Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8N2W9

- PIAS4_HUMAN

UniProt

Q8N2W9 - PIAS4_HUMAN

Protein

E3 SUMO-protein ligase PIAS4

Gene

PIAS4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Oct 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation.7 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri311 – 38878SP-RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. SUMO ligase activity Source: UniProtKB
    4. ubiquitin protein ligase binding Source: BHF-UCL
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
    2. negative regulation of transcription, DNA-templated Source: UniProtKB
    3. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    4. positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
    5. positive regulation of keratinocyte apoptotic process Source: BHF-UCL
    6. positive regulation of protein sumoylation Source: UniProtKB
    7. protein sumoylation Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB-KW
    9. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway, Wnt signaling pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ8N2W9.
    UniPathwayiUPA00886.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 SUMO-protein ligase PIAS4 (EC:6.3.2.-)
    Alternative name(s):
    PIASy
    Protein inhibitor of activated STAT protein 4
    Protein inhibitor of activated STAT protein gamma
    Short name:
    PIAS-gamma
    Gene namesi
    Name:PIAS4
    Synonyms:PIASG
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:17002. PIAS4.

    Subcellular locationi

    NucleusPML body 3 Publications
    Note: Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. nuclear matrix Source: Ensembl
    3. nucleus Source: UniProtKB
    4. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi23 – 242LL → AA: Loss of repression of AR- and STAT1-induced transcription; no effect on AR- and STAT1-binding.
    Mutagenesisi35 – 351K → R: Complete loss of sumoylation. No enhancement of TCF4 sumoylation. No effect on interaction with TCF4. Colocalizes with SUMO1 in nucleus but concentrated into nuclear granules. 2 Publications
    Mutagenesisi128 – 1281K → R: Some loss of sumoylation. 2 Publications
    Mutagenesisi342 – 3421C → A: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-347.
    Mutagenesisi347 – 3471C → A: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-342. AR- and STAT1-binding.

    Organism-specific databases

    PharmGKBiPA134945903.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 510509E3 SUMO-protein ligase PIAS4PRO_0000218982Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei114 – 1141N6-acetyllysine1 Publication
    Cross-linki128 – 128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Sumoylated. Lys-35 is the main site of sumoylation. Sumoylation is required for TCF4 sumoylation and transcriptional activation. Represses LEF1 transcriptional activity. SUMO1 is the preferred conjugate.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ8N2W9.
    PaxDbiQ8N2W9.
    PRIDEiQ8N2W9.

    PTM databases

    PhosphoSiteiQ8N2W9.

    Expressioni

    Tissue specificityi

    Highly expressed in testis and, at lower levels, in spleen, prostate, ovary, colon and peripheral blood leukocytes.1 Publication

    Gene expression databases

    ArrayExpressiQ8N2W9.
    BgeeiQ8N2W9.
    CleanExiHS_PIAS4.
    GenevestigatoriQ8N2W9.

    Organism-specific databases

    HPAiHPA010598.

    Interactioni

    Subunit structurei

    Interacts with AR, AXIN1, GATA2, LEF1, TP53 and STAT1 (IFNG-induced). Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) By similarity. Interacts with TICAM1. Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase. Interacts with MTA1.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HIF1AQ166653EBI-473160,EBI-447269
    HTTP428583EBI-473160,EBI-466029
    PARP1P098745EBI-473160,EBI-355676
    SUMO2P619563EBI-473160,EBI-473220
    TADA3O755282EBI-473160,EBI-473249
    TP53P046372EBI-473160,EBI-366083

    Protein-protein interaction databases

    BioGridi119624. 87 interactions.
    DIPiDIP-32499N.
    IntActiQ8N2W9. 55 interactions.
    MINTiMINT-1181821.
    STRINGi9606.ENSP00000262971.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N2W9.
    SMRiQ8N2W9. Positions 3-66, 130-407.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 4635SAPCuratedPROSITE-ProRule annotationAdd
    BLAST
    Domaini119 – 279161PINITPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi20 – 245LXXLL motif

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi464 – 49229Asp/Glu-rich (acidic)Add
    BLAST

    Domaini

    The LXXLL motif is a coregulator signature that is essential for transcriptional corepression.

    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 fingeri311 – 38878SP-RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG125513.
    HOGENOMiHOG000230594.
    HOVERGENiHBG053598.
    InParanoidiQ8N2W9.
    KOiK16065.
    OMAiRICYTDT.
    OrthoDBiEOG7HF1JB.
    PhylomeDBiQ8N2W9.
    TreeFamiTF323787.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    InterProiIPR023321. PINIT.
    IPR003034. SAP_dom.
    IPR004181. Znf_MIZ.
    [Graphical view]
    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.

    Q8N2W9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAAELVEAKN MVMSFRVSDL QMLLGFVGRS KSGLKHELVT RALQLVQFDC    50
    SPELFKKIKE LYETRYAKKN SEPAPQPHRP LDPLTMHSTY DRAGAVPRTP 100
    LAGPNIDYPV LYGKYLNGLG RLPAKTLKPE VRLVKLPFFN MLDELLKPTE 150
    LVPQNNEKLQ ESPCIFALTP RQVELIRNSR ELQPGVKAVQ VVLRICYSDT 200
    SCPQEDQYPP NIAVKVNHSY CSVPGYYPSN KPGVEPKRPC RPINLTHLMY 250
    LSSATNRITV TWGNYGKSYS VALYLVRQLT SSELLQRLKT IGVKHPELCK 300
    ALVKEKLRLD PDSEIATTGV RVSLICPLVK MRLSVPCRAE TCAHLQCFDA 350
    VFYLQMNEKK PTWMCPVCDK PAPYDQLIID GLLSKILSEC EDADEIEYLV 400
    DGSWCPIRAE KERSCSPQGA ILVLGPSDAN GLLPAPSVNG SGALGSTGGG 450
    GPVGSMENGK PGADVVDLTL DSSSSSEDEE EEEEEEEDED EEGPRPKRRC 500
    PFQKGLVPAC 510
    Length:510
    Mass (Da):56,504
    Last modified:October 1, 2002 - v1
    Checksum:i26AAA18246E1ACE3
    GO

    Sequence cautioni

    The sequence AAD45155.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti178 – 1781N → K(PubMed:9724754)Curated
    Sequence conflicti179 – 1824SREL → FQGM(PubMed:9724754)Curated
    Sequence conflicti179 – 1824SREL → FQGM(PubMed:11388671)Curated
    Sequence conflicti482 – 4821E → G in AAH66895. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077952 mRNA. Translation: AAC36703.1.
    BC010047 mRNA. Translation: AAH10047.2.
    BC029874 mRNA. Translation: AAH29874.1.
    BC066895 mRNA. Translation: AAH66895.1.
    AF164437 mRNA. Translation: AAD45155.1. Different initiation.
    CCDSiCCDS12118.1.
    RefSeqiNP_056981.2. NM_015897.2.
    UniGeneiHs.105779.

    Genome annotation databases

    EnsembliENST00000262971; ENSP00000262971; ENSG00000105229.
    GeneIDi51588.
    KEGGihsa:51588.
    UCSCiuc002lzg.3. human.

    Polymorphism databases

    DMDMi34922831.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF077952 mRNA. Translation: AAC36703.1 .
    BC010047 mRNA. Translation: AAH10047.2 .
    BC029874 mRNA. Translation: AAH29874.1 .
    BC066895 mRNA. Translation: AAH66895.1 .
    AF164437 mRNA. Translation: AAD45155.1 . Different initiation.
    CCDSi CCDS12118.1.
    RefSeqi NP_056981.2. NM_015897.2.
    UniGenei Hs.105779.

    3D structure databases

    ProteinModelPortali Q8N2W9.
    SMRi Q8N2W9. Positions 3-66, 130-407.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119624. 87 interactions.
    DIPi DIP-32499N.
    IntActi Q8N2W9. 55 interactions.
    MINTi MINT-1181821.
    STRINGi 9606.ENSP00000262971.

    PTM databases

    PhosphoSitei Q8N2W9.

    Polymorphism databases

    DMDMi 34922831.

    Proteomic databases

    MaxQBi Q8N2W9.
    PaxDbi Q8N2W9.
    PRIDEi Q8N2W9.

    Protocols and materials databases

    DNASUi 51588.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262971 ; ENSP00000262971 ; ENSG00000105229 .
    GeneIDi 51588.
    KEGGi hsa:51588.
    UCSCi uc002lzg.3. human.

    Organism-specific databases

    CTDi 51588.
    GeneCardsi GC19P004007.
    HGNCi HGNC:17002. PIAS4.
    HPAi HPA010598.
    MIMi 605989. gene.
    neXtProti NX_Q8N2W9.
    PharmGKBi PA134945903.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG125513.
    HOGENOMi HOG000230594.
    HOVERGENi HBG053598.
    InParanoidi Q8N2W9.
    KOi K16065.
    OMAi RICYTDT.
    OrthoDBi EOG7HF1JB.
    PhylomeDBi Q8N2W9.
    TreeFami TF323787.

    Enzyme and pathway databases

    UniPathwayi UPA00886 .
    SignaLinki Q8N2W9.

    Miscellaneous databases

    ChiTaRSi PIAS4. human.
    GeneWikii PIAS4.
    GenomeRNAii 51588.
    NextBioi 55429.
    PROi Q8N2W9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8N2W9.
    Bgeei Q8N2W9.
    CleanExi HS_PIAS4.
    Genevestigatori Q8N2W9.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    InterProi IPR023321. PINIT.
    IPR003034. SAP_dom.
    IPR004181. Znf_MIZ.
    [Graphical view ]
    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 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].
      Tissue: Brain, Lung and Skin.
    3. "A putative protein inhibitor of activated STAT (PIASy) interacts with p53 and inhibits p53-mediated transactivation but not apoptosis."
      Nelson V., Davis G.E., Maxwell S.A.
      Apoptosis 6:221-234(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-510, INTERACTION WITH TP53.
    4. "A transcriptional corepressor of Stat1 with an essential LXXLL signature motif."
      Liu B., Gross M., ten Hoeve J., Shuai K.
      Proc. Natl. Acad. Sci. U.S.A. 98:3203-3207(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STAT1, SUBCELLULAR LOCATION, MUTAGENESIS OF 23-LEU-LEU-24.
    5. "Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells."
      Gross M., Liu B., Tan J.-A., French F.S., Carey M., Shuai K.
      Oncogene 20:3880-3887(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AR, TISSUE SPECIFICITY, MUTAGENESIS OF 23-LEU-LEU-24.
    6. "SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling."
      Rui H.L., Fan E., Zhou H.M., Xu Z., Zhang Y., Lin S.C.
      J. Biol. Chem. 277:42981-42986(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AXIN1.
    7. "Modification of GATA-2 transcriptional activity in endothelial cells by the SUMO E3 ligase PIASy."
      Chun T.-H., Itoh H., Subramanian L., Iniguez-Lluhi J.A., Nakao K.
      Circ. Res. 92:1201-1208(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GATA2.
    8. "Sumoylation is involved in beta-catenin-dependent activation of Tcf-4."
      Yamamoto H., Ihara M., Matsuura Y., Kikuchi A.
      EMBO J. 22:2047-2059(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SUMOYLATION OF TCF4, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-35 AND LYS-128.
    9. "Transactivation properties of c-Myb are critically dependent on two SUMO-1 acceptor sites that are conjugated in a PIASy enhanced manner."
      Dahle O., Andersen T.O., Nordgaard O., Matre V., Del Sal G., Gabrielsen O.S.
      Eur. J. Biochem. 270:1338-1348(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SUMOYLATION OF MYB.
    10. "A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3."
      Subramanian L., Benson M.D., Iniguez-Lluhi J.A.
      J. Biol. Chem. 278:9134-9141(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SUMOYLATION OF CEBPA.
    11. "PIASy represses TRIF-induced ISRE and NF-kappaB activation but not apoptosis."
      Zhang J., Xu L.G., Han K.J., Wei X., Shu H.B.
      FEBS Lett. 570:97-101(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TICAM1.
    12. "SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4."
      Ihara M., Yamamoto H., Kikuchi A.
      Mol. Cell. Biol. 25:3506-3518(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-35 AND LYS-128, FUNCTION IN SUMOYLATION OF TCF4, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-35 AND LYS-128.
    13. "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities."
      Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C., Seino C., Iguchi-Ariga S.M.M., Ariga H.
      Cell Death Differ. 13:96-108(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SUMOYLATION OF PARK7.
    14. "Sumoylation delimits KLF8 transcriptional activity associated with the cell cycle regulation."
      Wei H., Wang X., Gan B., Urvalek A.M., Melkoumian Z.K., Guan J.-L., Zhao J.
      J. Biol. Chem. 281:16664-16671(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KLF8.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
      Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
      J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MTA1.
    18. "DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger."
      Danielsen J.R., Povlsen L.K., Villumsen B.H., Streicher W., Nilsson J., Wikstrom M., Bekker-Jensen S., Mailand N.
      J. Cell Biol. 197:179-187(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SUMOYLATION OF HERC2 AND RNF168.

    Entry informationi

    Entry nameiPIAS4_HUMAN
    AccessioniPrimary (citable) accession number: Q8N2W9
    Secondary accession number(s): O75926, Q96G19, Q9UN16
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2003
    Last sequence update: October 1, 2002
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3