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Q07075

- AMPE_HUMAN

UniProt

Q07075 - AMPE_HUMAN

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Protein

Glutamyl aminopeptidase

Gene

ENPEP

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

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

Zn2+By similarityNote: 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1818CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei19 – 3921Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini40 – 957918ExtracellularSequence AnalysisAdd
BLAST

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: UniProtKB
  7. integral component of plasma membrane Source: UniProtKB
  8. lysosomal membrane Source: UniProtKB
  9. plasma membrane Source: Reactome
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

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.
GeneTreeiENSGT00760000119082.
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

        10         20         30         40         50
MNFAEREGSK RYCIQTKHVA ILCAVVVGVG LIVGLAVGLT RSCDSSGDGG
60 70 80 90 100
PGTAPAPSHL PSSTASPSGP PAQDQDICPA SEDESGQWKN FRLPDFVNPV
110 120 130 140 150
HYDLHVKPLL EEDTYTGTVS ISINLSAPTR YLWLHLRETR ITRLPELKRP
160 170 180 190 200
SGDQVQVRRC FEYKKQEYVV VEAEEELTPS SGDGLYLLTM EFAGWLNGSL
210 220 230 240 250
VGFYRTTYTE NGQVKSIVAT DHEPTDARKS FPCFDEPNKK ATYTISITHP
260 270 280 290 300
KEYGALSNMP VAKEESVDDK WTRTTFEKSV PMSTYLVCFA VHQFDSVKRI
310 320 330 340 350
SNSGKPLTIY VQPEQKHTAE YAANITKSVF DYFEEYFAMN YSLPKLDKIA
360 370 380 390 400
IPDFGTGAME NWGLITYRET NLLYDPKESA SSNQQRVATV VAHELVHQWF
410 420 430 440 450
GNIVTMDWWE DLWLNEGFAS FFEFLGVNHA ETDWQMRDQM LLEDVLPVQE
460 470 480 490 500
DDSLMSSHPI IVTVTTPDEI TSVFDGISYS KGSSILRMLE DWIKPENFQK
510 520 530 540 550
GCQMYLEKYQ FKNAKTSDFW AALEEASRLP VKEVMDTWTR QMGYPVLNVN
560 570 580 590 600
GVKNITQKRF LLDPRANPSQ PPSDLGYTWN IPVKWTEDNI TSSVLFNRSE
610 620 630 640 650
KEGITLNSSN PSGNAFLKIN PDHIGFYRVN YEVATWDSIA TALSLNHKTF
660 670 680 690 700
SSADRASLID DAFALARAQL LDYKVALNLT KYLKREENFL PWQRVISAVT
710 720 730 740 750
YIISMFEDDK ELYPMIEEYF QGQVKPIADS LGWNDAGDHV TKLLRSSVLG
760 770 780 790 800
FACKMGDREA LNNASSLFEQ WLNGTVSLPV NLRLLVYRYG MQNSGNEISW
810 820 830 840 850
NYTLEQYQKT SLAQEKEKLL YGLASVKNVT LLSRYLDLLK DTNLIKTQDV
860 870 880 890 900
FTVIRYISYN SYGKNMAWNW IQLNWDYLVN RYTLNNRNLG RIVTIAEPFN
910 920 930 940 950
TELQLWQMES FFAKYPQAGA GEKPREQVLE TVKNNIEWLK QHRNTIREWF

FNLLESG
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

BindingDBi Q07075.
ChEMBLi CHEMBL3439.

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.
GeneTreei ENSGT00760000119082.
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

ChiTaRSi ENPEP. human.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 152 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