinModelPortali O88907.
    SMRi O88907. Positions 1-65, 135-416.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 208005. 34 interactions.
    DIPi DIP-29277N.
    IntActi O88907. 16 interactions.
    MINTi MINT-4107556.

    PTM databases

    PhosphoSitei O88907.

    Proteomic databases

    PaxDbi O88907.
    PRIDEi O88907.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000098651 ; ENSMUSP00000096248 ; ENSMUSG00000032405 .
    GeneIDi 56469.
    KEGGi mmu:56469.
    UCSCi uc009qas.1. mouse.

    Organism-specific databases

    CTDi 8554.
    MGIi MGI:1913125. Pias1.

    Phylogenomic databases

    eggNOGi NOG125513.
    HOGENOMi HOG000230594.
    HOVERGENi HBG053598.
    InParanoidi O88907.
    KOi K04706.
    OMAi GRTYSMA.
    OrthoDBi EOG7HF1JB.
    PhylomeDBi O88907.
    TreeFami TF323787.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .
    Reactomei REACT_198645. Regulation of IFNG signaling.

    Miscellaneous databases

    ChiTaRSi PIAS1. mouse.
    NextBioi 312730.
    PROi O88907.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88907.
    Bgeei O88907.
    CleanExi MM_PIAS1.
    Genevestigatori O88907.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    InterProi IPR027227. PIAS1.
    IPR023321. PINIT.
    IPR003034. SAP_dom.
    IPR004181. Znf_MIZ.
    [Graphical view ]
    PANTHERi PTHR10782:SF11. PTHR10782:SF11. 1 hit.
    Pfami PF14324. PINIT. 1 hit.
    PF02891. zf-MIZ. 1 hit.
    [Graphical view ]
    SMARTi SM00513. SAP. 1 hit.
    [Graphical view ]
    PROSITEi PS51466. PINIT. 1 hit.
    PS50800. SAP. 1 hit.
    PS51044. ZF_SP_RING. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: B-cell.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Lung.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N-3.
      Tissue: Mammary tumor.
    4. "Cloning and analysis of a murine Pias family member, Pias-gamma, in developing skin and neurons."
      Sturm S., Koch M., White F.A.
      J. Mol. Neurosci. 14:107-121(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
      Tissue: Brain.
    5. "ARIP3 (androgen receptor-interacting protein 3) and other PIAS (protein inhibitor of activated STAT) proteins differ in their ability to modulate steroid receptor-dependent transcriptional activation."
      Kotaja N., Aittomaeki S., Silvennoinen O., Palvimo J.J., Jaenne O.A.
      Mol. Endocrinol. 14:1986-2000(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AR.
    6. "PIAS proteins modulate transcription factors by functioning as SUMO-1 ligases."
      Kotaja N., Karvonen U., Jaenne O.A., Palvimo J.J.
      Mol. Cell. Biol. 22:5222-5234(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUMO1; UBE2I AND NCOA2, SUBCELLULAR LOCATION, SUMOYLATION OF AR AND NCOA2, MUTAGENESIS OF TRP-372.
    7. Cited for: STAT1 SUMOYLATION.
    8. "Sumoylation of EKLF promotes transcriptional repression and is involved in inhibition of megakaryopoiesis."
      Siatecka M., Xue L., Bieker J.J.
      Mol. Cell. Biol. 27:8547-8560(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION OF KLF1, MUTAGENESIS OF CYS-346; CYS-351; CYS-356; ILE-363 AND 375-PRO-VAL-376.
    9. "SUMOylation of Tr2 orphan receptor involves Pml and fine-tunes Oct4 expression in stem cells."
      Park S.W., Hu X., Gupta P., Lin Y.P., Ha S.G., Wei L.N.
      Nat. Struct. Mol. Biol. 14:68-75(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NR2C1.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-485 AND THR-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA."
      Rabellino A., Carter B., Konstantinidou G., Wu S.Y., Rimessi A., Byers L.A., Heymach J.V., Girard L., Chiang C.M., Teruya-Feldstein J., Scaglioni P.P.
      Cancer Res. 72:2275-2284(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PML.

    Entry informationi

    Entry nameiPIAS1_MOUSE
    AccessioniPrimary (citable) accession number: O88907
    Secondary accession number(s): Q8C6H5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 5, 2002
    Last sequence update: December 7, 2004
    Last modified: October 1, 2014
    This is version 129 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3