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Q9UJX5

- APC4_HUMAN

UniProt

Q9UJX5 - APC4_HUMAN

Protein

Anaphase-promoting complex subunit 4

Gene

ANAPC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 2 (02 Sep 2008)
      Previous versions | rss
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    Functioni

    Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein phosphatase binding Source: BHF-UCL
    3. ubiquitin-protein transferase activity Source: ProtInc

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. G2/M transition of mitotic cell cycle Source: ProtInc
    3. mitotic anaphase Source: ProtInc
    4. mitotic cell cycle Source: Reactome
    5. mitotic nuclear division Source: ProtInc
    6. mitotic spindle assembly checkpoint Source: Reactome
    7. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    8. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    9. protein K11-linked ubiquitination Source: UniProtKB
    10. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    11. ubiquitin-dependent protein catabolic process Source: ProtInc

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Anaphase-promoting complex subunit 4
    Short name:
    APC4
    Alternative name(s):
    Cyclosome subunit 4
    Gene namesi
    Name:ANAPC4
    Synonyms:APC4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:19990. ANAPC4.

    Subcellular locationi

    GO - Cellular componenti

    1. anaphase-promoting complex Source: UniProtKB
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: BHF-UCL

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134894250.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 808808Anaphase-promoting complex subunit 4PRO_0000064595Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei469 – 4691Phosphotyrosine1 Publication
    Modified residuei757 – 7571Phosphoserine1 Publication
    Modified residuei758 – 7581Phosphoserine1 Publication
    Modified residuei777 – 7771Phosphoserine1 Publication
    Modified residuei779 – 7791Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UJX5.
    PaxDbiQ9UJX5.
    PRIDEiQ9UJX5.

    PTM databases

    PhosphoSiteiQ9UJX5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UJX5.
    BgeeiQ9UJX5.
    CleanExiHS_ANAPC4.
    GenevestigatoriQ9UJX5.

    Organism-specific databases

    HPAiCAB032519.
    HPA038395.
    HPA038396.

    Interactioni

    Subunit structurei

    The APC/C is composed of at least 12 subunits.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KIF18AQ8NI772EBI-2554854,EBI-355426
    NEK2P519556EBI-2554854,EBI-633182

    Protein-protein interaction databases

    BioGridi118982. 49 interactions.
    DIPiDIP-56450N.
    IntActiQ9UJX5. 26 interactions.
    MINTiMINT-4787108.
    STRINGi9606.ENSP00000318775.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UJX5.
    SMRiQ9UJX5. Positions 175-215, 721-749.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the APC4 family.Curated

    Phylogenomic databases

    eggNOGiNOG248176.
    HOGENOMiHOG000033987.
    HOVERGENiHBG044815.
    InParanoidiQ9UJX5.
    KOiK03351.
    OMAiRVWSLPP.
    OrthoDBiEOG7S21XB.
    PhylomeDBiQ9UJX5.
    TreeFamiTF105443.

    Family and domain databases

    Gene3Di2.130.10.10. 2 hits.
    InterProiIPR024789. APC4.
    IPR024790. APC4_long_dom.
    IPR017169. APC4_metazoa.
    IPR024977. Apc4_WD40_dom.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PANTHERiPTHR13260. PTHR13260. 1 hit.
    PfamiPF12896. Apc4. 1 hit.
    PF12894. Apc4_WD40. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037303. APC4. 1 hit.
    SUPFAMiSSF50978. SSF50978. 2 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UJX5-1) [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

    MLRFPTCFPS FRVVGEKQLP QEIIFLVWSP KRDLIALANT AGEVLLHRLA    50
    SFHRVWSFPP NENTGKEVTC LAWRPDGKLL AFALADTKKI VLCDVEKPES 100
    LHSFSVEAPV SCMHWMEVTV ESSVLTSFYN AEDESNLLLP KLPTLPKNYS 150
    NTSKIFSEEN SDEIIKLLGD VRLNILVLGG SSGFIELYAY GMFKIARVTG 200
    IAGTCLALCL SSDLKSLSVV TEVSTNGASE VSYFQLETNL LYSFLPEVTR 250
    MARKFTHISA LLQYINLSLT CMCEAWEEIL MQMDSRLTKF VQEKNTTTSV 300
    QDEFMHLLLW GKASAELQTL LMNQLTVKGL KKLGQSIESS YSSIQKLVIS 350
    HLQSGSESLL YHLSELKGMA SWKQKYEPLG LDAAGIEEAI TAVGSFILKA 400
    NELLQVIDSS MKNFKAFFRW LYVAMLRMTE DHVLPELNKM TQKDITFVAE 450
    FLTEHFNEAP DLYNRKGKYF NVERVGQYLK DEDDDLVSPP NTEGNQWYDF 500
    LQNSSHLKES PLLFPYYPRK SLHFVKRRME NIIDQCLQKP ADVIGKSMNQ 550
    AICIPLYRDT RSEDSTRRLF KFPFLWNNKT SNLHYLLFTI LEDSLYKMCI 600
    LRRHTDISQS VSNGLIAIKF GSFTYATTEK VRRSIYSCLD AQFYDDETVT 650
    VVLKDTVGRE GRDRLLVQLP LSLVYNSEDS AEYQFTGTYS TRLDEQCSAI 700
    PTRTMHFEKH WRLLESMKAQ YVAGNGFRKV SCVLSSNLRH VRVFEMDIDD 750
    EWELDESSDE EEEASNKPVK IKEEVLSESE AENQQAGAAA LAPEIVIKVE 800
    KLDPELDS 808
    Length:808
    Mass (Da):92,116
    Last modified:September 2, 2008 - v2
    Checksum:i80362CC8D8B2063F
    GO
    Isoform 2 (identifier: Q9UJX5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         542-551: DVIGKSMNQA → VSLKEMHVFV
         552-808: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:551
    Mass (Da):62,639
    Checksum:i16829B75DE9987DF
    GO
    Isoform 3 (identifier: Q9UJX5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         439-439: K → KV

    Note: No experimental confirmation available.

    Show »
    Length:809
    Mass (Da):92,216
    Checksum:iDD0B4899C6501E09
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti286 – 2861R → C in AAF05752. (PubMed:9469815)Curated
    Sequence conflicti293 – 2953EKN → GKD in AAF05752. (PubMed:9469815)Curated
    Sequence conflicti756 – 7561E → G in AAH59383. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti155 – 1551I → V in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035792
    Natural varianti465 – 4651R → Q.
    Corresponds to variant rs34811474 [ dbSNP | Ensembl ].
    VAR_054044
    Natural varianti800 – 8001E → G.
    Corresponds to variant rs11550697 [ dbSNP | Ensembl ].
    VAR_054045

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei439 – 4391K → KV in isoform 3. CuratedVSP_056708
    Alternative sequencei542 – 55110DVIGKSMNQA → VSLKEMHVFV in isoform 2. 1 PublicationVSP_008464
    Alternative sequencei552 – 808257Missing in isoform 2. 1 PublicationVSP_008465Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191338 mRNA. Translation: AAF05752.1.
    AK292336 mRNA. Translation: BAF85025.1.
    CH471069 Genomic DNA. Translation: EAW92839.1.
    BC059383 mRNA. Translation: AAH59383.1.
    AL353932 mRNA. Translation: CAB89245.1.
    CCDSiCCDS3434.1. [Q9UJX5-1]
    PIRiT48682.
    RefSeqiNP_001273685.1. NM_001286756.1.
    NP_037499.2. NM_013367.2. [Q9UJX5-1]
    UniGeneiHs.152173.

    Genome annotation databases

    EnsembliENST00000315368; ENSP00000318775; ENSG00000053900. [Q9UJX5-1]
    ENST00000510092; ENSP00000426654; ENSG00000053900. [Q9UJX5-3]
    GeneIDi29945.
    KEGGihsa:29945.
    UCSCiuc003gro.3. human. [Q9UJX5-1]

    Polymorphism databases

    DMDMi205371737.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF191338 mRNA. Translation: AAF05752.1 .
    AK292336 mRNA. Translation: BAF85025.1 .
    CH471069 Genomic DNA. Translation: EAW92839.1 .
    BC059383 mRNA. Translation: AAH59383.1 .
    AL353932 mRNA. Translation: CAB89245.1 .
    CCDSi CCDS3434.1. [Q9UJX5-1 ]
    PIRi T48682.
    RefSeqi NP_001273685.1. NM_001286756.1.
    NP_037499.2. NM_013367.2. [Q9UJX5-1 ]
    UniGenei Hs.152173.

    3D structure databases

    ProteinModelPortali Q9UJX5.
    SMRi Q9UJX5. Positions 175-215, 721-749.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118982. 49 interactions.
    DIPi DIP-56450N.
    IntActi Q9UJX5. 26 interactions.
    MINTi MINT-4787108.
    STRINGi 9606.ENSP00000318775.

    PTM databases

    PhosphoSitei Q9UJX5.

    Polymorphism databases

    DMDMi 205371737.

    Proteomic databases

    MaxQBi Q9UJX5.
    PaxDbi Q9UJX5.
    PRIDEi Q9UJX5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315368 ; ENSP00000318775 ; ENSG00000053900 . [Q9UJX5-1 ]
    ENST00000510092 ; ENSP00000426654 ; ENSG00000053900 . [Q9UJX5-3 ]
    GeneIDi 29945.
    KEGGi hsa:29945.
    UCSCi uc003gro.3. human. [Q9UJX5-1 ]

    Organism-specific databases

    CTDi 29945.
    GeneCardsi GC04P025462.
    HGNCi HGNC:19990. ANAPC4.
    HPAi CAB032519.
    HPA038395.
    HPA038396.
    MIMi 606947. gene.
    neXtProti NX_Q9UJX5.
    PharmGKBi PA134894250.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248176.
    HOGENOMi HOG000033987.
    HOVERGENi HBG044815.
    InParanoidi Q9UJX5.
    KOi K03351.
    OMAi RVWSLPP.
    OrthoDBi EOG7S21XB.
    PhylomeDBi Q9UJX5.
    TreeFami TF105443.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_1072. Inactivation of APC/C via direct inhibition of the APC/C complex.
    REACT_150471. Separation of Sister Chromatids.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6781. APC/C:Cdc20 mediated degradation of mitotic proteins.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6837. Regulation of APC/C activators between G1/S and early anaphase.
    REACT_6867. Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_6904. Phosphorylation of the APC/C.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi ANAPC4. human.
    GeneWikii ANAPC4.
    GenomeRNAii 29945.
    NextBioi 52611.
    PROi Q9UJX5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UJX5.
    Bgeei Q9UJX5.
    CleanExi HS_ANAPC4.
    Genevestigatori Q9UJX5.

    Family and domain databases

    Gene3Di 2.130.10.10. 2 hits.
    InterProi IPR024789. APC4.
    IPR024790. APC4_long_dom.
    IPR017169. APC4_metazoa.
    IPR024977. Apc4_WD40_dom.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    PANTHERi PTHR13260. PTHR13260. 1 hit.
    Pfami PF12896. Apc4. 1 hit.
    PF12894. Apc4_WD40. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037303. APC4. 1 hit.
    SUPFAMi SSF50978. SSF50978. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a cullin homology region in a subunit of the anaphase-promoting complex."
      Yu H., Peters J.-M., King R.W., Page A.M., Hieter P., Kirschner M.W.
      Science 279:1219-1222(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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).
      Tissue: Placenta.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-808 (ISOFORM 2).
      Tissue: Amygdala.
    6. "Mitotic regulation of the human anaphase-promoting complex by phosphorylation."
      Kraft C., Herzog F., Gieffers C., Mechtler K., Hagting A., Pines J., Peters J.-M.
      EMBO J. 22:6598-6609(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-469 AND SER-779.
    7. "Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex."
      Jin L., Williamson A., Banerjee S., Philipp I., Rape M.
      Cell 133:653-665(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE APC/C.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-757; SER-758; SER-777 AND SER-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a cryo-electron microscopy model of vertebrate APC/C."
      Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A., Engel A., Peters J.-M., Stark H.
      Mol. Cell 20:867-879(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: ELECTRON MICROSCOPY OF THE APC/C.
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-155.

    Entry informationi

    Entry nameiAPC4_HUMAN
    AccessioniPrimary (citable) accession number: Q9UJX5
    Secondary accession number(s): A8K8H1
    , E9PCR4, Q6PCC6, Q9NSH6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: September 2, 2008
    Last modified: October 1, 2014
    This is version 116 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3