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O94972

- TRI37_HUMAN

UniProt

O94972 - TRI37_HUMAN

Protein

E3 ubiquitin-protein ligase TRIM37

Gene

TRIM37

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (23 Nov 2004)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase required to prevent centriole reduplication. Probably acts by ubiquitinating positive regulators of centriole reduplication.2 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri15 – 5541RING-type; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri90 – 13243B box-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein homodimerization activity Source: UniProtKB
    4. tumor necrosis factor receptor binding Source: UniProtKB
    5. ubiquitin protein ligase binding Source: UniProtKB
    6. ubiquitin-protein transferase activity Source: UniProtKB
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. aggresome assembly Source: UniProtKB
    2. negative regulation of centriole replication Source: UniProtKB
    3. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    4. positive regulation of NF-kappaB transcription factor activity Source: UniProt
    5. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProt
    6. protein autoubiquitination Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiO94972.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase TRIM37 (EC:6.3.2.-)
    Alternative name(s):
    Mulibrey nanism protein
    Tripartite motif-containing protein 37
    Gene namesi
    Name:TRIM37
    Synonyms:KIAA0898, MUL, POB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7523. TRIM37.

    Subcellular locationi

    Cytoplasmperinuclear region. Peroxisome
    Note: Found in vesicles of the peroxisome. Aggregates as aggresomes, a perinuclear region where certain misfolded or aggregated proteins are sequestered for proteasomal degradation.

    GO - Cellular componenti

    1. aggresome Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    5. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Peroxisome

    Pathology & Biotechi

    Involvement in diseasei

    Mulibrey nanism (MUL) [MIM:253250]: Autosomal recessive disorder that involves several tissues of mesodermal origin, implying a defect in a highly pleiotropic gene. Characteristic features include severe growth failure of prenatal onset and constrictive pericardium with consequent hepatomegaly. In addition, muscle hypotonia, J-shaped sella turcica, yellowish dots in the ocular fundi, typical dysmorphic features and hypoplasia of various endocrine glands causing hormonal deficiency are common.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti76 – 761L → P in MUL; decreased ubiquitination and abolishes the formation of perinuclear aggregates. 1 Publication
    VAR_060217
    Natural varianti109 – 1091C → S in MUL; no effect on E3 ubiquitin-protein ligase activity. 1 Publication
    VAR_060219
    Natural varianti322 – 3221G → V in MUL; no effect on ubiquitination but affects subcellular localization. 1 Publication
    VAR_060220

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi35 – 362CC → SS: Reduces ubiquitination and abolishes the formation of perinuclear aggregates. 1 Publication

    Organism-specific databases

    MIMi253250. phenotype.
    Orphaneti2576. MULIBREY nanism.
    PharmGKBiPA35497.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 964964E3 ubiquitin-protein ligase TRIM37PRO_0000056254Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Post-translational modificationi

    Auto-ubiquitinated.1 Publication

    Keywords - PTMi

    Acetylation, Ubl conjugation

    Proteomic databases

    MaxQBiO94972.
    PaxDbiO94972.
    PRIDEiO94972.

    PTM databases

    PhosphoSiteiO94972.

    Expressioni

    Tissue specificityi

    Ubiquitous.1 Publication

    Gene expression databases

    ArrayExpressiO94972.
    BgeeiO94972.
    CleanExiHS_TRIM37.
    GenevestigatoriO94972.

    Organism-specific databases

    HPAiHPA021911.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRC1O436633EBI-741602,EBI-741137

    Protein-protein interaction databases

    BioGridi110678. 48 interactions.
    DIPiDIP-34437N.
    IntActiO94972. 30 interactions.
    MINTiMINT-1433848.
    STRINGi9606.ENSP00000262294.

    Structurei

    Secondary structure

    964
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1 – 1212
    Turni16 – 183
    Beta strandi23 – 275
    Turni29 – 313
    Beta strandi34 – 363
    Helixi37 – 4610
    Turni52 – 543
    Helixi60 – 623
    Helixi69 – 7911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3LRQX-ray2.29A/B/C/D1-90[»]
    ProteinModelPortaliO94972.
    SMRiO94972. Positions 1-84.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO94972.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini276 – 403128MATHPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili132 – 234103Sequence AnalysisAdd
    BLAST
    Coiled coili419 – 45032Sequence AnalysisAdd
    BLAST
    Coiled coili673 – 70028Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi534 – 5407Poly-Ser
    Compositional biasi578 – 5814Poly-Ala

    Sequence similaritiesi

    Belongs to the TRIM/RBCC family.Curated
    Contains 1 B box-type zinc finger.PROSITE-ProRule annotation
    Contains 1 MATH domain.PROSITE-ProRule annotation
    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri15 – 5541RING-type; degeneratePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri90 – 13243B box-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG251245.
    HOGENOMiHOG000013010.
    HOVERGENiHBG057591.
    InParanoidiO94972.
    KOiK10608.
    OMAiVRCMKTD.
    OrthoDBiEOG7QG442.
    PhylomeDBiO94972.
    TreeFamiTF351092.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    4.10.45.10. 1 hit.
    InterProiIPR003649. Bbox_C.
    IPR002083. MATH.
    IPR008974. TRAF-like.
    IPR000315. Znf_B-box.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF00917. MATH. 1 hit.
    PF00643. zf-B_box. 1 hit.
    [Graphical view]
    SMARTiSM00502. BBC. 1 hit.
    SM00336. BBOX. 1 hit.
    SM00061. MATH. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view]
    SUPFAMiSSF49599. SSF49599. 1 hit.
    PROSITEiPS50144. MATH. 1 hit.
    PS50119. ZF_BBOX. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O94972-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDEQSVESIA EVFRCFICME KLRDARLCPH CSKLCCFSCI RRWLTEQRAQ    50
    CPHCRAPLQL RELVNCRWAE EVTQQLDTLQ LCSLTKHEEN EKDKCENHHE 100
    KLSVFCWTCK KCICHQCALW GGMHGGHTFK PLAEIYEQHV TKVNEEVAKL 150
    RRRLMELISL VQEVERNVEA VRNAKDERVR EIRNAVEMMI ARLDTQLKNK 200
    LITLMGQKTS LTQETELLES LLQEVEHQLR SCSKSELISK SSEILMMFQQ 250
    VHRKPMASFV TTPVPPDFTS ELVPSYDSAT FVLENFSTLR QRADPVYSPP 300
    LQVSGLCWRL KVYPDGNGVV RGYYLSVFLE LSAGLPETSK YEYRVEMVHQ 350
    SCNDPTKNII REFASDFEVG ECWGYNRFFR LDLLANEGYL NPQNDTVILR 400
    FQVRSPTFFQ KSRDQHWYIT QLEAAQTSYI QQINNLKERL TIELSRTQKS 450
    RDLSPPDNHL SPQNDDALET RAKKSACSDM LLEGGPTTAS VREAKEDEED 500
    EEKIQNEDYH HELSDGDLDL DLVYEDEVNQ LDGSSSSASS TATSNTEEND 550
    IDEETMSGEN DVEYNNMELE EGELMEDAAA AGPAGSSHGY VGSSSRISRR 600
    THLCSAATSS LLDIDPLILI HLLDLKDRSS IENLWGLQPR PPASLLQPTA 650
    SYSRKDKDQR KQQAMWRVPS DLKMLKRLKT QMAEVRCMKT DVKNTLSEIK 700
    SSSAASGDMQ TSLFSADQAA LAACGTENSG RLQDLGMELL AKSSVANCYI 750
    RNSTNKKSNS PKPARSSVAG SLSLRRAVDP GENSRSKGDC QTLSEGSPGS 800
    SQSGSRHSSP RALIHGSIGD ILPKTEDRQC KALDSDAVVV AVFSGLPAVE 850
    KRRKMVTLGA NAKGGHLEGL QMTDLENNSE TGELQPVLPE GASAAPEEGM 900
    SSDSDIECDT ENEEQEEHTS VGGFHDSFMV MTQPPDEDTH SSFPDGEQIG 950
    PEDLSFNTDE NSGR 964
    Length:964
    Mass (Da):107,906
    Last modified:November 23, 2004 - v2
    Checksum:iC0F08D5A5DC3B5AC
    GO
    Isoform 2 (identifier: O94972-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-122: Missing.
         899-937: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:803
    Mass (Da):89,186
    Checksum:i43486E1064478477
    GO

    Sequence cautioni

    The sequence BAA74921.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti624 – 6241D → A in AAL36460. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti76 – 761L → P in MUL; decreased ubiquitination and abolishes the formation of perinuclear aggregates. 1 Publication
    VAR_060217
    Natural varianti108 – 1081T → A.1 Publication
    Corresponds to variant rs17853504 [ dbSNP | Ensembl ].
    VAR_060218
    Natural varianti109 – 1091C → S in MUL; no effect on E3 ubiquitin-protein ligase activity. 1 Publication
    VAR_060219
    Natural varianti322 – 3221G → V in MUL; no effect on ubiquitination but affects subcellular localization. 1 Publication
    VAR_060220
    Natural varianti838 – 8381V → I.
    Corresponds to variant rs7222388 [ dbSNP | Ensembl ].
    VAR_052142

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 122122Missing in isoform 2. 1 PublicationVSP_011919Add
    BLAST
    Alternative sequencei899 – 93739Missing in isoform 2. 1 PublicationVSP_011920Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF213365 mRNA. Translation: AAL36460.1.
    AB020705 mRNA. Translation: BAA74921.1. Different initiation.
    BX537955 mRNA. Translation: CAD97922.1.
    BC036012 mRNA. Translation: AAH36012.1.
    CCDSiCCDS32694.1. [O94972-1]
    CCDS45746.1. [O94972-1]
    RefSeqiNP_001005207.1. NM_001005207.2. [O94972-1]
    NP_056109.1. NM_015294.3. [O94972-1]
    UniGeneiHs.579079.

    Genome annotation databases

    EnsembliENST00000262294; ENSP00000262294; ENSG00000108395. [O94972-1]
    ENST00000393066; ENSP00000376785; ENSG00000108395. [O94972-1]
    GeneIDi4591.
    KEGGihsa:4591.
    UCSCiuc002iwy.4. human. [O94972-1]
    uc002ixa.4. human. [O94972-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF213365 mRNA. Translation: AAL36460.1 .
    AB020705 mRNA. Translation: BAA74921.1 . Different initiation.
    BX537955 mRNA. Translation: CAD97922.1 .
    BC036012 mRNA. Translation: AAH36012.1 .
    CCDSi CCDS32694.1. [O94972-1 ]
    CCDS45746.1. [O94972-1 ]
    RefSeqi NP_001005207.1. NM_001005207.2. [O94972-1 ]
    NP_056109.1. NM_015294.3. [O94972-1 ]
    UniGenei Hs.579079.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3LRQ X-ray 2.29 A/B/C/D 1-90 [» ]
    ProteinModelPortali O94972.
    SMRi O94972. Positions 1-84.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110678. 48 interactions.
    DIPi DIP-34437N.
    IntActi O94972. 30 interactions.
    MINTi MINT-1433848.
    STRINGi 9606.ENSP00000262294.

    PTM databases

    PhosphoSitei O94972.

    Proteomic databases

    MaxQBi O94972.
    PaxDbi O94972.
    PRIDEi O94972.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262294 ; ENSP00000262294 ; ENSG00000108395 . [O94972-1 ]
    ENST00000393066 ; ENSP00000376785 ; ENSG00000108395 . [O94972-1 ]
    GeneIDi 4591.
    KEGGi hsa:4591.
    UCSCi uc002iwy.4. human. [O94972-1 ]
    uc002ixa.4. human. [O94972-2 ]

    Organism-specific databases

    CTDi 4591.
    GeneCardsi GC17M057059.
    H-InvDB HIX0014039.
    HGNCi HGNC:7523. TRIM37.
    HPAi HPA021911.
    MIMi 253250. phenotype.
    605073. gene.
    neXtProti NX_O94972.
    Orphaneti 2576. MULIBREY nanism.
    PharmGKBi PA35497.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG251245.
    HOGENOMi HOG000013010.
    HOVERGENi HBG057591.
    InParanoidi O94972.
    KOi K10608.
    OMAi VRCMKTD.
    OrthoDBi EOG7QG442.
    PhylomeDBi O94972.
    TreeFami TF351092.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki O94972.

    Miscellaneous databases

    ChiTaRSi TRIM37. human.
    EvolutionaryTracei O94972.
    GeneWikii TRIM37.
    GenomeRNAii 4591.
    NextBioi 17650.
    PROi O94972.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94972.
    Bgeei O94972.
    CleanExi HS_TRIM37.
    Genevestigatori O94972.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    4.10.45.10. 1 hit.
    InterProi IPR003649. Bbox_C.
    IPR002083. MATH.
    IPR008974. TRAF-like.
    IPR000315. Znf_B-box.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF00917. MATH. 1 hit.
    PF00643. zf-B_box. 1 hit.
    [Graphical view ]
    SMARTi SM00502. BBC. 1 hit.
    SM00336. BBOX. 1 hit.
    SM00061. MATH. 1 hit.
    SM00184. RING. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49599. SSF49599. 1 hit.
    PROSITEi PS50144. MATH. 1 hit.
    PS50119. ZF_BBOX. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Gene POB1 is amplified and overexpressed in human breast cancer."
      Wu G., Couch F.J.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    4. "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] (ISOFORM 1), VARIANT ALA-108.
      Tissue: Testis.
    5. Cited for: DISEASE, TISSUE SPECIFICITY.
    6. "The TRIM37 gene encodes a peroxisomal RING-B-box-coiled-coil protein: classification of mulibrey nanism as a new peroxisomal disorder."
      Kallijarvi J., Avela K., Lipsanen-Nyman M., Ulmanen I., Lehesjoki A.E.
      Am. J. Hum. Genet. 70:1215-1228(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "A novel splice site mutation in the TRIM37 gene causes mulibrey nanism in a Turkish family with phenotypic heterogeneity."
      Jagiello P., Hammans C., Wieczorek S., Arning L., Stefanski A., Strehl H., Epplen J.T., Gencik M.
      Hum. Mutat. 21:630-635(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE.
    8. "TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase."
      Kallijaervi J., Lahtinen U., Haemaelaeinen R., Lipsanen-Nyman M., Palvimo J.J., Lehesjoki A.-E.
      Exp. Cell Res. 308:146-155(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, AUTOUBIQUITINATION, MUTAGENESIS OF 35-CYS-CYS-36, VARIANT MUL PRO-76, CHARACTERIZATION OF VARIANTS MUL PRO-76 AND MUL VAL-322.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Discovering regulators of centriole biogenesis through siRNA-based functional genomics in human cells."
      Balestra F.R., Strnad P., Fluckiger I., Gonczy P.
      Dev. Cell 25:555-571(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. Cited for: VARIANT MUL VAL-322, CHARACTERIZATION OF VARIANT MUL VAR-322.
    12. "Wilms' tumor and novel TRIM37 mutations in an Australian patient with mulibrey nanism."
      Haemaelaeinen R.H., Mowat D., Gabbett M.T., O'brien T.A., Kallijaervi J., Lehesjoki A.-E.
      Clin. Genet. 70:473-479(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MUL SER-109, CHARACTERIZATION OF VARIANT MUL SER-109.

    Entry informationi

    Entry nameiTRI37_HUMAN
    AccessioniPrimary (citable) accession number: O94972
    Secondary accession number(s): Q7Z3E6, Q8IYF7, Q8WYF7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: November 23, 2004
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3