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O00487

- PSDE_HUMAN

UniProt

O00487 - PSDE_HUMAN

Protein

26S proteasome non-ATPase regulatory subunit 14

Gene

PSMD14

Organism
Homo sapiens (Human)
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 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi113 – 1131Zinc; catalyticCurated
    Metal bindingi115 – 1151Zinc; catalyticCurated
    Metal bindingi126 – 1261Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. endopeptidase activator activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. metallopeptidase activity Source: UniProtKB
    4. proteasome binding Source: UniProtKB
    5. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    5. apoptotic process Source: Reactome
    6. cellular nitrogen compound metabolic process Source: Reactome
    7. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    8. double-strand break repair via homologous recombination Source: UniProtKB
    9. double-strand break repair via nonhomologous end joining Source: UniProtKB
    10. G1/S transition of mitotic cell cycle Source: Reactome
    11. gene expression Source: Reactome
    12. mitotic cell cycle Source: Reactome
    13. mRNA metabolic process Source: Reactome
    14. negative regulation of apoptotic process Source: Reactome
    15. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    16. positive regulation of endopeptidase activity Source: GOC
    17. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    18. protein K63-linked deubiquitination Source: UniProtKB
    19. protein polyubiquitination Source: Reactome
    20. regulation of apoptotic process Source: Reactome
    21. regulation of cellular amino acid metabolic process Source: Reactome
    22. regulation of proteasomal protein catabolic process Source: UniProtKB
    23. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    24. RNA metabolic process Source: Reactome
    25. small molecule metabolic process Source: Reactome
    26. ubiquitin-dependent protein catabolic process Source: UniProtKB
    27. viral process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    DNA damage, DNA repair, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Protein family/group databases

    MEROPSiM67.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    26S proteasome non-ATPase regulatory subunit 14 (EC:3.4.19.-)
    Alternative name(s):
    26S proteasome regulatory subunit RPN11
    26S proteasome-associated PAD1 homolog 1
    Gene namesi
    Name:PSMD14
    Synonyms:POH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:16889. PSMD14.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProt
    5. proteasome accessory complex Source: UniProtKB
    6. proteasome complex Source: UniProtKB
    7. proteasome regulatory particle, lid subcomplex Source: UniProtKB

    Keywords - Cellular componenti

    Proteasome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi113 – 1153HSH → ASA: Abolishes ubiquitin thioesterase activity, leading to prevent maintenance of JMJD2A/KDM4A on chromatin. 1 Publication

    Organism-specific databases

    PharmGKBiPA134957776.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 31031026S proteasome non-ATPase regulatory subunit 14PRO_0000213952Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei150 – 1501Phosphoserine1 Publication
    Modified residuei224 – 2241Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO00487.
    PaxDbiO00487.
    PeptideAtlasiO00487.
    PRIDEiO00487.

    2D gel databases

    OGPiO00487.
    REPRODUCTION-2DPAGEIPI00024821.

    PTM databases

    PhosphoSiteiO00487.

    Expressioni

    Tissue specificityi

    Widely expressed. Highest levels in heart and skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiO00487.
    BgeeiO00487.
    CleanExiHS_PSMD14.
    GenevestigatoriO00487.

    Organism-specific databases

    HPAiHPA002114.

    Interactioni

    Subunit structurei

    Component of the lid subcomplex of the 19S proteasome regulatory particle complex (also named PA700 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. Interacts with TXNL1.3 Publications

    Protein-protein interaction databases

    BioGridi115508. 65 interactions.
    IntActiO00487. 23 interactions.
    MINTiMINT-5003743.
    STRINGi9606.ENSP00000386541.

    Structurei

    3D structure databases

    ProteinModelPortaliO00487.
    SMRiO00487. Positions 27-302.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 139114MPNAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi113 – 12614JAMM motifAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M67A family. PSMD14 subfamily.Curated
    Contains 1 MPN (JAB/Mov34) domain.Curated

    Phylogenomic databases

    eggNOGiCOG1310.
    HOGENOMiHOG000183690.
    HOVERGENiHBG053742.
    InParanoidiO00487.
    KOiK03030.
    OMAiQDPKKHL.
    OrthoDBiEOG7T7GTF.
    PhylomeDBiO00487.
    TreeFamiTF105748.

    Family and domain databases

    InterProiIPR000555. JAMM/MPN+_dom.
    IPR024969. Rpn11/EIF3F_C.
    [Graphical view]
    PfamiPF01398. JAB. 1 hit.
    PF13012. MitMem_reg. 1 hit.
    [Graphical view]
    SMARTiSM00232. JAB_MPN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O00487-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDRLLRLGGG MPGLGQGPPT DAPAVDTAEQ VYISSLALLK MLKHGRAGVP    50
    MEVMGLMLGE FVDDYTVRVI DVFAMPQSGT GVSVEAVDPV FQAKMLDMLK 100
    QTGRPEMVVG WYHSHPGFGC WLSGVDINTQ QSFEALSERA VAVVVDPIQS 150
    VKGKVVIDAF RLINANMMVL GHEPRQTTSN LGHLNKPSIQ ALIHGLNRHY 200
    YSITINYRKN ELEQKMLLNL HKKSWMEGLT LQDYSEHCKH NESVVKEMLE 250
    LAKNYNKAVE EEDKMTPEQL AIKNVGKQDP KRHLEEHVDV LMTSNIVQCL 300
    AAMLDTVVFK 310
    Length:310
    Mass (Da):34,577
    Last modified:July 1, 1997 - v1
    Checksum:i18ACE876C7682039
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86782 mRNA. Translation: AAC51866.1.
    AK055128 mRNA. Translation: BAG51474.1.
    CH471058 Genomic DNA. Translation: EAX11370.1.
    BC066336 mRNA. Translation: AAH66336.1.
    CCDSiCCDS46437.1.
    RefSeqiNP_005796.1. NM_005805.5.
    UniGeneiHs.740477.

    Genome annotation databases

    EnsembliENST00000409682; ENSP00000386541; ENSG00000115233.
    GeneIDi10213.
    KEGGihsa:10213.
    UCSCiuc002ubu.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86782 mRNA. Translation: AAC51866.1 .
    AK055128 mRNA. Translation: BAG51474.1 .
    CH471058 Genomic DNA. Translation: EAX11370.1 .
    BC066336 mRNA. Translation: AAH66336.1 .
    CCDSi CCDS46437.1.
    RefSeqi NP_005796.1. NM_005805.5.
    UniGenei Hs.740477.

    3D structure databases

    ProteinModelPortali O00487.
    SMRi O00487. Positions 27-302.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115508. 65 interactions.
    IntActi O00487. 23 interactions.
    MINTi MINT-5003743.
    STRINGi 9606.ENSP00000386541.

    Chemistry

    BindingDBi O00487.
    ChEMBLi CHEMBL2007629.

    Protein family/group databases

    MEROPSi M67.001.

    PTM databases

    PhosphoSitei O00487.

    2D gel databases

    OGPi O00487.
    REPRODUCTION-2DPAGE IPI00024821.

    Proteomic databases

    MaxQBi O00487.
    PaxDbi O00487.
    PeptideAtlasi O00487.
    PRIDEi O00487.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000409682 ; ENSP00000386541 ; ENSG00000115233 .
    GeneIDi 10213.
    KEGGi hsa:10213.
    UCSCi uc002ubu.3. human.

    Organism-specific databases

    CTDi 10213.
    GeneCardsi GC02P162164.
    HGNCi HGNC:16889. PSMD14.
    HPAi HPA002114.
    MIMi 607173. gene.
    neXtProti NX_O00487.
    PharmGKBi PA134957776.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1310.
    HOGENOMi HOG000183690.
    HOVERGENi HBG053742.
    InParanoidi O00487.
    KOi K03030.
    OMAi QDPKKHL.
    OrthoDBi EOG7T7GTF.
    PhylomeDBi O00487.
    TreeFami TF105748.

    Enzyme and pathway databases

    Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
    REACT_111178. ER-Phagosome pathway.
    REACT_1156. Orc1 removal from chromatin.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13565. Regulation of ornithine decarboxylase (ODC).
    REACT_150471. Separation of Sister Chromatids.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_200766. degradation of AXIN.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Miscellaneous databases

    GeneWikii PSMD14.
    GenomeRNAii 10213.
    NextBioi 38668.
    PROi O00487.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00487.
    Bgeei O00487.
    CleanExi HS_PSMD14.
    Genevestigatori O00487.

    Family and domain databases

    InterProi IPR000555. JAMM/MPN+_dom.
    IPR024969. Rpn11/EIF3F_C.
    [Graphical view ]
    Pfami PF01398. JAB. 1 hit.
    PF13012. MitMem_reg. 1 hit.
    [Graphical view ]
    SMARTi SM00232. JAB_MPN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Resistance to diverse drugs and ultraviolet light conferred by overexpression of a novel human 26 S proteasome subunit."
      Spataro V., Toda T., Craig R., Seeger M., Dubiel W., Harris A.L., Norbury C.
      J. Biol. Chem. 272:30470-30475(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Lung.
    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].
      Tissue: Brain.
    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].
      Tissue: Testis.
    5. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 199-208, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    6. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
      Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
      Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    7. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. "K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1."
      Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., Cohen R.E.
      EMBO J. 28:621-631(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROBABLE FUNCTION, IDENTIFICATION IN THE PROTEASOME.
    9. "Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasome."
      Andersen K.M., Madsen L., Prag S., Johnsen A.H., Semple C.A., Hendil K.B., Hartmann-Petersen R.
      J. Biol. Chem. 284:15246-15254(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TXNL1.
    10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response."
      Butler L.R., Densham R.M., Jia J., Garvin A.J., Stone H.R., Shah V., Weekes D., Festy F., Beesley J., Morris J.R.
      EMBO J. 31:3918-3934(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE PROTEASOME, MUTAGENESIS OF 113-HIS--HIS-115.

    Entry informationi

    Entry nameiPSDE_HUMAN
    AccessioniPrimary (citable) accession number: O00487
    Secondary accession number(s): B3KNW2, O00176
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 129 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3