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P12544

- GRAA_HUMAN

UniProt

P12544 - GRAA_HUMAN

Protein

Granzyme A

Gene

GZMA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent cell death with morphological features of apoptosis when delivered into the target cell through the immunological synapse. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA.4 Publications

    Catalytic activityi

    Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin. Preferential cleavage: -Arg-|-Xaa-, -Lys-|-Xaa- >> -Phe-|-Xaa- in small molecule substrates.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei69 – 691Charge relay system
    Active sitei114 – 1141Charge relay system
    Active sitei212 – 2121Charge relay system

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein homodimerization activity Source: UniProtKB
    3. serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB
    2. cytolysis Source: UniProtKB-KW
    3. immune response Source: UniProtKB
    4. negative regulation of DNA binding Source: UniProtKB
    5. negative regulation of endodeoxyribonuclease activity Source: UniProtKB
    6. negative regulation of oxidoreductase activity Source: UniProtKB
    7. positive regulation of apoptotic process Source: UniProtKB
    8. proteolysis involved in cellular protein catabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Apoptosis, Cytolysis

    Enzyme and pathway databases

    BRENDAi3.4.21.78. 2681.

    Protein family/group databases

    MEROPSiS01.135.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Granzyme A (EC:3.4.21.78)
    Alternative name(s):
    CTL tryptase
    Cytotoxic T-lymphocyte proteinase 1
    Fragmentin-1
    Granzyme-1
    Hanukkah factor
    Short name:
    H factor
    Short name:
    HF
    Gene namesi
    Name:GZMA
    Synonyms:CTLA3, HFSP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:4708. GZMA.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. immunological synapse Source: UniProtKB
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29086.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626In isoform alphaAdd
    BLAST
    Propeptidei27 – 282Activation peptide (in isoform alpha)3 PublicationsPRO_0000027393
    Chaini29 – 262234Granzyme APRO_0000027394Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 70
    Disulfide bondi148 ↔ 218
    Glycosylationi170 – 1701N-linked (GlcNAc...)1 Publication
    Disulfide bondi179 ↔ 197
    Disulfide bondi208 ↔ 234

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP12544.
    PaxDbiP12544.
    PRIDEiP12544.

    PTM databases

    PhosphoSiteiP12544.

    Expressioni

    Inductioni

    Dexamethasone (DEX) induces expression of isoform beta and represses expression of isoform alpha. The alteration in expression is mediated by binding of glucocorticoid receptor to independent promoters adjacent to the alternative first exons of isoform alpha and isoform beta.1 Publication

    Gene expression databases

    BgeeiP12544.
    CleanExiHS_GZMA.
    GenevestigatoriP12544.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Interacts with APEX1.3 Publications

    Protein-protein interaction databases

    BioGridi109256. 17 interactions.
    IntActiP12544. 4 interactions.
    STRINGi9606.ENSP00000274306.

    Structurei

    Secondary structure

    1
    262
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi43 – 475
    Beta strandi49 – 513
    Beta strandi53 – 608
    Beta strandi63 – 664
    Beta strandi77 – 815
    Beta strandi83 – 875
    Beta strandi93 – 953
    Beta strandi97 – 1026
    Turni108 – 1103
    Beta strandi116 – 1227
    Beta strandi127 – 1304
    Beta strandi147 – 1548
    Beta strandi156 – 1605
    Beta strandi167 – 1748
    Helixi176 – 1794
    Turni182 – 1898
    Beta strandi195 – 1995
    Beta strandi215 – 2184
    Beta strandi221 – 2288
    Beta strandi241 – 2455
    Helixi248 – 25811

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1HF1model-A29-262[»]
    1OP8X-ray2.50A/B/C/D/E/F29-262[»]
    1ORFX-ray2.40A29-262[»]
    ProteinModelPortaliP12544.
    SMRiP12544. Positions 29-260.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12544.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 259231Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family. Granzyme subfamily.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000251820.
    HOVERGENiHBG013304.
    InParanoidiP12544.
    KOiK01352.
    OMAiWIIMTIK.
    OrthoDBiEOG7W9RVH.
    PhylomeDBiP12544.
    TreeFamiTF333630.

    Family and domain databases

    InterProiIPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    PROSITEiPS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative promoter usage. Align

    Isoform alpha (identifier: P12544-1) [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

    MRNSYRFLAS SLSVVVSLLL IPEDVCEKII GGNEVTPHSR PYMVLLSLDR    50
    KTICAGALIA KDWVLTAAHC NLNKRSQVIL GAHSITREEP TKQIMLVKKE 100
    FPYPCYDPAT REGDLKLLQL MEKAKINKYV TILHLPKKGD DVKPGTMCQV 150
    AGWGRTHNSA SWSDTLREVN ITIIDRKVCN DRNHYNFNPV IGMNMVCAGS 200
    LRGGRDSCNG DSGSPLLCEG VFRGVTSFGL ENKCGDPRGP GVYILLSKKH 250
    LNWIIMTIKG AV 262
    Length:262
    Mass (Da):28,999
    Last modified:January 11, 2011 - v2
    Checksum:iFD773628BA6F301B
    GO
    Isoform beta (identifier: P12544-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: Missing.
         18-23: LLLIPE → MTKGLR

    Show »
    Length:245
    Mass (Da):27,109
    Checksum:i7489DB5C158483F6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 342NE → DT no nucleotide entry (PubMed:17180578)Curated
    Sequence conflicti36 – 361T → V no nucleotide entry (PubMed:17180578)Curated
    Sequence conflicti47 – 471S → K no nucleotide entry (PubMed:17180578)Curated
    Sequence conflicti49 – 524DRKT → KPDS no nucleotide entry (PubMed:17180578)Curated
    Sequence conflicti62 – 621D → N no nucleotide entry (PubMed:17180578)Curated
    Sequence conflicti71 – 722NL → IP no nucleotide entry (PubMed:17180578)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti121 – 1211M → T.3 Publications
    Corresponds to variant rs3104233 [ dbSNP | Ensembl ].
    VAR_024291

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1717Missing in isoform beta. 1 PublicationVSP_038571Add
    BLAST
    Alternative sequencei18 – 236LLLIPE → MTKGLR in isoform beta. 1 PublicationVSP_038572

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M18737 mRNA. Translation: AAA52647.1.
    CR456968 mRNA. Translation: CAG33249.1.
    AC091977 Genomic DNA. No translation available.
    BC015739 mRNA. Translation: AAH15739.1.
    AB284134 mRNA. Translation: BAF56159.1.
    U40006 Genomic DNA. Translation: AAD00009.1.
    CCDSiCCDS3965.1. [P12544-1]
    PIRiA31372.
    RefSeqiNP_006135.1. NM_006144.3.
    UniGeneiHs.90708.

    Genome annotation databases

    EnsembliENST00000274306; ENSP00000274306; ENSG00000145649. [P12544-1]
    GeneIDi3001.
    KEGGihsa:3001.
    UCSCiuc003jpm.3. human. [P12544-1]

    Polymorphism databases

    DMDMi317373360.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, 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
    M18737 mRNA. Translation: AAA52647.1 .
    CR456968 mRNA. Translation: CAG33249.1 .
    AC091977 Genomic DNA. No translation available.
    BC015739 mRNA. Translation: AAH15739.1 .
    AB284134 mRNA. Translation: BAF56159.1 .
    U40006 Genomic DNA. Translation: AAD00009.1 .
    CCDSi CCDS3965.1. [P12544-1 ]
    PIRi A31372.
    RefSeqi NP_006135.1. NM_006144.3.
    UniGenei Hs.90708.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1HF1 model - A 29-262 [» ]
    1OP8 X-ray 2.50 A/B/C/D/E/F 29-262 [» ]
    1ORF X-ray 2.40 A 29-262 [» ]
    ProteinModelPortali P12544.
    SMRi P12544. Positions 29-260.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109256. 17 interactions.
    IntActi P12544. 4 interactions.
    STRINGi 9606.ENSP00000274306.

    Chemistry

    ChEMBLi CHEMBL4307.

    Protein family/group databases

    MEROPSi S01.135.

    PTM databases

    PhosphoSitei P12544.

    Polymorphism databases

    DMDMi 317373360.

    Proteomic databases

    MaxQBi P12544.
    PaxDbi P12544.
    PRIDEi P12544.

    Protocols and materials databases

    DNASUi 3001.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000274306 ; ENSP00000274306 ; ENSG00000145649 . [P12544-1 ]
    GeneIDi 3001.
    KEGGi hsa:3001.
    UCSCi uc003jpm.3. human. [P12544-1 ]

    Organism-specific databases

    CTDi 3001.
    GeneCardsi GC05P054398.
    HGNCi HGNC:4708. GZMA.
    MIMi 140050. gene.
    neXtProti NX_P12544.
    PharmGKBi PA29086.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000251820.
    HOVERGENi HBG013304.
    InParanoidi P12544.
    KOi K01352.
    OMAi WIIMTIK.
    OrthoDBi EOG7W9RVH.
    PhylomeDBi P12544.
    TreeFami TF333630.

    Enzyme and pathway databases

    BRENDAi 3.4.21.78. 2681.

    Miscellaneous databases

    EvolutionaryTracei P12544.
    GeneWikii GZMA.
    GenomeRNAii 3001.
    NextBioi 11900.
    PROi P12544.
    SOURCEi Search...

    Gene expression databases

    Bgeei P12544.
    CleanExi HS_GZMA.
    Genevestigatori P12544.

    Family and domain databases

    InterProi IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    PROSITEi PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and chromosomal assignment of a human cDNA encoding a T cell- and natural killer cell-specific trypsin-like serine protease."
      Gershenfeld H.K., Hershberger R.J., Shows T.B., Weissman I.L.
      Proc. Natl. Acad. Sci. U.S.A. 85:1184-1188(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), VARIANT THR-121.
      Tissue: T-cell.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), VARIANT THR-121.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [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] (ISOFORM ALPHA), VARIANT THR-121.
      Tissue: Blood.
    5. "Glucocorticoid-induced alternative promoter usage for a novel 5' variant of granzyme A."
      Ruike Y., Katsuma S., Hirasawa A., Tsujimoto G.
      J. Hum. Genet. 52:172-178(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-72, NUCLEOTIDE SEQUENCE [MRNA] OF 1-34 (ISOFORM BETA), ALTERNATIVE PROMOTER USAGE, INDUCTION.
    6. "The upstream region of the human granzyme A locus contains both positive and negative transcriptional regulatory elements."
      Goralski T.J., Krensky A.M.
      Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-23.
    7. "Human cytotoxic lymphocyte tryptase. Its purification from granules and the characterization of inhibitor and substrate specificity."
      Poe M., Bennett C.D., Biddison W.E., Blake J.T., Norton G.P., Rodkey J.A., Sigal N.H., Turner R.V., Wu J.K., Zweerink H.J.
      J. Biol. Chem. 263:13215-13222(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-53.
    8. "Characterization of three serine esterases isolated from human IL-2 activated killer cells."
      Hameed A., Lowrey D.M., Lichtenheld M., Podack E.R.
      J. Immunol. 141:3142-3147(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-40, CHARACTERIZATION.
    9. "Characterization of granzymes A and B isolated from granules of cloned human cytotoxic T lymphocytes."
      Kraehenbuhl O., Rey C., Jenne D.E., Lanzavecchia A., Groscurth P., Carrel S., Tschopp J.
      J. Immunol. 141:3471-3477(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-39, CHARACTERIZATION.
    10. "Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks."
      Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., Lieberman J.
      J. Biol. Chem. 276:43285-43293(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS SET PROTEASE.
    11. "Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor."
      Fan Z., Beresford P.J., Oh D.Y., Zhang D., Lieberman J.
      Cell 112:659-672(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS SET PROTEASE.
    12. "Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A."
      Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A., Pommier Y., Lieberman J.
      Nat. Immunol. 4:145-153(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH APEX1.
    13. "The exonuclease TREX1 is in the SET complex and acts in concert with NM23-H1 to degrade DNA during granzyme A-mediated cell death."
      Chowdhury D., Beresford P.J., Zhu P., Zhang D., Sung J.S., Demple B., Perrino F.W., Lieberman J.
      Mol. Cell 23:133-142(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS SET PROTEASE.
    14. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-170.
      Tissue: Liver.
    15. "Comparative molecular model building of two serine proteinases from cytotoxic T lymphocytes."
      Murphy M.E.P., Moult J., Bleackley R.C., Gershenfeld H., Weissman I.L., James M.N.G.
      Proteins 4:190-204(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 29-262.
    16. "The oligomeric structure of human granzyme A is a determinant of its extended substrate specificity."
      Bell J.K., Goetz D.H., Mahrus S., Harris J.L., Fletterick R.J., Craik C.S.
      Nat. Struct. Biol. 10:527-534(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 29-262 IN COMPLEX WITH A TRIPEPTIDE CMK INHIBITOR.
    17. "Crystal structure of the apoptosis-inducing human granzyme A dimer."
      Hink-Schauer C., Estebanez-Perpina E., Kurschus F.C., Bode W., Jenne D.E.
      Nat. Struct. Biol. 10:535-540(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 29-262 IN COMPLEX WITH SUBSTRATE.

    Entry informationi

    Entry nameiGRAA_HUMAN
    AccessioniPrimary (citable) accession number: P12544
    Secondary accession number(s): A4PHN1, Q6IB36
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 164 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

    Caution

    Exons 1a and 1b of the sequence reported in PubMed:17180578 are of human origin, however exon 2 shows strong similarity to the rat sequence.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3