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Protein

Carboxypeptidase Z

Gene

CPZ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing.3 Publications

Cofactori

Zn2+By similarity

Enzyme regulationi

Inhibited by 2-mercaptomethyl-3-guanidinoethylthiopropanoic acid (MGTA) and guanidinoethylmercaptosuccinic acid (GEMSA). Inhibited by chelating agents such as EDTA and EGTA.1 Publication

Kineticsi

  1. KM=2 mM for dansyl-Phe-Ala-Arg2 Publications
  2. KM=2 mM for dansyl-Pro-Ala-Arg2 Publications

    pH dependencei

    Optimum pH is 7.8.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi248 – 2481Zinc; catalyticBy similarity
    Metal bindingi251 – 2511Zinc; catalyticBy similarity
    Metal bindingi380 – 3801Zinc; catalyticBy similarity
    Active sitei472 – 4721Proton donor/acceptorBy similarity

    GO - Molecular functioni

    • metallocarboxypeptidase activity Source: ProtInc
    • serine-type carboxypeptidase activity Source: GO_Central
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • peptide metabolic process Source: GO_Central
    • protein processing Source: GO_Central
    • proteolysis Source: ProtInc
    • Wnt signaling pathway Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Wnt signaling pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM14.012.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase Z (EC:3.4.17.-)
    Short name:
    CPZ
    Gene namesi
    Name:CPZ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:2333. CPZ.

    Subcellular locationi

    GO - Cellular componenti

    • extracellular exosome Source: UniProtKB
    • extracellular space Source: GO_Central
    • proteinaceous extracellular matrix Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26854.

    Polymorphism and mutation databases

    BioMutaiCPZ.
    DMDMi296434423.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence analysisAdd
    BLAST
    Chaini19 – 652634Carboxypeptidase ZBy similarityPRO_0000252456Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi43 ↔ 109PROSITE-ProRule annotation
    Disulfide bondi51 ↔ 102PROSITE-ProRule annotation
    Disulfide bondi93 ↔ 129PROSITE-ProRule annotation
    Disulfide bondi118 ↔ 157PROSITE-ProRule annotation
    Disulfide bondi122 ↔ 146PROSITE-ProRule annotation
    Glycosylationi281 – 2811N-linked (GlcNAc...)Sequence analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ66K79.
    PRIDEiQ66K79.

    Expressioni

    Tissue specificityi

    In placenta, it is present within invasive trophoblasts and in the surrounding extracellular space. Also present in amnion cells, but is not readily apparent in the extracellular matrix of this cell type. Present in normal pituitary gland and neoplastic pituitary gland (especially POMC-, GH- and PRL-producing adenomas) (at protein level). Widely expressed.3 Publications

    Gene expression databases

    BgeeiQ66K79.
    CleanExiHS_CPZ.
    ExpressionAtlasiQ66K79. baseline and differential.
    GenevisibleiQ66K79. HS.

    Organism-specific databases

    HPAiHPA029082.
    HPA029083.

    Interactioni

    Protein-protein interaction databases

    BioGridi114102. 3 interactions.
    STRINGi9606.ENSP00000354255.

    Structurei

    3D structure databases

    ProteinModelPortaliQ66K79.
    SMRiQ66K79. Positions 43-148, 183-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 160134FZPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M14 family.Curated
    Contains 1 FZ (frizzled) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG2649. Eukaryota.
    ENOG410XX0H. LUCA.
    GeneTreeiENSGT00760000119124.
    HOGENOMiHOG000232185.
    HOVERGENiHBG003410.
    InParanoidiQ66K79.
    KOiK13022.
    OMAiIEFSSRP.
    OrthoDBiEOG7B8S32.
    PhylomeDBiQ66K79.
    TreeFamiTF315592.

    Family and domain databases

    Gene3Di1.10.2000.10. 1 hit.
    2.60.40.1120. 1 hit.
    InterProiIPR008969. CarboxyPept-like_regulatory.
    IPR014766. CarboxyPept_regulatory_dom.
    IPR020067. Frizzled_dom.
    IPR000834. Peptidase_M14.
    [Graphical view]
    PfamiPF01392. Fz. 1 hit.
    PF00246. Peptidase_M14. 1 hit.
    [Graphical view]
    PRINTSiPR00765. CRBOXYPTASEA.
    SMARTiSM00063. FRI. 1 hit.
    SM00631. Zn_pept. 1 hit.
    [Graphical view]
    SUPFAMiSSF49464. SSF49464. 1 hit.
    SSF63501. SSF63501. 1 hit.
    PROSITEiPS00133. CARBOXYPEPT_ZN_2. 1 hit.
    PS50038. FZ. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q66K79-1) [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

            10         20         30         40         50
    MPPPLPLLLL TVLVVAAARP GCEFERNPAG ECHRPPAADS ATCVDLQLRT
    60 70 80 90 100
    CSDAAYNHTT FPNLLQHRSW EVVEASSEYI LLSVLHQLLE GQCNPDLRLL
    110 120 130 140 150
    GCAVLAPRCE GGWVRRPCRH ICEGLREVCQ PAFDAIDMAW PYFLDCHRYF
    160 170 180 190 200
    TREDEGCYDP LEKLRGGLEA DEALPSGLPP TFIRFSHHSY AQMVRVLRRT
    210 220 230 240 250
    ASRCAHVART YSIGRSFDGR ELLVIEFSSR PGQHELMEPE VKLIGNIHGN
    260 270 280 290 300
    EVAGREMLIY LAQYLCSEYL LGNPRIQRLL NTTRIHLLPS MNPDGYEVAA
    310 320 330 340 350
    AEGAGYNGWT SGRQNAQNLD LNRNFPDLTS EYYRLAETRG ARSDHIPIPQ
    360 370 380 390 400
    HYWWGKVAPE TKAIMKWMQT IPFVLSASLH GGDLVVSYPF DFSKHPQEEK
    410 420 430 440 450
    MFSPTPDEKM FKLLSRAYAD VHPMMMDRSE NRCGGNFLKR GSIINGADWY
    460 470 480 490 500
    SFTGGMSDFN YLHTNCFEIT VELGCVKFPP EEALYILWQH NKESLLNFVE
    510 520 530 540 550
    TVHRGIKGVV TDKFGKPVKN ARISVKGIRH DITTAPDGDY WRLLPPGIHI
    560 570 580 590 600
    VIAQAPGYAK VIKKVIIPAR MKRAGRVDFI LQPLGMGPKN FIHGLRRTGP
    610 620 630 640 650
    HDPLGGASSL GEATEPDPLR ARRQPSADGS KPWWWSYFTS LSTHRPRWLL

    KY
    Length:652
    Mass (Da):73,655
    Last modified:May 18, 2010 - v2
    Checksum:iBFA1EA7753E63F98
    GO
    Isoform 2 (identifier: Q66K79-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         30-40: Missing.

    Show »
    Length:641
    Mass (Da):72,534
    Checksum:iE88E3425C36F1576
    GO
    Isoform 3 (identifier: Q66K79-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-137: Missing.

    Show »
    Length:515
    Mass (Da):58,591
    Checksum:i50FB57968AB4B212
    GO

    Sequence cautioni

    The sequence BAB71147.1 differs from that shown. Reason: Frameshift at position 358. Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti200 – 2001T → M in BC006393 (PubMed:15489334).Curated
    Sequence conflicti291 – 2911M → I in AAB58911 (PubMed:9099699).Curated
    Sequence conflicti523 – 5231I → T in BAB71147 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti5 – 51L → P.2 Publications
    Corresponds to variant rs2302583 [ dbSNP | Ensembl ].
    VAR_027883
    Natural varianti6 – 61P → L.1 Publication
    Corresponds to variant rs34964084 [ dbSNP | Ensembl ].
    VAR_047244
    Natural varianti130 – 1301Q → L.
    Corresponds to variant rs35993494 [ dbSNP | Ensembl ].
    VAR_047245
    Natural varianti486 – 4861I → T.2 Publications
    Corresponds to variant rs7378066 [ dbSNP | Ensembl ].
    VAR_047246
    Natural varianti501 – 5011T → M.
    Corresponds to variant rs9991535 [ dbSNP | Ensembl ].
    VAR_027884

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 137137Missing in isoform 3. 1 PublicationVSP_040356Add
    BLAST
    Alternative sequencei30 – 4011Missing in isoform 2. 1 PublicationVSP_020983Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U83411 mRNA. Translation: AAB58911.1.
    AK056317 mRNA. Translation: BAB71147.1. Frameshift.
    AC105345 Genomic DNA. No translation available.
    BC006393 mRNA. No translation available.
    BC080539 mRNA. Translation: AAH80539.1.
    CCDSiCCDS33953.1. [Q66K79-1]
    CCDS3404.1. [Q66K79-2]
    CCDS43212.1. [Q66K79-3]
    RefSeqiNP_001014447.1. NM_001014447.2.
    NP_001014448.1. NM_001014448.2.
    NP_003643.2. NM_003652.3.
    UniGeneiHs.61995.

    Genome annotation databases

    EnsembliENST00000315782; ENSP00000315074; ENSG00000109625. [Q66K79-2]
    ENST00000360986; ENSP00000354255; ENSG00000109625. [Q66K79-1]
    ENST00000382480; ENSP00000371920; ENSG00000109625. [Q66K79-3]
    GeneIDi8532.
    KEGGihsa:8532.
    UCSCiuc003glm.4. human. [Q66K79-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U83411 mRNA. Translation: AAB58911.1.
    AK056317 mRNA. Translation: BAB71147.1. Frameshift.
    AC105345 Genomic DNA. No translation available.
    BC006393 mRNA. No translation available.
    BC080539 mRNA. Translation: AAH80539.1.
    CCDSiCCDS33953.1. [Q66K79-1]
    CCDS3404.1. [Q66K79-2]
    CCDS43212.1. [Q66K79-3]
    RefSeqiNP_001014447.1. NM_001014447.2.
    NP_001014448.1. NM_001014448.2.
    NP_003643.2. NM_003652.3.
    UniGeneiHs.61995.

    3D structure databases

    ProteinModelPortaliQ66K79.
    SMRiQ66K79. Positions 43-148, 183-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114102. 3 interactions.
    STRINGi9606.ENSP00000354255.

    Protein family/group databases

    MEROPSiM14.012.

    Polymorphism and mutation databases

    BioMutaiCPZ.
    DMDMi296434423.

    Proteomic databases

    PaxDbiQ66K79.
    PRIDEiQ66K79.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000315782; ENSP00000315074; ENSG00000109625. [Q66K79-2]
    ENST00000360986; ENSP00000354255; ENSG00000109625. [Q66K79-1]
    ENST00000382480; ENSP00000371920; ENSG00000109625. [Q66K79-3]
    GeneIDi8532.
    KEGGihsa:8532.
    UCSCiuc003glm.4. human. [Q66K79-1]

    Organism-specific databases

    CTDi8532.
    GeneCardsiCPZ.
    HGNCiHGNC:2333. CPZ.
    HPAiHPA029082.
    HPA029083.
    MIMi603105. gene.
    neXtProtiNX_Q66K79.
    PharmGKBiPA26854.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2649. Eukaryota.
    ENOG410XX0H. LUCA.
    GeneTreeiENSGT00760000119124.
    HOGENOMiHOG000232185.
    HOVERGENiHBG003410.
    InParanoidiQ66K79.
    KOiK13022.
    OMAiIEFSSRP.
    OrthoDBiEOG7B8S32.
    PhylomeDBiQ66K79.
    TreeFamiTF315592.

    Miscellaneous databases

    GeneWikiiCPZ_(gene).
    GenomeRNAii8532.
    PROiQ66K79.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ66K79.
    CleanExiHS_CPZ.
    ExpressionAtlasiQ66K79. baseline and differential.
    GenevisibleiQ66K79. HS.

    Family and domain databases

    Gene3Di1.10.2000.10. 1 hit.
    2.60.40.1120. 1 hit.
    InterProiIPR008969. CarboxyPept-like_regulatory.
    IPR014766. CarboxyPept_regulatory_dom.
    IPR020067. Frizzled_dom.
    IPR000834. Peptidase_M14.
    [Graphical view]
    PfamiPF01392. Fz. 1 hit.
    PF00246. Peptidase_M14. 1 hit.
    [Graphical view]
    PRINTSiPR00765. CRBOXYPTASEA.
    SMARTiSM00063. FRI. 1 hit.
    SM00631. Zn_pept. 1 hit.
    [Graphical view]
    SUPFAMiSSF49464. SSF49464. 1 hit.
    SSF63501. SSF63501. 1 hit.
    PROSITEiPS00133. CARBOXYPEPT_ZN_2. 1 hit.
    PS50038. FZ. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and expression of human carboxypeptidase Z, a novel metallocarboxypeptidase."
      Song L., Fricker L.D.
      J. Biol. Chem. 272:10543-10550(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY, VARIANTS PRO-5; LEU-6 AND THR-486.
    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: Teratocarcinoma.
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORMS 1 AND 3), VARIANTS PRO-5 AND THR-486.
      Tissue: Muscle.
    5. "Purification and characterization of human metallocarboxypeptidase Z."
      Novikova E.G., Fricker L.D.
      Biochem. Biophys. Res. Commun. 256:564-568(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    6. "Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues."
      Novikova E.G., Reznik S.E., Varlamov O., Fricker L.D.
      J. Biol. Chem. 275:4865-4870(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    7. "Carboxypeptidases from A to Z: implications in embryonic development and Wnt binding."
      Reznik S.E., Fricker L.D.
      Cell. Mol. Life Sci. 58:1790-1804(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Immunohistochemical localization of carboxypeptidases D, E, and Z in pituitary adenomas and normal human pituitary."
      Fan X., Olson S.J., Blevins L.S., Allen G.S., Johnson M.D.
      J. Histochem. Cytochem. 50:1509-1516(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiCBPZ_HUMAN
    AccessioniPrimary (citable) accession number: Q66K79
    Secondary accession number(s): O00520, Q96MX2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: May 18, 2010
    Last modified: June 8, 2016
    This is version 100 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.