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Q6P179

- ERAP2_HUMAN

UniProt

Q6P179 - ERAP2_HUMAN

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Protein

Endoplasmic reticulum aminopeptidase 2

Gene

ERAP2

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. Preferentially hydrolyzes the basic residues Arg and Lys.3 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei200 – 2001Substrate1 Publication
Metal bindingi370 – 3701Zinc; catalytic
Active sitei371 – 3711Proton acceptor1 PublicationPROSITE-ProRule annotation
Metal bindingi374 – 3741Zinc; catalytic
Metal bindingi393 – 3931Zinc; catalytic
Sitei455 – 4551Transition state stabilizer

GO - Molecular functioni

  1. aminopeptidase activity Source: HGNC
  2. metallopeptidase activity Source: HGNC
  3. zinc ion binding Source: HGNC

GO - Biological processi

  1. antigen processing and presentation of endogenous peptide antigen via MHC class I Source: HGNC
  2. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  3. regulation of blood pressure Source: HGNC
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.
SABIO-RKQ6P179.

Protein family/group databases

MEROPSiM01.024.

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum aminopeptidase 2 (EC:3.4.11.-)
Alternative name(s):
Leukocyte-derived arginine aminopeptidase
Short name:
L-RAP
Gene namesi
Name:ERAP2
Synonyms:LRAP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:29499. ERAP2.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei21 – 4020Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini41 – 960920LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: HGNC
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162385208.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 960960Endoplasmic reticulum aminopeptidase 2PRO_0000315719Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi85 – 851N-linked (GlcNAc...)1 Publication
Glycosylationi119 – 1191N-linked (GlcNAc...)1 Publication
Glycosylationi405 – 4051N-linked (GlcNAc...)1 Publication
Disulfide bondi421 ↔ 4601 Publication
Glycosylationi650 – 6501N-linked (GlcNAc...)1 Publication
Disulfide bondi759 ↔ 7661 Publication

Post-translational modificationi

N-glycosylated.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ6P179.
PaxDbiQ6P179.
PeptideAtlasiQ6P179.
PRIDEiQ6P179.

PTM databases

PhosphoSiteiQ6P179.

Expressioni

Tissue specificityi

Ubiquitously expressed. Highly expressed in spleen and leukocytes.1 Publication

Inductioni

By IFNG/IFN-gamma.2 Publications

Gene expression databases

BgeeiQ6P179.
CleanExiHS_ERAP2.
ExpressionAtlasiQ6P179. baseline and differential.
GenevestigatoriQ6P179.

Organism-specific databases

HPAiCAB025618.
HPA034498.

Interactioni

Subunit structurei

Heterodimer with ERAP1.2 Publications

Protein-protein interaction databases

IntActiQ6P179. 1 interaction.
STRINGi9606.ENSP00000342447.

Structurei

Secondary structure

1
960
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi57 – 604Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 8515Combined sources
Turni86 – 894Combined sources
Beta strandi90 – 10314Combined sources
Beta strandi106 – 1116Combined sources
Beta strandi116 – 1249Combined sources
Beta strandi138 – 1425Combined sources
Helixi143 – 1453Combined sources
Beta strandi147 – 1515Combined sources
Beta strandi161 – 17111Combined sources
Beta strandi173 – 18513Combined sources
Beta strandi191 – 1988Combined sources
Turni200 – 2034Combined sources
Helixi204 – 2063Combined sources
Beta strandi218 – 2269Combined sources
Beta strandi231 – 2366Combined sources
Beta strandi238 – 2436Combined sources
Beta strandi249 – 2535Combined sources
Helixi261 – 2633Combined sources
Beta strandi266 – 2694Combined sources
Beta strandi272 – 2776Combined sources
Beta strandi283 – 2886Combined sources
Helixi290 – 2967Combined sources
Helixi297 – 31418Combined sources
Beta strandi319 – 33012Combined sources
Beta strandi332 – 3365Combined sources
Beta strandi341 – 3455Combined sources
Helixi346 – 3494Combined sources
Turni353 – 3553Combined sources
Helixi358 – 37619Combined sources
Turni378 – 3803Combined sources
Beta strandi381 – 3855Combined sources
Helixi386 – 3894Combined sources
Helixi390 – 40718Combined sources
Helixi409 – 4113Combined sources
Helixi413 – 4175Combined sources
Helixi418 – 42811Combined sources
Helixi443 – 4475Combined sources
Turni452 – 4554Combined sources
Helixi456 – 46914Combined sources
Helixi471 – 48414Combined sources
Turni485 – 4873Combined sources
Beta strandi488 – 4903Combined sources
Helixi492 – 5009Combined sources
Helixi534 – 54310Combined sources
Beta strandi548 – 5558Combined sources
Beta strandi558 – 5658Combined sources
Beta strandi590 – 5923Combined sources
Beta strandi594 – 5963Combined sources
Beta strandi601 – 6033Combined sources
Beta strandi607 – 6137Combined sources
Beta strandi621 – 6244Combined sources
Helixi625 – 6273Combined sources
Beta strandi632 – 6365Combined sources
Helixi639 – 64810Combined sources
Helixi651 – 6533Combined sources
Helixi656 – 67015Combined sources
Turni671 – 6733Combined sources
Helixi677 – 6815Combined sources
Turni682 – 6854Combined sources
Helixi686 – 6883Combined sources
Helixi693 – 71220Combined sources
Helixi716 – 72813Combined sources
Helixi731 – 7355Combined sources
Helixi745 – 76016Combined sources
Helixi764 – 78017Combined sources
Helixi788 – 79811Combined sources
Helixi802 – 81211Combined sources
Helixi818 – 82912Combined sources
Helixi834 – 84613Combined sources
Beta strandi848 – 8503Combined sources
Helixi852 – 8543Combined sources
Helixi855 – 86410Combined sources
Helixi866 – 87813Combined sources
Helixi880 – 8867Combined sources
Helixi892 – 90211Combined sources
Helixi908 – 92013Combined sources
Beta strandi923 – 9253Combined sources
Helixi930 – 95930Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SE6X-ray3.08A/B1-960[»]
4E36X-ray3.22A/B1-960[»]
4JBSX-ray2.79A/B3-960[»]
ProteinModelPortaliQ6P179.
SMRiQ6P179. Positions 54-960.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni334 – 3385Substrate binding

Sequence similaritiesi

Belongs to the peptidase M1 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
GeneTreeiENSGT00760000119082.
HOGENOMiHOG000106482.
HOVERGENiHBG108296.
InParanoidiQ6P179.
KOiK13723.
OMAiYLDINRE.
OrthoDBiEOG754HNR.
PhylomeDBiQ6P179.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q6P179-1) [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
MFHSSAMVNS HRKPMFNIHR GFYCLTAILP QICICSQFSV PSSYHFTEDP
60 70 80 90 100
GAFPVATNGE RFPWQELRLP SVVIPLHYDL FVHPNLTSLD FVASEKIEVL
110 120 130 140 150
VSNATQFIIL HSKDLEITNA TLQSEEDSRY MKPGKELKVL SYPAHEQIAL
160 170 180 190 200
LVPEKLTPHL KYYVAMDFQA KLGDGFEGFY KSTYRTLGGE TRILAVTDFE
210 220 230 240 250
PTQARMAFPC FDEPLFKANF SIKIRRESRH IALSNMPKVK TIELEGGLLE
260 270 280 290 300
DHFETTVKMS TYLVAYIVCD FHSLSGFTSS GVKVSIYASP DKRNQTHYAL
310 320 330 340 350
QASLKLLDFY EKYFDIYYPL SKLDLIAIPD FAPGAMENWG LITYRETSLL
360 370 380 390 400
FDPKTSSASD KLWVTRVIAH ELAHQWFGNL VTMEWWNDIW LKEGFAKYME
410 420 430 440 450
LIAVNATYPE LQFDDYFLNV CFEVITKDSL NSSRPISKPA ETPTQIQEMF
460 470 480 490 500
DEVSYNKGAC ILNMLKDFLG EEKFQKGIIQ YLKKFSYRNA KNDDLWSSLS
510 520 530 540 550
NSCLESDFTS GGVCHSDPKM TSNMLAFLGE NAEVKEMMTT WTLQKGIPLL
560 570 580 590 600
VVKQDGCSLR LQQERFLQGV FQEDPEWRAL QERYLWHIPL TYSTSSSNVI
610 620 630 640 650
HRHILKSKTD TLDLPEKTSW VKFNVDSNGY YIVHYEGHGW DQLITQLNQN
660 670 680 690 700
HTLLRPKDRV GLIHDVFQLV GAGRLTLDKA LDMTYYLQHE TSSPALLEGL
710 720 730 740 750
SYLESFYHMM DRRNISDISE NLKRYLLQYF KPVIDRQSWS DKGSVWDRML
760 770 780 790 800
RSALLKLACD LNHAPCIQKA AELFSQWMES SGKLNIPTDV LKIVYSVGAQ
810 820 830 840 850
TTAGWNYLLE QYELSMSSAE QNKILYALST SKHQEKLLKL IELGMEGKVI
860 870 880 890 900
KTQNLAALLH AIARRPKGQQ LAWDFVRENW THLLKKFDLG SYDIRMIISG
910 920 930 940 950
TTAHFSSKDK LQEVKLFFES LEAQGSHLDI FQTVLETITK NIKWLEKNLP
960
TLRTWLMVNT
Length:960
Mass (Da):110,462
Last modified:January 15, 2008 - v2
Checksum:i261EFC06870D644E
GO
Isoform 2 (identifier: Q6P179-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     525-532: LAFLGENA → VRIKRVTE
     533-960: Missing.

Show »
Length:532
Mass (Da):60,952
Checksum:iDA0F49B61F79B920
GO
Isoform 3 (identifier: Q6P179-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     238-282: Missing.

Note: No experimental confirmation available.

Show »
Length:915
Mass (Da):105,526
Checksum:i10075BE1C076377F
GO
Isoform 4 (identifier: Q6P179-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     324-350: DLIAIPDFAPGAMENWGLITYRETSLL → GMFKFHIIVFIFAHKTCFDLFPLSLSM
     351-960: Missing.

Note: No experimental confirmation available.

Show »
Length:350
Mass (Da):40,088
Checksum:i189B8EF5D9D4BD11
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291R → K in AAH17927. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti214 – 2141P → L.
Corresponds to variant rs3733905 [ dbSNP | Ensembl ].
VAR_038285
Natural varianti392 – 3921K → N.2 Publications
Corresponds to variant rs2549782 [ dbSNP | Ensembl ].
VAR_038286
Natural varianti411 – 4111L → R.
Corresponds to variant rs34261036 [ dbSNP | Ensembl ].
VAR_051569
Natural varianti669 – 6691L → Q.
Corresponds to variant rs17408150 [ dbSNP | Ensembl ].
VAR_038287

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei238 – 28245Missing in isoform 3. 1 PublicationVSP_030671Add
BLAST
Alternative sequencei324 – 35027DLIAI…ETSLL → GMFKFHIIVFIFAHKTCFDL FPLSLSM in isoform 4. 1 PublicationVSP_030672Add
BLAST
Alternative sequencei351 – 960610Missing in isoform 4. 1 PublicationVSP_030673Add
BLAST
Alternative sequencei525 – 5328LAFLGENA → VRIKRVTE in isoform 2. 1 PublicationVSP_030674
Alternative sequencei533 – 960428Missing in isoform 2. 1 PublicationVSP_030675Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB109031 mRNA. Translation: BAC78818.1.
AB163917 mRNA. Translation: BAD90015.1.
AY028805 mRNA. Translation: AAK37776.1.
AF191545 mRNA. Translation: AAG28383.1.
CH471084 Genomic DNA. Translation: EAW96080.1.
BC065240 mRNA. Translation: AAH65240.1.
BC017927 mRNA. Translation: AAH17927.1.
CCDSiCCDS4086.1. [Q6P179-1]
RefSeqiNP_001123612.1. NM_001130140.1. [Q6P179-1]
NP_071745.1. NM_022350.3. [Q6P179-1]
UniGeneiHs.482910.

Genome annotation databases

EnsembliENST00000379904; ENSP00000369235; ENSG00000164308. [Q6P179-3]
ENST00000437043; ENSP00000400376; ENSG00000164308. [Q6P179-1]
ENST00000510309; ENSP00000425758; ENSG00000164308. [Q6P179-4]
ENST00000513084; ENSP00000421849; ENSG00000164308. [Q6P179-2]
GeneIDi64167.
KEGGihsa:64167.
UCSCiuc003kmq.3. human. [Q6P179-1]
uc003kms.3. human. [Q6P179-3]

Polymorphism databases

DMDMi166232401.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB109031 mRNA. Translation: BAC78818.1 .
AB163917 mRNA. Translation: BAD90015.1 .
AY028805 mRNA. Translation: AAK37776.1 .
AF191545 mRNA. Translation: AAG28383.1 .
CH471084 Genomic DNA. Translation: EAW96080.1 .
BC065240 mRNA. Translation: AAH65240.1 .
BC017927 mRNA. Translation: AAH17927.1 .
CCDSi CCDS4086.1. [Q6P179-1 ]
RefSeqi NP_001123612.1. NM_001130140.1. [Q6P179-1 ]
NP_071745.1. NM_022350.3. [Q6P179-1 ]
UniGenei Hs.482910.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3SE6 X-ray 3.08 A/B 1-960 [» ]
4E36 X-ray 3.22 A/B 1-960 [» ]
4JBS X-ray 2.79 A/B 3-960 [» ]
ProteinModelPortali Q6P179.
SMRi Q6P179. Positions 54-960.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q6P179. 1 interaction.
STRINGi 9606.ENSP00000342447.

Chemistry

BindingDBi Q6P179.
ChEMBLi CHEMBL5043.

Protein family/group databases

MEROPSi M01.024.

PTM databases

PhosphoSitei Q6P179.

Polymorphism databases

DMDMi 166232401.

Proteomic databases

MaxQBi Q6P179.
PaxDbi Q6P179.
PeptideAtlasi Q6P179.
PRIDEi Q6P179.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000379904 ; ENSP00000369235 ; ENSG00000164308 . [Q6P179-3 ]
ENST00000437043 ; ENSP00000400376 ; ENSG00000164308 . [Q6P179-1 ]
ENST00000510309 ; ENSP00000425758 ; ENSG00000164308 . [Q6P179-4 ]
ENST00000513084 ; ENSP00000421849 ; ENSG00000164308 . [Q6P179-2 ]
GeneIDi 64167.
KEGGi hsa:64167.
UCSCi uc003kmq.3. human. [Q6P179-1 ]
uc003kms.3. human. [Q6P179-3 ]

Organism-specific databases

CTDi 64167.
GeneCardsi GC05P096211.
H-InvDB HIX0005053.
HGNCi HGNC:29499. ERAP2.
HPAi CAB025618.
HPA034498.
MIMi 609497. gene.
neXtProti NX_Q6P179.
PharmGKBi PA162385208.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0308.
GeneTreei ENSGT00760000119082.
HOGENOMi HOG000106482.
HOVERGENi HBG108296.
InParanoidi Q6P179.
KOi K13723.
OMAi YLDINRE.
OrthoDBi EOG754HNR.
PhylomeDBi Q6P179.
TreeFami TF300395.

Enzyme and pathway databases

Reactomei REACT_75795. Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
SABIO-RK Q6P179.

Miscellaneous databases

GenomeRNAii 64167.
NextBioi 66072.
PROi Q6P179.
SOURCEi Search...

Gene expression databases

Bgeei Q6P179.
CleanExi HS_ERAP2.
ExpressionAtlasi Q6P179. baseline and differential.
Genevestigatori Q6P179.

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. "Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases."
    Tanioka T., Hattori A., Masuda S., Nomura Y., Nakayama H., Mizutani S., Tsujimoto M.
    J. Biol. Chem. 278:32275-32283(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, GLYCOSYLATION, TOPOLOGY, TISSUE SPECIFICITY, VARIANT ASN-392.
  2. "Regulation of the human leukocyte-derived arginine aminopeptidase/endoplasmic reticulum-aminopeptidase 2 gene by interferon-gamma."
    Tanioka T., Hattori A., Mizutani S., Tsujimoto M.
    FEBS J. 272:916-928(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INDUCTION BY IFNG, VARIANT ASN-392.
  3. "Molecular characterization of aminopeptidase MAMS."
    Schomburg L.
    Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORMS 3 AND 4).
    Tissue: Skeletal muscle and Skin.
  6. "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-119.
    Tissue: Plasma.
  7. "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, SUBUNIT, INDUCTION BY IFNG.
  8. "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.
  9. "Expression of endoplasmic reticulum aminopeptidases in EBV-B cell lines from healthy donors and in leukemia/lymphoma, carcinoma, and melanoma cell lines."
    Fruci D., Ferracuti S., Limongi M.Z., Cunsolo V., Giorda E., Fraioli R., Sibilio L., Carroll O., Hattori A., van Endert P.M., Giacomini P.
    J. Immunol. 176:4869-4879(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE REGULATION.
  10. "Inactivation of RB1 in mantle-cell lymphoma detected by nonsense-mediated mRNA decay pathway inhibition and microarray analysis."
    Pinyol M., Bea S., Pla L., Ribrag V., Bosq J., Rosenwald A., Campo E., Jares P.
    Blood 109:5422-5429(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The crystal structure of human endoplasmic reticulum aminopeptidase 2 reveals the atomic basis for distinct roles in antigen processing."
    Birtley J.R., Saridakis E., Stratikos E., Mavridis I.M.
    Biochemistry 51:286-295(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.08 ANGSTROMS) OF 3-960 IN COMPLEX WITH SUBSTRATE, GLYCOSYLATION AT ASN-85; ASN-219; ASN-405 AND ASN-650, ACTIVE SITE, ZINC-BINDING SITES, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiERAP2_HUMAN
AccessioniPrimary (citable) accession number: Q6P179
Secondary accession number(s): Q7Z5K1
, Q8TD32, Q8WVJ4, Q9HBX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: November 26, 2014
This is version 98 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

Miscellaneous

Defects in the expression of this gene may cause improper antigen processing, possibly leading to favor tumor escape from the immune surveillance.

Keywords - Technical termi

3D-structure, Complete proteome, 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