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Q07075

- AMPE_HUMAN

UniProt

Q07075 - AMPE_HUMAN

Protein

Glutamyl aminopeptidase

Gene

ENPEP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Appears to have a role in the catabolic pathway of the renin-angiotensin system. Probably plays a role in regulating growth and differentiation of early B-lineage cells.

    Catalytic activityi

    Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei223 – 2231SubstrateBy similarity
    Metal bindingi393 – 3931Zinc; catalyticPROSITE-ProRule annotation
    Active sitei394 – 3941Proton acceptorPROSITE-ProRule annotation
    Metal bindingi397 – 3971Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi416 – 4161Zinc; catalyticPROSITE-ProRule annotation
    Sitei479 – 4791Transition state stabilizerBy similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB
    2. metalloaminopeptidase activity Source: UniProtKB
    3. metallopeptidase activity Source: Reactome
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. angiotensin catabolic process in blood Source: UniProtKB
    3. angiotensin maturation Source: Reactome
    4. cell-cell signaling Source: UniProtKB
    5. cell migration Source: MGI
    6. cell proliferation Source: UniProtKB
    7. cellular protein metabolic process Source: Reactome
    8. glomerulus development Source: UniProtKB
    9. regulation of systemic arterial blood pressure by renin-angiotensin Source: UniProtKB

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    Protein family/group databases

    MEROPSiM01.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamyl aminopeptidase (EC:3.4.11.7)
    Short name:
    EAP
    Alternative name(s):
    Aminopeptidase A
    Short name:
    AP-A
    Differentiation antigen gp160
    CD_antigen: CD249
    Gene namesi
    Name:ENPEP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:3355. ENPEP.

    Subcellular locationi

    GO - Cellular componenti

    1. apical part of cell Source: UniProtKB
    2. apical plasma membrane Source: UniProtKB
    3. brush border Source: UniProtKB
    4. cytoplasmic vesicle Source: UniProtKB
    5. external side of plasma membrane Source: UniProtKB
    6. extracellular vesicular exosome Source: UniProt
    7. integral component of plasma membrane Source: UniProtKB
    8. lysosomal membrane Source: UniProtKB
    9. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27790.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 957957Glutamyl aminopeptidasePRO_0000095095Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi124 – 1241N-linked (GlcNAc...)1 Publication
    Glycosylationi197 – 1971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)1 Publication
    Glycosylationi340 – 3401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi554 – 5541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi589 – 5891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi597 – 5971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi607 – 6071N-linked (GlcNAc...)2 Publications
    Glycosylationi610 – 6101N-linked (GlcNAc...)1 Publication
    Glycosylationi678 – 6781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi763 – 7631N-linked (GlcNAc...)1 Publication
    Glycosylationi773 – 7731N-linked (GlcNAc...)1 Publication
    Glycosylationi801 – 8011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi828 – 8281N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ07075.
    PaxDbiQ07075.
    PRIDEiQ07075.

    PTM databases

    PhosphoSiteiQ07075.

    Expressioni

    Tissue specificityi

    Expressed by epithelial cells of the proximal tubule cells and the glomerulus of the nephron. Also found in a variety of other tissues.

    Gene expression databases

    BgeeiQ07075.
    CleanExiHS_ENPEP.
    GenevestigatoriQ07075.

    Organism-specific databases

    HPAiHPA005128.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked.

    Protein-protein interaction databases

    IntActiQ07075. 3 interactions.
    STRINGi9606.ENSP00000265162.

    Structurei

    Secondary structure

    1
    957
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi87 – 893
    Beta strandi90 – 923
    Beta strandi97 – 10913
    Helixi110 – 1123
    Beta strandi114 – 12512
    Beta strandi129 – 1357
    Beta strandi138 – 14811
    Beta strandi157 – 1637
    Helixi164 – 1663
    Beta strandi168 – 17710
    Beta strandi181 – 1833
    Beta strandi186 – 19510
    Beta strandi200 – 21011
    Beta strandi213 – 2219
    Turni223 – 2264
    Helixi227 – 2304
    Beta strandi241 – 25010
    Beta strandi253 – 2597
    Beta strandi261 – 27616
    Helixi284 – 2863
    Beta strandi289 – 2924
    Beta strandi295 – 3006
    Beta strandi306 – 3116
    Helixi313 – 3197
    Helixi320 – 33617
    Beta strandi342 – 3443
    Beta strandi346 – 3538
    Beta strandi355 – 3595
    Beta strandi364 – 3685
    Helixi369 – 3713
    Turni376 – 3783
    Helixi381 – 39717
    Turni401 – 4033
    Beta strandi404 – 4085
    Helixi409 – 4124
    Helixi413 – 43018
    Helixi432 – 4343
    Helixi436 – 4438
    Helixi445 – 4517
    Helixi467 – 4726
    Helixi476 – 49318
    Helixi495 – 50814
    Beta strandi512 – 5143
    Helixi516 – 52712
    Helixi531 – 5355
    Helixi536 – 5383
    Beta strandi545 – 5506
    Turni551 – 5533
    Beta strandi554 – 5596
    Turni574 – 5774
    Beta strandi581 – 5877
    Beta strandi590 – 5967
    Beta strandi618 – 6203
    Helixi621 – 6233
    Beta strandi625 – 6306
    Helixi633 – 64614
    Helixi647 – 6493
    Helixi652 – 66716
    Helixi673 – 6786
    Turni679 – 6824
    Helixi683 – 6853
    Helixi689 – 70517
    Turni706 – 7083
    Helixi712 – 73120
    Helixi739 – 75416
    Helixi758 – 77114
    Turni780 – 7823
    Helixi783 – 79412
    Helixi797 – 80913
    Helixi813 – 82311
    Helixi829 – 83810
    Turni842 – 8443
    Helixi847 – 8493
    Helixi850 – 8589
    Helixi863 – 87311
    Helixi875 – 8828
    Helixi887 – 8915
    Helixi892 – 8965
    Helixi902 – 91413
    Helixi919 – 9213
    Helixi922 – 95332

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4KX7X-ray2.15A76-957[»]
    4KX8X-ray2.40A76-957[»]
    4KX9X-ray2.25A76-957[»]
    4KXAX-ray2.40A76-957[»]
    4KXBX-ray2.40A76-957[»]
    4KXCX-ray2.40A76-957[»]
    4KXDX-ray2.15A76-957[»]
    ProteinModelPortaliQ07075.
    SMRiQ07075. Positions 76-954.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1818CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini40 – 957918ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei19 – 3921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni357 – 3615Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the peptidase M1 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0308.
    HOGENOMiHOG000106482.
    HOVERGENiHBG006616.
    InParanoidiQ07075.
    KOiK11141.
    OMAiNPVHYDL.
    OrthoDBiEOG754HNR.
    PhylomeDBiQ07075.
    TreeFamiTF300395.

    Family and domain databases

    InterProiIPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view]
    PANTHERiPTHR11533. PTHR11533. 1 hit.
    PfamiPF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view]
    PRINTSiPR00756. ALADIPTASE.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q07075-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNFAEREGSK RYCIQTKHVA ILCAVVVGVG LIVGLAVGLT RSCDSSGDGG    50
    PGTAPAPSHL PSSTASPSGP PAQDQDICPA SEDESGQWKN FRLPDFVNPV 100
    HYDLHVKPLL EEDTYTGTVS ISINLSAPTR YLWLHLRETR ITRLPELKRP 150
    SGDQVQVRRC FEYKKQEYVV VEAEEELTPS SGDGLYLLTM EFAGWLNGSL 200
    VGFYRTTYTE NGQVKSIVAT DHEPTDARKS FPCFDEPNKK ATYTISITHP 250
    KEYGALSNMP VAKEESVDDK WTRTTFEKSV PMSTYLVCFA VHQFDSVKRI 300
    SNSGKPLTIY VQPEQKHTAE YAANITKSVF DYFEEYFAMN YSLPKLDKIA 350
    IPDFGTGAME NWGLITYRET NLLYDPKESA SSNQQRVATV VAHELVHQWF 400
    GNIVTMDWWE DLWLNEGFAS FFEFLGVNHA ETDWQMRDQM LLEDVLPVQE 450
    DDSLMSSHPI IVTVTTPDEI TSVFDGISYS KGSSILRMLE DWIKPENFQK 500
    GCQMYLEKYQ FKNAKTSDFW AALEEASRLP VKEVMDTWTR QMGYPVLNVN 550
    GVKNITQKRF LLDPRANPSQ PPSDLGYTWN IPVKWTEDNI TSSVLFNRSE 600
    KEGITLNSSN PSGNAFLKIN PDHIGFYRVN YEVATWDSIA TALSLNHKTF 650
    SSADRASLID DAFALARAQL LDYKVALNLT KYLKREENFL PWQRVISAVT 700
    YIISMFEDDK ELYPMIEEYF QGQVKPIADS LGWNDAGDHV TKLLRSSVLG 750
    FACKMGDREA LNNASSLFEQ WLNGTVSLPV NLRLLVYRYG MQNSGNEISW 800
    NYTLEQYQKT SLAQEKEKLL YGLASVKNVT LLSRYLDLLK DTNLIKTQDV 850
    FTVIRYISYN SYGKNMAWNW IQLNWDYLVN RYTLNNRNLG RIVTIAEPFN 900
    TELQLWQMES FFAKYPQAGA GEKPREQVLE TVKNNIEWLK QHRNTIREWF 950
    FNLLESG 957
    Length:957
    Mass (Da):109,244
    Last modified:May 18, 2010 - v3
    Checksum:iAB6407432A45A7C6
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti213 – 2131Q → R.4 Publications
    Corresponds to variant rs10004516 [ dbSNP | Ensembl ].
    VAR_030359
    Natural varianti218 – 2181V → A.1 Publication
    Corresponds to variant rs1126483 [ dbSNP | Ensembl ].
    VAR_030360
    Natural varianti437 – 4371R → H.
    Corresponds to variant rs34949711 [ dbSNP | Ensembl ].
    VAR_057056
    Natural varianti861 – 8611S → R.
    Corresponds to variant rs35812243 [ dbSNP | Ensembl ].
    VAR_057057
    Natural varianti887 – 8871R → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036047

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14721 mRNA. Translation: AAA35522.1.
    L12468 mRNA. Translation: AAA16876.1.
    AC017068 Genomic DNA. No translation available.
    AC098798 Genomic DNA. No translation available.
    BC094770 mRNA. Translation: AAH94770.1.
    CCDSiCCDS3691.1.
    PIRiA47531.
    RefSeqiNP_001968.3. NM_001977.3.
    UniGeneiHs.435765.

    Genome annotation databases

    EnsembliENST00000265162; ENSP00000265162; ENSG00000138792.
    GeneIDi2028.
    KEGGihsa:2028.
    UCSCiuc003iab.4. human.

    Polymorphism databases

    DMDMi296439445.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L14721 mRNA. Translation: AAA35522.1 .
    L12468 mRNA. Translation: AAA16876.1 .
    AC017068 Genomic DNA. No translation available.
    AC098798 Genomic DNA. No translation available.
    BC094770 mRNA. Translation: AAH94770.1 .
    CCDSi CCDS3691.1.
    PIRi A47531.
    RefSeqi NP_001968.3. NM_001977.3.
    UniGenei Hs.435765.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4KX7 X-ray 2.15 A 76-957 [» ]
    4KX8 X-ray 2.40 A 76-957 [» ]
    4KX9 X-ray 2.25 A 76-957 [» ]
    4KXA X-ray 2.40 A 76-957 [» ]
    4KXB X-ray 2.40 A 76-957 [» ]
    4KXC X-ray 2.40 A 76-957 [» ]
    4KXD X-ray 2.15 A 76-957 [» ]
    ProteinModelPortali Q07075.
    SMRi Q07075. Positions 76-954.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q07075. 3 interactions.
    STRINGi 9606.ENSP00000265162.

    Chemistry

    ChEMBLi CHEMBL3439.
    DrugBanki DB00142. L-Glutamic Acid.

    Protein family/group databases

    MEROPSi M01.003.

    PTM databases

    PhosphoSitei Q07075.

    Polymorphism databases

    DMDMi 296439445.

    Proteomic databases

    MaxQBi Q07075.
    PaxDbi Q07075.
    PRIDEi Q07075.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265162 ; ENSP00000265162 ; ENSG00000138792 .
    GeneIDi 2028.
    KEGGi hsa:2028.
    UCSCi uc003iab.4. human.

    Organism-specific databases

    CTDi 2028.
    GeneCardsi GC04P111286.
    H-InvDB HIX0024609.
    HGNCi HGNC:3355. ENPEP.
    HPAi HPA005128.
    MIMi 138297. gene.
    neXtProti NX_Q07075.
    PharmGKBi PA27790.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0308.
    HOGENOMi HOG000106482.
    HOVERGENi HBG006616.
    InParanoidi Q07075.
    KOi K11141.
    OMAi NPVHYDL.
    OrthoDBi EOG754HNR.
    PhylomeDBi Q07075.
    TreeFami TF300395.

    Enzyme and pathway databases

    Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.

    Miscellaneous databases

    GenomeRNAii 2028.
    NextBioi 8213.
    PROi Q07075.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q07075.
    CleanExi HS_ENPEP.
    Genevestigatori Q07075.

    Family and domain databases

    InterProi IPR024571. ERAP1-like_C_dom.
    IPR001930. Peptidase_M1.
    IPR014782. Peptidase_M1_N.
    [Graphical view ]
    PANTHERi PTHR11533. PTHR11533. 1 hit.
    Pfami PF11838. ERAP1_C. 1 hit.
    PF01433. Peptidase_M1. 1 hit.
    [Graphical view ]
    PRINTSi PR00756. ALADIPTASE.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the human kidney differentiation antigen gp160: human aminopeptidase A."
      Nanus D.M., Engelstein D., Gastl G.A., Gluck L., Vidal M.J., Morrison M., Finstad C.L., Bander N.H., Albino A.P.
      Proc. Natl. Acad. Sci. U.S.A. 90:7069-7073(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 242-251; 300-316 AND 369-377, VARIANTS ARG-213 AND ALA-218.
      Tissue: Kidney cortex.
    2. "cDNA cloning and expression of human glutamyl aminopeptidase (aminopeptidase A)."
      Li L., Wang J., Cooper M.D.
      Genomics 17:657-664(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-213.
      Tissue: Kidney.
    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], VARIANT ARG-213.
    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], VARIANT ARG-213.
      Tissue: Placenta.
    5. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-607.
      Tissue: Plasma.
    6. "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-124; ASN-324; ASN-607; ASN-610; ASN-763 AND ASN-773.
      Tissue: Liver.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-887.

    Entry informationi

    Entry nameiAMPE_HUMAN
    AccessioniPrimary (citable) accession number: Q07075
    Secondary accession number(s): Q504U2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 150 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

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

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. Peptidase families
      Classification of peptidase families and list of entries
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3