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Q6P179

- ERAP2_HUMAN

UniProt

Q6P179 - ERAP2_HUMAN

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Protein
Endoplasmic reticulum aminopeptidase 2
Gene
ERAP2, LRAP
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

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei200 – 2001Substrate
Metal bindingi370 – 3701Zinc; catalytic
Active sitei371 – 3711Proton acceptor1 Publication
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
Complete GO annotation...

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; Single-pass type II membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2020Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei21 – 4020Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini41 – 960920Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: HGNC
  2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  3. 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 2
PRO_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.2 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.3 Publications

Gene expression databases

ArrayExpressiQ6P179.
BgeeiQ6P179.
CleanExiHS_ERAP2.
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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the peptidase M1 family.

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0308.
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

MFHSSAMVNS HRKPMFNIHR GFYCLTAILP QICICSQFSV PSSYHFTEDP    50
GAFPVATNGE RFPWQELRLP SVVIPLHYDL FVHPNLTSLD FVASEKIEVL 100
VSNATQFIIL HSKDLEITNA TLQSEEDSRY MKPGKELKVL SYPAHEQIAL 150
LVPEKLTPHL KYYVAMDFQA KLGDGFEGFY KSTYRTLGGE TRILAVTDFE 200
PTQARMAFPC FDEPLFKANF SIKIRRESRH IALSNMPKVK TIELEGGLLE 250
DHFETTVKMS TYLVAYIVCD FHSLSGFTSS GVKVSIYASP DKRNQTHYAL 300
QASLKLLDFY EKYFDIYYPL SKLDLIAIPD FAPGAMENWG LITYRETSLL 350
FDPKTSSASD KLWVTRVIAH ELAHQWFGNL VTMEWWNDIW LKEGFAKYME 400
LIAVNATYPE LQFDDYFLNV CFEVITKDSL NSSRPISKPA ETPTQIQEMF 450
DEVSYNKGAC ILNMLKDFLG EEKFQKGIIQ YLKKFSYRNA KNDDLWSSLS 500
NSCLESDFTS GGVCHSDPKM TSNMLAFLGE NAEVKEMMTT WTLQKGIPLL 550
VVKQDGCSLR LQQERFLQGV FQEDPEWRAL QERYLWHIPL TYSTSSSNVI 600
HRHILKSKTD TLDLPEKTSW VKFNVDSNGY YIVHYEGHGW DQLITQLNQN 650
HTLLRPKDRV GLIHDVFQLV GAGRLTLDKA LDMTYYLQHE TSSPALLEGL 700
SYLESFYHMM DRRNISDISE NLKRYLLQYF KPVIDRQSWS DKGSVWDRML 750
RSALLKLACD LNHAPCIQKA AELFSQWMES SGKLNIPTDV LKIVYSVGAQ 800
TTAGWNYLLE QYELSMSSAE QNKILYALST SKHQEKLLKL IELGMEGKVI 850
KTQNLAALLH AIARRPKGQQ LAWDFVRENW THLLKKFDLG SYDIRMIISG 900
TTAHFSSKDK LQEVKLFFES LEAQGSHLDI FQTVLETITK NIKWLEKNLP 950
TLRTWLMVNT 960
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

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.
VSP_030671Add
BLAST
Alternative sequencei324 – 35027DLIAI…ETSLL → GMFKFHIIVFIFAHKTCFDL FPLSLSM in isoform 4.
VSP_030672Add
BLAST
Alternative sequencei351 – 960610Missing in isoform 4.
VSP_030673Add
BLAST
Alternative sequencei525 – 5328LAFLGENA → VRIKRVTE in isoform 2.
VSP_030674
Alternative sequencei533 – 960428Missing in isoform 2.
VSP_030675Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti129 – 1291R → K in AAH17927. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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...

Protein-protein interaction databases

IntActi Q6P179. 1 interaction.
STRINGi 9606.ENSP00000342447.

Chemistry

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 GC05P096238.
H-InvDB HIX0005053.
HGNCi HGNC:29499. ERAP2.
HPAi CAB025618.
HPA034498.
MIMi 609497. gene.
neXtProti NX_Q6P179.
PharmGKBi PA162385208.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0308.
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

ArrayExpressi Q6P179.
Bgeei Q6P179.
CleanExi HS_ERAP2.
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: September 3, 2014
This is version 95 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

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