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Q9NZ08

- ERAP1_HUMAN

UniProt

Q9NZ08 - ERAP1_HUMAN

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Protein
Endoplasmic reticulum aminopeptidase 1
Gene
ERAP1, APPILS, ARTS1, KIAA0525, UNQ584/PRO1154
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei183 – 1831Substrate By similarity
Metal bindingi353 – 3531Zinc; catalytic
Active sitei354 – 3541Proton acceptor By similarity
Metal bindingi357 – 3571Zinc; catalytic
Metal bindingi376 – 3761Zinc; catalytic
Sitei438 – 4381Transition state stabilizer By similarity

GO - Molecular functioni

  1. aminopeptidase activity Source: UniProtKB
  2. interleukin-1, Type II receptor binding Source: HGNC
  3. interleukin-6 receptor binding Source: UniProtKB
  4. metalloexopeptidase activity Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. zinc ion binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. angiogenesis Source: HGNC
  2. antigen processing and presentation of endogenous peptide antigen via MHC class I Source: UniProtKB
  3. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  4. fat cell differentiation Source: UniProtKB
  5. membrane protein ectodomain proteolysis Source: UniProtKB
  6. positive regulation of angiogenesis Source: Ensembl
  7. regulation of blood pressure Source: UniProtKB
  8. regulation of innate immune response Source: UniProtKB
  9. 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

ReactomeiREACT_75795. 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
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:18173. ERAP1.

Subcellular locationi

Endoplasmic reticulum membrane; Single-pass type II membrane protein Inferred 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 11Cytoplasmic Reviewed prediction
Transmembranei2 – 2120Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini22 – 941920Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. endoplasmic reticulum Source: UniProtKB
  3. endoplasmic reticulum lumen Source: HGNC
  4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  5. extracellular region Source: UniProtKB
  6. extracellular space Source: UniProt
  7. extracellular vesicular exosome Source: UniProt
  8. integral component of membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi438 – 4381Y → F: Loss of enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA162385163.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 941941Endoplasmic reticulum aminopeptidase 1
PRO_0000026751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi70 – 701N-linked (GlcNAc...)2 Publications
Glycosylationi154 – 1541N-linked (GlcNAc...)2 Publications
Disulfide bondi404 ↔ 4432 Publications
Glycosylationi414 – 4141N-linked (GlcNAc...)2 Publications
Disulfide bondi736 ↔ 7432 Publications
Glycosylationi760 – 7601N-linked (GlcNAc...)1 Publication
Glycosylationi901 – 9011N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9NZ08.
PaxDbiQ9NZ08.
PRIDEiQ9NZ08.

PTM databases

PhosphoSiteiQ9NZ08.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

By IFNG/IFN-gamma.1 Publication

Gene expression databases

ArrayExpressiQ9NZ08.
BgeeiQ9NZ08.
CleanExiHS_ERAP1.
GenevestigatoriQ9NZ08.

Organism-specific databases

HPAiCAB025095.
HPA042317.

Interactioni

Subunit structurei

Monomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX.3 Publications

Protein-protein interaction databases

BioGridi119713. 3 interactions.
IntActiQ9NZ08. 3 interactions.
STRINGi9606.ENSP00000296754.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi56 – 7015
Turni71 – 744
Beta strandi75 – 8814
Beta strandi90 – 967
Beta strandi101 – 1099
Beta strandi116 – 1194
Beta strandi121 – 1255
Turni126 – 1294
Beta strandi130 – 13910
Beta strandi145 – 15410
Beta strandi156 – 16813
Beta strandi174 – 1818
Turni183 – 1864
Helixi187 – 1904
Beta strandi201 – 2099
Beta strandi214 – 2196
Beta strandi221 – 2288
Beta strandi231 – 2366
Helixi244 – 2463
Beta strandi249 – 2524
Beta strandi255 – 2606
Beta strandi266 – 2716
Turni273 – 2753
Helixi276 – 2783
Helixi280 – 29617
Beta strandi303 – 31311
Beta strandi315 – 3195
Beta strandi324 – 3285
Helixi329 – 3313
Turni336 – 3383
Helixi341 – 35616
Turni357 – 3593
Turni361 – 3633
Beta strandi364 – 3685
Helixi369 – 3724
Helixi373 – 39018
Helixi392 – 3943
Helixi396 – 3994
Helixi400 – 41112
Helixi426 – 4316
Helixi435 – 45117
Helixi454 – 46815
Beta strandi471 – 4733
Helixi475 – 4839
Helixi517 – 5259
Beta strandi530 – 5389
Beta strandi541 – 5499
Beta strandi565 – 5739
Beta strandi578 – 5825
Beta strandi584 – 5907
Beta strandi598 – 6069
Beta strandi609 – 6113
Helixi613 – 62715
Helixi628 – 6303
Helixi633 – 64816
Helixi654 – 6618
Helixi662 – 6665
Helixi670 – 68718
Helixi693 – 71321
Beta strandi716 – 7183
Helixi722 – 73716
Helixi741 – 75616
Turni757 – 7593
Helixi765 – 7673
Helixi768 – 7758
Helixi779 – 79113
Helixi795 – 80511
Helixi811 – 82313
Beta strandi824 – 8274
Helixi829 – 8313
Helixi832 – 8409
Turni843 – 8453
Helixi846 – 86419
Helixi869 – 8779
Turni878 – 8814
Helixi885 – 89612
Turni897 – 9004
Turni902 – 9043
Helixi906 – 94136

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 46-941.

Miscellaneous databases

EvolutionaryTraceiQ9NZ08.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni317 – 3215Substrate binding By similarity

Sequence similaritiesi

Belongs to the peptidase M1 family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
HOVERGENiHBG108296.
InParanoidiQ9NZ08.
KOiK09604.
OMAiLIHANLT.
OrthoDBiEOG754HNR.
PhylomeDBiQ9NZ08.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

MVFLPLKWSL ATMSFLLSSL LALLTVSTPS WCQSTEASPK RSDGTPFPWN    50
KIRLPEYVIP VHYDLLIHAN LTTLTFWGTT KVEITASQPT STIILHSHHL 100
QISRATLRKG AGERLSEEPL QVLEHPRQEQ IALLAPEPLL VGLPYTVVIH 150
YAGNLSETFH GFYKSTYRTK EGELRILAST QFEPTAARMA FPCFDEPAFK 200
ASFSIKIRRE PRHLAISNMP LVKSVTVAEG LIEDHFDVTV KMSTYLVAFI 250
ISDFESVSKI TKSGVKVSVY AVPDKINQAD YALDAAVTLL EFYEDYFSIP 300
YPLPKQDLAA IPDFQSGAME NWGLTTYRES ALLFDAEKSS ASSKLGITMT 350
VAHELAHQWF GNLVTMEWWN DLWLNEGFAK FMEFVSVSVT HPELKVGDYF 400
FGKCFDAMEV DALNSSHPVS TPVENPAQIR EMFDDVSYDK GACILNMLRE 450
YLSADAFKSG IVQYLQKHSY KNTKNEDLWD SMASICPTDG VKGMDGFCSR 500
SQHSSSSSHW HQEGVDVKTM MNTWTLQKGF PLITITVRGR NVHMKQEHYM 550
KGSDGAPDTG YLWHVPLTFI TSKSDMVHRF LLKTKTDVLI LPEEVEWIKF 600
NVGMNGYYIV HYEDDGWDSL TGLLKGTHTA VSSNDRASLI NNAFQLVSIG 650
KLSIEKALDL SLYLKHETEI MPVFQGLNEL IPMYKLMEKR DMNEVETQFK 700
AFLIRLLRDL IDKQTWTDEG SVSERMLRSQ LLLLACVHNY QPCVQRAEGY 750
FRKWKESNGN LSLPVDVTLA VFAVGAQSTE GWDFLYSKYQ FSLSSTEKSQ 800
IEFALCRTQN KEKLQWLLDE SFKGDKIKTQ EFPQILTLIG RNPVGYPLAW 850
QFLRKNWNKL VQKFELGSSS IAHMVMGTTN QFSTRTRLEE VKGFFSSLKE 900
NGSQLRCVQQ TIETIEENIG WMDKNFDKIR VWLQSEKLER M 941
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 BAA25451.2 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti56 – 561E → K.
Corresponds to variant rs3734016 [ dbSNP | Ensembl ].
VAR_046681
Natural varianti127 – 1271R → P.4 Publications
Corresponds to variant rs26653 [ dbSNP | Ensembl ].
VAR_012779
Natural varianti276 – 2761I → M.
Corresponds to variant rs26618 [ dbSNP | Ensembl ].
VAR_012780
Natural varianti346 – 3461G → D.1 Publication
Corresponds to variant rs27895 [ dbSNP | Ensembl ].
VAR_012781
Natural varianti349 – 3491M → V.3 Publications
Corresponds to variant rs2287987 [ dbSNP | Ensembl ].
VAR_012782
Natural varianti528 – 5281K → R.4 Publications
Corresponds to variant rs30187 [ dbSNP | Ensembl ].
VAR_012783
Natural varianti575 – 5751D → G.
Corresponds to variant rs6863093 [ dbSNP | Ensembl ].
VAR_046682
Natural varianti575 – 5751D → N.3 Publications
Corresponds to variant rs10050860 [ dbSNP | Ensembl ].
VAR_021555
Natural varianti725 – 7251R → Q.3 Publications
Corresponds to variant rs17482078 [ dbSNP | Ensembl ].
VAR_021556
Natural varianti730 – 7301Q → E.4 Publications
Corresponds to variant rs27044 [ dbSNP | Ensembl ].
VAR_012784

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei940 – 9412RM → HDPEADATG in isoform 2.
VSP_005450

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121T → I in AAF07395. 1 Publication
Sequence conflicti12 – 121T → I in AAK37777. 1 Publication
Sequence conflicti12 – 121T → I in AAK37778. 1 Publication
Sequence conflicti514 – 5141G → R in AAF20384. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
UniGeneiHs.666524.

Genome annotation databases

EnsembliENST00000296754; ENSP00000296754; ENSG00000164307. [Q9NZ08-2]
ENST00000443439; ENSP00000406304; ENSG00000164307. [Q9NZ08-1]
GeneIDi51752.
KEGGihsa:51752.
UCSCiuc003kml.3. human. [Q9NZ08-2]
uc003kmm.3. human. [Q9NZ08-1]

Polymorphism databases

DMDMi158937334.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4085.1. [Q9NZ08-2 ]
CCDS47250.1. [Q9NZ08-1 ]
RefSeqi NP_001035548.1. NM_001040458.1. [Q9NZ08-1 ]
NP_001185470.1. NM_001198541.1. [Q9NZ08-1 ]
NP_057526.3. NM_016442.3. [Q9NZ08-2 ]
UniGenei Hs.666524.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YD0 X-ray 2.70 A 46-940 [» ]
3MDJ X-ray 2.95 A/B/C 37-939 [» ]
3QNF X-ray 3.00 A/B/C 1-941 [» ]
3RJO X-ray 2.30 A 529-941 [» ]
ProteinModelPortali Q9NZ08.
SMRi Q9NZ08. Positions 46-941.
ModBasei Search...

Protein-protein interaction databases

BioGridi 119713. 3 interactions.
IntActi Q9NZ08. 3 interactions.
STRINGi 9606.ENSP00000296754.

Chemistry

ChEMBLi CHEMBL5939.

Protein family/group databases

MEROPSi M01.018.

PTM databases

PhosphoSitei Q9NZ08.

Polymorphism databases

DMDMi 158937334.

Proteomic databases

MaxQBi Q9NZ08.
PaxDbi Q9NZ08.
PRIDEi Q9NZ08.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296754 ; ENSP00000296754 ; ENSG00000164307 . [Q9NZ08-2 ]
ENST00000443439 ; ENSP00000406304 ; ENSG00000164307 . [Q9NZ08-1 ]
GeneIDi 51752.
KEGGi hsa:51752.
UCSCi uc003kml.3. human. [Q9NZ08-2 ]
uc003kmm.3. human. [Q9NZ08-1 ]

Organism-specific databases

CTDi 51752.
GeneCardsi GC05M096124.
H-InvDB HIX0164377.
HGNCi HGNC:18173. ERAP1.
HPAi CAB025095.
HPA042317.
MIMi 606832. gene.
neXtProti NX_Q9NZ08.
PharmGKBi PA162385163.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0308.
HOVERGENi HBG108296.
InParanoidi Q9NZ08.
KOi K09604.
OMAi LIHANLT.
OrthoDBi EOG754HNR.
PhylomeDBi Q9NZ08.
TreeFami TF300395.

Enzyme and pathway databases

Reactomei REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.

Miscellaneous databases

EvolutionaryTracei Q9NZ08.
GeneWikii ARTS-1.
GenomeRNAii 51752.
NextBioi 55845.
PROi Q9NZ08.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NZ08.
Bgeei Q9NZ08.
CleanExi HS_ERAP1.
Genevestigatori Q9NZ08.

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 adipocyte-derived leucine aminopeptidase highly related to placental leucine aminopeptidase/oxytocinase."
    Hattori A., Matsumoto H., Mizutani S., Tsujimoto M.
    J. Biochem. 125:931-938(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PRO-127.
    Tissue: White adipose tissue.
  2. "Genomic organization of the human adipocyte-derived leucine aminopeptidase gene and its relationship to the placental leucine aminopeptidase/oxytocinase gene."
    Hattori A., Matsumoto K., Mizutani S., Tsujimoto M.
    J. Biochem. 130:235-241(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730.
    Tissue: Leukocyte.
  3. "Molecular characterization of human aminopeptidase PILS."
    Schomburg L.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-346; ARG-528 AND GLU-730.
  4. "Identification of an aminopeptidase regulator of type I tumor necrosis factor receptor shedding."
    Cui X., Alsaaty S., Lawrence M., Combs C.A., Rouhani F.N., Levine S.J.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730.
    Tissue: Brain.
  6. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PRO-127; VAL-349; ARG-528; ASN-575; GLN-725 AND GLU-730.
  8. "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 1).
    Tissue: Testis.
  9. "Characterization of recombinant human adipocyte-derived leucine aminopeptidase expressed in Chinese hamster ovary cells."
    Hattori A., Kitatani K., Matsumoto H., Miyazawa S., Rogi T., Tsuruoka N., Mizutani S., Natori Y., Tsujimoto M.
    J. Biochem. 128:755-762(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 37-49, CHARACTERIZATION.
  10. "Concerted peptide trimming by human ERAP1 and ERAP2 aminopeptidase complexes in the endoplasmic reticulum."
    Saveanu L., Carroll O., Lindo V., Del Val M., Lopez D., Lepelletier Y., Greer F., Schomburg L., Fruci D., Niedermann G., van Endert P.M.
    Nat. Immunol. 6:689-697(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INDUCTION BY IFNG.
  11. "The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a 'molecular ruler' mechanism."
    Chang S.-C., Momburg F., Bhutani N., Goldberg A.L.
    Proc. Natl. Acad. Sci. U.S.A. 102:17107-17112(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "An association between RBMX, a heterogeneous nuclear ribonucleoprotein, and ARTS-1 regulates extracellular TNFR1 release."
    Adamik B., Islam A., Rouhani F.N., Hawari F.I., Zhang J., Levine S.J.
    Biochem. Biophys. Res. Commun. 371:505-509(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBMX.
  13. "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-414.
    Tissue: Liver.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Crystal structure of the soluble domain of human endoplasmic reticulum aminopeptidase 1 ERAP1."
    Structural genomics consortium (SGC)
    Submitted (MAY-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 46-940 IN COMPLEX WITH ZINC IONS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-70; ASN-154 AND ASN-414.
  16. "Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1."
    Nguyen T.T., Chang S.C., Evnouchidou I., York I.A., Zikos C., Rock K.L., Goldberg A.L., Stratikos E., Stern L.J.
    Nat. Struct. Mol. Biol. 18:604-613(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 37-939 IN COMPLEX WITH ZINC IONS AND BESTATIN, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-70; ASN-154 AND ASN-760, ACTIVE SITE, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF TYR-438.

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: September 3, 2014
This is version 139 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.

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

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