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Protein

Endoplasmic reticulum aminopeptidase 1

Gene

ERAP1

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

Functioni

Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.3 Publications

Catalytic activityi

Release of an N-terminal amino acid, Xaa-|-Xbb-, in which Xaa is preferably Leu, but may be other amino acids including Met, Cys and Phe.1 Publication

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei183SubstrateBy similarity1
Metal bindingi353Zinc; catalytic1
Active sitei354Proton acceptorPROSITE-ProRule annotation1
Metal bindingi357Zinc; catalytic1
Metal bindingi376Zinc; catalytic1
Sitei438Transition state stabilizerBy similarity1

GO - Molecular functioni

  • aminopeptidase activity Source: UniProtKB
  • endopeptidase activity Source: Reactome
  • interleukin-1, Type II receptor binding Source: HGNC
  • interleukin-6 receptor binding Source: UniProtKB
  • metalloaminopeptidase activity Source: GO_Central
  • metalloexopeptidase activity Source: UniProtKB
  • peptide binding Source: GO_Central
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • angiogenesis Source: HGNC
  • antigen processing and presentation of endogenous peptide antigen via MHC class I Source: UniProtKB
  • antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  • fat cell differentiation Source: UniProtKB
  • membrane protein ectodomain proteolysis Source: UniProtKB
  • peptide catabolic process Source: GO_Central
  • positive regulation of angiogenesis Source: Ensembl
  • regulation of blood pressure Source: UniProtKB
  • regulation of innate immune response Source: UniProtKB
  • response to bacterium Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Adaptive immunity, Immunity

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000164307-MONOMER.
ReactomeiR-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Protein family/group databases

MEROPSiM01.018.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum aminopeptidase 1 (EC:3.4.11.-)
Alternative name(s):
ARTS-1
Adipocyte-derived leucine aminopeptidase
Short name:
A-LAP
Aminopeptidase PILS
Puromycin-insensitive leucyl-specific aminopeptidase
Short name:
PILS-AP
Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator
Gene namesi
Name:ERAP1
Synonyms:APPILS, ARTS1, KIAA0525
ORF Names:UNQ584/PRO1154
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:18173. ERAP1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1CytoplasmicSequence analysis1
Transmembranei2 – 21Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini22 – 941LumenalSequence analysisAdd BLAST920

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum lumen Source: HGNC
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi438Y → F: Loss of enzyme activity. 1 Publication1

Organism-specific databases

DisGeNETi51752.
OpenTargetsiENSG00000164307.
PharmGKBiPA162385163.

Chemistry databases

ChEMBLiCHEMBL5939.
GuidetoPHARMACOLOGYi1566.

Polymorphism and mutation databases

BioMutaiERAP1.
DMDMi158937334.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000267511 – 941Endoplasmic reticulum aminopeptidase 1Add BLAST941

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi70N-linked (GlcNAc...)2 Publications1
Glycosylationi154N-linked (GlcNAc...)2 Publications1
Disulfide bondi404 ↔ 443
Glycosylationi414N-linked (GlcNAc...)2 Publications1
Disulfide bondi736 ↔ 743
Glycosylationi760N-linked (GlcNAc...)1 Publication1
Glycosylationi901N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

N-glycosylated.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9NZ08.
MaxQBiQ9NZ08.
PaxDbiQ9NZ08.
PeptideAtlasiQ9NZ08.
PRIDEiQ9NZ08.

PTM databases

iPTMnetiQ9NZ08.
PhosphoSitePlusiQ9NZ08.
SwissPalmiQ9NZ08.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

By IFNG/IFN-gamma.1 Publication

Gene expression databases

BgeeiENSG00000164307.
CleanExiHS_ERAP1.
ExpressionAtlasiQ9NZ08. baseline and differential.
GenevisibleiQ9NZ08. HS.

Organism-specific databases

HPAiCAB025095.
HPA042317.

Interactioni

Subunit structurei

Monomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX.4 Publications

GO - Molecular functioni

  • interleukin-1, Type II receptor binding Source: HGNC
  • interleukin-6 receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119713. 19 interactors.
IntActiQ9NZ08. 3 interactors.
STRINGi9606.ENSP00000296754.

Chemistry databases

BindingDBiQ9NZ08.

Structurei

Secondary structure

1941
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi56 – 70Combined sources15
Turni71 – 74Combined sources4
Beta strandi75 – 88Combined sources14
Beta strandi90 – 96Combined sources7
Beta strandi101 – 109Combined sources9
Beta strandi116 – 119Combined sources4
Beta strandi121 – 125Combined sources5
Turni126 – 129Combined sources4
Beta strandi130 – 139Combined sources10
Beta strandi145 – 154Combined sources10
Beta strandi156 – 168Combined sources13
Beta strandi174 – 181Combined sources8
Turni183 – 186Combined sources4
Helixi187 – 190Combined sources4
Beta strandi201 – 209Combined sources9
Beta strandi214 – 219Combined sources6
Beta strandi221 – 228Combined sources8
Beta strandi231 – 236Combined sources6
Helixi244 – 246Combined sources3
Beta strandi249 – 252Combined sources4
Beta strandi255 – 260Combined sources6
Beta strandi266 – 271Combined sources6
Turni273 – 275Combined sources3
Helixi276 – 278Combined sources3
Helixi280 – 296Combined sources17
Beta strandi303 – 313Combined sources11
Beta strandi315 – 319Combined sources5
Beta strandi324 – 328Combined sources5
Helixi329 – 331Combined sources3
Turni336 – 338Combined sources3
Helixi341 – 356Combined sources16
Turni357 – 359Combined sources3
Turni361 – 363Combined sources3
Beta strandi364 – 368Combined sources5
Helixi369 – 372Combined sources4
Helixi373 – 390Combined sources18
Helixi392 – 394Combined sources3
Helixi396 – 399Combined sources4
Helixi400 – 411Combined sources12
Helixi426 – 431Combined sources6
Helixi435 – 451Combined sources17
Helixi454 – 468Combined sources15
Beta strandi471 – 473Combined sources3
Helixi475 – 483Combined sources9
Helixi517 – 525Combined sources9
Beta strandi530 – 538Combined sources9
Beta strandi541 – 549Combined sources9
Beta strandi565 – 573Combined sources9
Beta strandi578 – 582Combined sources5
Beta strandi584 – 590Combined sources7
Beta strandi598 – 606Combined sources9
Beta strandi609 – 611Combined sources3
Helixi613 – 627Combined sources15
Helixi628 – 630Combined sources3
Helixi633 – 648Combined sources16
Helixi654 – 661Combined sources8
Helixi662 – 666Combined sources5
Helixi670 – 687Combined sources18
Helixi693 – 713Combined sources21
Beta strandi716 – 718Combined sources3
Helixi722 – 737Combined sources16
Helixi741 – 756Combined sources16
Turni757 – 759Combined sources3
Helixi765 – 767Combined sources3
Helixi768 – 775Combined sources8
Helixi779 – 791Combined sources13
Helixi795 – 805Combined sources11
Helixi811 – 823Combined sources13
Beta strandi824 – 827Combined sources4
Helixi829 – 831Combined sources3
Helixi832 – 840Combined sources9
Turni843 – 845Combined sources3
Helixi846 – 864Combined sources19
Helixi869 – 877Combined sources9
Turni878 – 881Combined sources4
Helixi885 – 896Combined sources12
Turni897 – 900Combined sources4
Turni902 – 904Combined sources3
Helixi906 – 941Combined sources36

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YD0X-ray2.70A46-940[»]
3MDJX-ray2.95A/B/C37-939[»]
3QNFX-ray3.00A/B/C1-941[»]
3RJOX-ray2.30A529-941[»]
ProteinModelPortaliQ9NZ08.
SMRiQ9NZ08.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NZ08.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni317 – 321Substrate bindingBy similarity5

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00760000119082.
HOVERGENiHBG108296.
InParanoidiQ9NZ08.
KOiK09604.
OMAiVLEHPPQ.
OrthoDBiEOG091G01GH.
PhylomeDBiQ9NZ08.
TreeFamiTF300395.

Family and domain databases

InterProiIPR033520. ERAP1.
IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PTHR11533:SF156. PTHR11533:SF156. 2 hits.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NZ08-1) [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
MVFLPLKWSL ATMSFLLSSL LALLTVSTPS WCQSTEASPK RSDGTPFPWN
60 70 80 90 100
KIRLPEYVIP VHYDLLIHAN LTTLTFWGTT KVEITASQPT STIILHSHHL
110 120 130 140 150
QISRATLRKG AGERLSEEPL QVLEHPRQEQ IALLAPEPLL VGLPYTVVIH
160 170 180 190 200
YAGNLSETFH GFYKSTYRTK EGELRILAST QFEPTAARMA FPCFDEPAFK
210 220 230 240 250
ASFSIKIRRE PRHLAISNMP LVKSVTVAEG LIEDHFDVTV KMSTYLVAFI
260 270 280 290 300
ISDFESVSKI TKSGVKVSVY AVPDKINQAD YALDAAVTLL EFYEDYFSIP
310 320 330 340 350
YPLPKQDLAA IPDFQSGAME NWGLTTYRES ALLFDAEKSS ASSKLGITMT
360 370 380 390 400
VAHELAHQWF GNLVTMEWWN DLWLNEGFAK FMEFVSVSVT HPELKVGDYF
410 420 430 440 450
FGKCFDAMEV DALNSSHPVS TPVENPAQIR EMFDDVSYDK GACILNMLRE
460 470 480 490 500
YLSADAFKSG IVQYLQKHSY KNTKNEDLWD SMASICPTDG VKGMDGFCSR
510 520 530 540 550
SQHSSSSSHW HQEGVDVKTM MNTWTLQKGF PLITITVRGR NVHMKQEHYM
560 570 580 590 600
KGSDGAPDTG YLWHVPLTFI TSKSDMVHRF LLKTKTDVLI LPEEVEWIKF
610 620 630 640 650
NVGMNGYYIV HYEDDGWDSL TGLLKGTHTA VSSNDRASLI NNAFQLVSIG
660 670 680 690 700
KLSIEKALDL SLYLKHETEI MPVFQGLNEL IPMYKLMEKR DMNEVETQFK
710 720 730 740 750
AFLIRLLRDL IDKQTWTDEG SVSERMLRSQ LLLLACVHNY QPCVQRAEGY
760 770 780 790 800
FRKWKESNGN LSLPVDVTLA VFAVGAQSTE GWDFLYSKYQ FSLSSTEKSQ
810 820 830 840 850
IEFALCRTQN KEKLQWLLDE SFKGDKIKTQ EFPQILTLIG RNPVGYPLAW
860 870 880 890 900
QFLRKNWNKL VQKFELGSSS IAHMVMGTTN QFSTRTRLEE VKGFFSSLKE
910 920 930 940
NGSQLRCVQQ TIETIEENIG WMDKNFDKIR VWLQSEKLER M
Length:941
Mass (Da):107,235
Last modified:July 24, 2007 - v3
Checksum:i22A0795C90155F04
GO
Isoform 2 (identifier: Q9NZ08-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     940-941: RM → HDPEADATG

Show »
Length:948
Mass (Da):107,841
Checksum:iB7DEE159B1D591EE
GO

Sequence cautioni

The sequence BAA25451 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti12T → I in AAF07395 (PubMed:10220586).Curated1
Sequence conflicti12T → I in AAK37777 (PubMed:11481040).Curated1
Sequence conflicti12T → I in AAK37778 (PubMed:11481040).Curated1
Sequence conflicti514G → R in AAF20384 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04668156E → K.Corresponds to variant rs3734016dbSNPEnsembl.1
Natural variantiVAR_012779127R → P.4 PublicationsCorresponds to variant rs26653dbSNPEnsembl.1
Natural variantiVAR_012780276I → M.Corresponds to variant rs26618dbSNPEnsembl.1
Natural variantiVAR_012781346G → D.1 PublicationCorresponds to variant rs27895dbSNPEnsembl.1
Natural variantiVAR_012782349M → V.3 PublicationsCorresponds to variant rs2287987dbSNPEnsembl.1
Natural variantiVAR_012783528K → R.4 PublicationsCorresponds to variant rs30187dbSNPEnsembl.1
Natural variantiVAR_046682575D → G.Corresponds to variant rs6863093dbSNPEnsembl.1
Natural variantiVAR_021555575D → N.3 PublicationsCorresponds to variant rs10050860dbSNPEnsembl.1
Natural variantiVAR_021556725R → Q.3 PublicationsCorresponds to variant rs17482078dbSNPEnsembl.1
Natural variantiVAR_012784730Q → E.4 PublicationsCorresponds to variant rs27044dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005450940 – 941RM → HDPEADATG in isoform 2. 2 Publications2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106037 mRNA. Translation: AAF07395.1.
AY028806 mRNA. Translation: AAK37777.1.
AY028807 mRNA. Translation: AAK37778.1.
AF183569 mRNA. Translation: AAF20384.1.
AF222340 mRNA. Translation: AAF34664.1.
AB011097 mRNA. Translation: BAA25451.2. Different initiation.
AY358590 mRNA. Translation: AAQ88953.1.
BC030775 mRNA. Translation: AAH30775.1.
CCDSiCCDS4085.1. [Q9NZ08-2]
CCDS47250.1. [Q9NZ08-1]
RefSeqiNP_001035548.1. NM_001040458.1. [Q9NZ08-1]
NP_001185470.1. NM_001198541.1. [Q9NZ08-1]
NP_057526.3. NM_016442.3. [Q9NZ08-2]
XP_011541788.1. XM_011543486.2. [Q9NZ08-1]
XP_016865071.1. XM_017009582.1. [Q9NZ08-2]
UniGeneiHs.666524.
Hs.667944.

Genome annotation databases

EnsembliENST00000296754; ENSP00000296754; ENSG00000164307. [Q9NZ08-2]
ENST00000443439; ENSP00000406304; ENSG00000164307. [Q9NZ08-1]
GeneIDi51752.
KEGGihsa:51752.
UCSCiuc003kml.4. human. [Q9NZ08-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF106037 mRNA. Translation: AAF07395.1.
AY028806 mRNA. Translation: AAK37777.1.
AY028807 mRNA. Translation: AAK37778.1.
AF183569 mRNA. Translation: AAF20384.1.
AF222340 mRNA. Translation: AAF34664.1.
AB011097 mRNA. Translation: BAA25451.2. Different initiation.
AY358590 mRNA. Translation: AAQ88953.1.
BC030775 mRNA. Translation: AAH30775.1.
CCDSiCCDS4085.1. [Q9NZ08-2]
CCDS47250.1. [Q9NZ08-1]
RefSeqiNP_001035548.1. NM_001040458.1. [Q9NZ08-1]
NP_001185470.1. NM_001198541.1. [Q9NZ08-1]
NP_057526.3. NM_016442.3. [Q9NZ08-2]
XP_011541788.1. XM_011543486.2. [Q9NZ08-1]
XP_016865071.1. XM_017009582.1. [Q9NZ08-2]
UniGeneiHs.666524.
Hs.667944.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YD0X-ray2.70A46-940[»]
3MDJX-ray2.95A/B/C37-939[»]
3QNFX-ray3.00A/B/C1-941[»]
3RJOX-ray2.30A529-941[»]
ProteinModelPortaliQ9NZ08.
SMRiQ9NZ08.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119713. 19 interactors.
IntActiQ9NZ08. 3 interactors.
STRINGi9606.ENSP00000296754.

Chemistry databases

BindingDBiQ9NZ08.
ChEMBLiCHEMBL5939.
GuidetoPHARMACOLOGYi1566.

Protein family/group databases

MEROPSiM01.018.

PTM databases

iPTMnetiQ9NZ08.
PhosphoSitePlusiQ9NZ08.
SwissPalmiQ9NZ08.

Polymorphism and mutation databases

BioMutaiERAP1.
DMDMi158937334.

Proteomic databases

EPDiQ9NZ08.
MaxQBiQ9NZ08.
PaxDbiQ9NZ08.
PeptideAtlasiQ9NZ08.
PRIDEiQ9NZ08.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296754; ENSP00000296754; ENSG00000164307. [Q9NZ08-2]
ENST00000443439; ENSP00000406304; ENSG00000164307. [Q9NZ08-1]
GeneIDi51752.
KEGGihsa:51752.
UCSCiuc003kml.4. human. [Q9NZ08-1]

Organism-specific databases

CTDi51752.
DisGeNETi51752.
GeneCardsiERAP1.
H-InvDBHIX0164377.
HGNCiHGNC:18173. ERAP1.
HPAiCAB025095.
HPA042317.
MIMi606832. gene.
neXtProtiNX_Q9NZ08.
OpenTargetsiENSG00000164307.
PharmGKBiPA162385163.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1046. Eukaryota.
COG0308. LUCA.
GeneTreeiENSGT00760000119082.
HOVERGENiHBG108296.
InParanoidiQ9NZ08.
KOiK09604.
OMAiVLEHPPQ.
OrthoDBiEOG091G01GH.
PhylomeDBiQ9NZ08.
TreeFamiTF300395.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000164307-MONOMER.
ReactomeiR-HSA-983170. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

EvolutionaryTraceiQ9NZ08.
GeneWikiiARTS-1.
GenomeRNAii51752.
PROiQ9NZ08.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000164307.
CleanExiHS_ERAP1.
ExpressionAtlasiQ9NZ08. baseline and differential.
GenevisibleiQ9NZ08. HS.

Family and domain databases

InterProiIPR033520. ERAP1.
IPR024571. ERAP1-like_C_dom.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]
PANTHERiPTHR11533. PTHR11533. 2 hits.
PTHR11533:SF156. PTHR11533:SF156. 2 hits.
PfamiPF11838. ERAP1_C. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]
PRINTSiPR00756. ALADIPTASE.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiERAP1_HUMAN
AccessioniPrimary (citable) accession number: Q9NZ08
Secondary accession number(s): O60278
, Q6UWY6, Q8NEL4, Q8TAD0, Q9UHF8, Q9UKY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: July 24, 2007
Last modified: November 2, 2016
This is version 159 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

Caution

It is uncertain whether Met-1 or Met-13 is the initiator.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

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.