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P49593

- PPM1F_HUMAN

UniProt

P49593 - PPM1F_HUMAN

Protein

Protein phosphatase 1F

Gene

PPM1F

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (01 Nov 2002)
      Previous versions | rss
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    Functioni

    Dephosphorylates and concomitantly deactivates CaM-kinase II activated upon autophosphorylation, and CaM-kinases IV and I activated upon phosphorylation by CaM-kinase kinase. Promotes apoptosis.

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi198 – 1981Manganese 1By similarity
    Metal bindingi198 – 1981Manganese 2By similarity
    Metal bindingi199 – 1991Manganese 1; via carbonyl oxygenBy similarity
    Metal bindingi360 – 3601Manganese 2By similarity
    Metal bindingi404 – 4041Manganese 2By similarity

    GO - Molecular functioni

    1. calmodulin-dependent protein phosphatase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. phosphatase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein serine/threonine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to drug Source: UniProtKB
    2. histone dephosphorylation Source: Ensembl
    3. intrinsic apoptotic signaling pathway Source: UniProtKB
    4. negative regulation of peptidyl-serine phosphorylation Source: UniProtKB
    5. negative regulation of protein kinase activity Source: UniProtKB
    6. negative regulation of protein kinase activity by regulation of protein phosphorylation Source: UniProtKB
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. peptidyl-threonine dephosphorylation Source: UniProtKB
    9. positive regulation of cell-substrate adhesion Source: UniProtKB
    10. positive regulation of chemotaxis Source: UniProtKB
    11. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
    12. positive regulation of epithelial cell migration Source: UniProtKB
    13. positive regulation of focal adhesion assembly Source: UniProtKB
    14. positive regulation of gene expression Source: UniProtKB
    15. positive regulation of growth Source: UniProtKB
    16. positive regulation of stress fiber assembly Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 1F (EC:3.1.3.16)
    Alternative name(s):
    Ca(2+)/calmodulin-dependent protein kinase phosphatase
    Short name:
    CaM-kinase phosphatase
    Short name:
    CaMKPase
    Partner of PIX 2
    Protein fem-2 homolog
    Short name:
    hFem-2
    Gene namesi
    Name:PPM1F
    Synonyms:KIAA0015, POPX2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:19388. PPM1F.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. perinuclear region of cytoplasm Source: Ensembl
    3. protein complex Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134935566.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 454454Protein phosphatase 1FPRO_0000057758Add
    BLAST

    Proteomic databases

    MaxQBiP49593.
    PaxDbiP49593.
    PeptideAtlasiP49593.
    PRIDEiP49593.

    2D gel databases

    OGPiP49593.

    PTM databases

    PhosphoSiteiP49593.

    Expressioni

    Gene expression databases

    ArrayExpressiP49593.
    BgeeiP49593.
    CleanExiHS_PPM1F.
    GenevestigatoriP49593.

    Organism-specific databases

    HPAiHPA030989.
    HPA030990.

    Interactioni

    Subunit structurei

    Associates with FEM1B.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Camkk2Q8C0783EBI-719945,EBI-937199From a different organism.
    DIAPH1O606103EBI-719945,EBI-3959709
    FEM1BQ9UK732EBI-719945,EBI-310482

    Protein-protein interaction databases

    BioGridi115005. 11 interactions.
    IntActiP49593. 10 interactions.
    MINTiMINT-1397077.
    STRINGi9606.ENSP00000263212.

    Structurei

    3D structure databases

    ProteinModelPortaliP49593.
    SMRiP49593. Positions 84-445.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi101 – 1077Poly-Glu

    Sequence similaritiesi

    Belongs to the PP2C family.Curated

    Phylogenomic databases

    eggNOGiCOG0631.
    HOGENOMiHOG000232094.
    HOVERGENiHBG053656.
    InParanoidiP49593.
    KOiK17502.
    OMAiGDVFQKP.
    OrthoDBiEOG7D2FDH.
    PhylomeDBiP49593.
    TreeFamiTF317617.

    Family and domain databases

    Gene3Di3.60.40.10. 1 hit.
    InterProiIPR001932. PP2C-like_dom.
    IPR000222. PP2C_Mn2_Asp60_BS.
    IPR015655. Protein_Pase_2C.
    [Graphical view]
    PANTHERiPTHR13832. PTHR13832. 1 hit.
    PfamiPF00481. PP2C. 1 hit.
    [Graphical view]
    SMARTiSM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view]
    SUPFAMiSSF81606. SSF81606. 1 hit.
    PROSITEiPS01032. PP2C. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49593-1) [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

    MSSGAPQKSS PMASGAEETP GFLDTLLQDF PALLNPEDPL PWKAPGTVLS    50
    QEEVEGELAE LAMGFLGSRK APPPLAAALA HEAVSQLLQT DLSEFRKLPR 100
    EEEEEEEDDD EEEKAPVTLL DAQSLAQSFF NRLWEVAGQW QKQVPLAARA 150
    SQRQWLVSIH AIRNTRRKME DRHVSLPSFN QLFGLSDPVN RAYFAVFDGH 200
    GGVDAARYAA VHVHTNAARQ PELPTDPEGA LREAFRRTDQ MFLRKAKRER 250
    LQSGTTGVCA LIAGATLHVA WLGDSQVILV QQGQVVKLME PHRPERQDEK 300
    ARIEALGGFV SHMDCWRVNG TLAVSRAIGD VFQKPYVSGE ADAASRALTG 350
    SEDYLLLACD GFFDVVPHQE VVGLVQSHLT RQQGSGLRVA EELVAAARER 400
    GSHDNITVMV VFLRDPQELL EGGNQGEGDP QAEGRRQDLP SSLPEPETQA 450
    PPRS 454
    Length:454
    Mass (Da):49,831
    Last modified:November 1, 2002 - v3
    Checksum:i2B49262333D4C9CF
    GO
    Isoform 2 (identifier: P49593-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: MSSGAPQKSSPMASG → MGLCPSTRETAPPAV
         16-119: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:350
    Mass (Da):38,518
    Checksum:i3762283304FF2BA8
    GO

    Sequence cautioni

    The sequence BAA02803.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti202 – 2021G → D in AAL15579. (PubMed:11559703)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti132 – 1321R → C.
    Corresponds to variant rs9610645 [ dbSNP | Ensembl ].
    VAR_050620
    Natural varianti296 – 2961R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036520
    Natural varianti417 – 4171Q → K in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036521
    Natural varianti420 – 4201L → R.1 Publication
    Corresponds to variant rs2070507 [ dbSNP | Ensembl ].
    VAR_024580

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1515MSSGA…PMASG → MGLCPSTRETAPPAV in isoform 2. 1 PublicationVSP_056483Add
    BLAST
    Alternative sequencei16 – 119104Missing in isoform 2. 1 PublicationVSP_056484Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF305840 mRNA. Translation: AAL15579.1.
    AF520615 mRNA. Translation: AAM76059.1.
    D13640 mRNA. Translation: BAA02803.2. Different initiation.
    AK291628 mRNA. Translation: BAF84317.1.
    AK294557 mRNA. Translation: BAH11809.1.
    AP000555 Genomic DNA. No translation available.
    D86995 Genomic DNA. No translation available.
    D87012 Genomic DNA. No translation available.
    D87019 Genomic DNA. No translation available.
    CCDSiCCDS13796.1.
    RefSeqiNP_055449.1. NM_014634.3.
    UniGeneiHs.112728.

    Genome annotation databases

    EnsembliENST00000263212; ENSP00000263212; ENSG00000100034.
    ENST00000538191; ENSP00000439915; ENSG00000100034.
    GeneIDi9647.
    KEGGihsa:9647.
    UCSCiuc002zvp.2. human.

    Polymorphism databases

    DMDMi24638458.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF305840 mRNA. Translation: AAL15579.1 .
    AF520615 mRNA. Translation: AAM76059.1 .
    D13640 mRNA. Translation: BAA02803.2 . Different initiation.
    AK291628 mRNA. Translation: BAF84317.1 .
    AK294557 mRNA. Translation: BAH11809.1 .
    AP000555 Genomic DNA. No translation available.
    D86995 Genomic DNA. No translation available.
    D87012 Genomic DNA. No translation available.
    D87019 Genomic DNA. No translation available.
    CCDSi CCDS13796.1.
    RefSeqi NP_055449.1. NM_014634.3.
    UniGenei Hs.112728.

    3D structure databases

    ProteinModelPortali P49593.
    SMRi P49593. Positions 84-445.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115005. 11 interactions.
    IntActi P49593. 10 interactions.
    MINTi MINT-1397077.
    STRINGi 9606.ENSP00000263212.

    PTM databases

    PhosphoSitei P49593.

    Polymorphism databases

    DMDMi 24638458.

    2D gel databases

    OGPi P49593.

    Proteomic databases

    MaxQBi P49593.
    PaxDbi P49593.
    PeptideAtlasi P49593.
    PRIDEi P49593.

    Protocols and materials databases

    DNASUi 9647.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263212 ; ENSP00000263212 ; ENSG00000100034 .
    ENST00000538191 ; ENSP00000439915 ; ENSG00000100034 .
    GeneIDi 9647.
    KEGGi hsa:9647.
    UCSCi uc002zvp.2. human.

    Organism-specific databases

    CTDi 9647.
    GeneCardsi GC22M022273.
    H-InvDB HIX0027933.
    HGNCi HGNC:19388. PPM1F.
    HPAi HPA030989.
    HPA030990.
    neXtProti NX_P49593.
    PharmGKBi PA134935566.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0631.
    HOGENOMi HOG000232094.
    HOVERGENi HBG053656.
    InParanoidi P49593.
    KOi K17502.
    OMAi GDVFQKP.
    OrthoDBi EOG7D2FDH.
    PhylomeDBi P49593.
    TreeFami TF317617.

    Miscellaneous databases

    ChiTaRSi PPM1F. human.
    GeneWikii PPM1F.
    GenomeRNAii 9647.
    NextBioi 36211.
    PROi P49593.

    Gene expression databases

    ArrayExpressi P49593.
    Bgeei P49593.
    CleanExi HS_PPM1F.
    Genevestigatori P49593.

    Family and domain databases

    Gene3Di 3.60.40.10. 1 hit.
    InterProi IPR001932. PP2C-like_dom.
    IPR000222. PP2C_Mn2_Asp60_BS.
    IPR015655. Protein_Pase_2C.
    [Graphical view ]
    PANTHERi PTHR13832. PTHR13832. 1 hit.
    Pfami PF00481. PP2C. 1 hit.
    [Graphical view ]
    SMARTi SM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81606. SSF81606. 1 hit.
    PROSITEi PS01032. PP2C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Caenorhabditis elegans sex-determining protein fem-2 and its human homologue, hFEM-2, are Ca2+/calmodulin-dependent protein kinase phosphatases that promote apoptosis."
      Tan K.M.L., Chan S.-L., Tan K.O., Yu V.C.
      J. Biol. Chem. 276:44193-44202(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH FEM1B.
    2. "The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family."
      Koh C.-G., Tan E.-J., Manser E., Lim L.
      Curr. Biol. 12:317-321(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
      Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
      DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    4. "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] (ISOFORMS 1 AND 2), VARIANT ARG-420.
      Tissue: Amygdala and Placenta.
    5. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-296 AND LYS-417.

    Entry informationi

    Entry nameiPPM1F_HUMAN
    AccessioniPrimary (citable) accession number: P49593
    Secondary accession number(s): A8K6G3, B7Z2C3, Q96PM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: November 1, 2002
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 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 22
      Human chromosome 22: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3