Q9NZ08 (ERAP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ERAP1
Synonyms:	APPILS, ARTS1, KIAA0525
ORF Names:	UNQ584/PRO1154

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	941 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.10 Ref.11 Ref.16
Catalytic activity	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. Ref.16
Cofactor	Binds 1 zinc ion per subunit.
Subunit structure	Monomer. May also exist as a heterodimer; with ERAP2. Interacts with RBMX. Ref.10 Ref.12 Ref.16
Subcellular location	Endoplasmic reticulum membrane; Single-pass type II membrane protein Probable Ref.10.
Tissue specificity	Ubiquitous.
Induction	By IFNG/IFN-gamma. Ref.10
Post-translational modification	N-glycosylated. Ref.15 Ref.16
Sequence similarities	Belongs to the peptidase M1 family.
Caution	It is uncertain whether Met-1 or Met-13 is the initiator.
Sequence caution	The sequence BAA25451.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Adaptive immunity Immunity
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Metal-binding Zinc
Molecular function	Aminopeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Traceable author statement PubMed 15691326. Source: HGNC antigen processing and presentation of endogenous peptide antigen via MHC class I Non-traceable author statement PubMed 12748171. Source: UniProtKB fat cell differentiation Non-traceable author statement Ref.9. Source: UniProtKB membrane protein ectodomain proteolysis Inferred from direct assay PubMed 12748171. Source: UniProtKB positive regulation of angiogenesis Inferred from electronic annotation. Source: Compara regulation of blood pressure Non-traceable author statement Ref.9. Source: UniProtKB regulation of innate immune response Non-traceable author statement PubMed 12748171. Source: UniProtKB response to bacterium Inferred from expression pattern PubMed 16034137. Source: BHF-UCL
Cellular_component	cytosol Non-traceable author statement Ref.1. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement PubMed 15691326. Source: HGNC endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from direct assay Ref.9. Source: UniProtKB integral to membrane Non-traceable author statement PubMed 12748171. Source: UniProtKB
Molecular_function	aminopeptidase activity Inferred from direct assay Ref.1PubMed 12748171. Source: UniProtKB interleukin-1, Type II receptor binding Traceable author statement PubMed 15691326. Source: HGNC metalloexopeptidase activity Inferred from direct assay Ref.1. Source: UniProtKB zinc ion binding Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IL6R	P08887	1	EBI-299412,EBI-299383

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NZ08-1)

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.

Isoform 2 (identifier: Q9NZ08-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 941

941

Endoplasmic reticulum aminopeptidase 1

PRO_0000026751

Regions

Topological domain

1

1

Cytoplasmic Potential

Transmembrane

2 – 21

20

Helical; Signal-anchor for type II membrane protein; Potential

Topological domain

22 – 941

920

Lumenal Potential

Region

317 – 321

5

Substrate binding By similarity

Sites

Active site

354

1

Proton acceptor By similarity

Metal binding

353

1

Zinc; catalytic

Metal binding

357

1

Zinc; catalytic

Metal binding

376

1

Zinc; catalytic

Binding site

183

1

Substrate By similarity

Site

438

1

Transition state stabilizer By similarity

Amino acid modifications

Glycosylation

70

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

154

1

N-linked (GlcNAc...) Ref.15 Ref.16

Glycosylation

414

1

N-linked (GlcNAc...) Ref.13 Ref.15

Glycosylation

760

1

N-linked (GlcNAc...) Ref.16

Glycosylation

901

1

N-linked (GlcNAc...) Potential

Disulfide bond

404 ↔ 443

Ref.15 Ref.16

Disulfide bond

736 ↔ 743

Ref.15 Ref.16

Natural variations

Alternative sequence

940 – 941

2

RM → HDPEADATG in isoform 2.

VSP_005450

Natural variant

56

1

E → K.
Corresponds to variant rs3734016 [ dbSNP | Ensembl ].

VAR_046681

Natural variant

127

1

R → P. Ref.1 Ref.2 Ref.5 Ref.7
Corresponds to variant rs26653 [ dbSNP | Ensembl ].

VAR_012779

Natural variant

276

1

I → M.
Corresponds to variant rs26618 [ dbSNP | Ensembl ].

VAR_012780

Natural variant

346

1

G → D. Ref.3
Corresponds to variant rs27895 [ dbSNP | Ensembl ].

VAR_012781

Natural variant

349

1

M → V. Ref.2 Ref.5 Ref.7
Corresponds to variant rs2287987 [ dbSNP | Ensembl ].

VAR_012782

Natural variant

528

1

K → R. Ref.2 Ref.3 Ref.5 Ref.7
Corresponds to variant rs30187 [ dbSNP | Ensembl ].

VAR_012783

Natural variant

575

1

D → G.
Corresponds to variant rs6863093 [ dbSNP | Ensembl ].

VAR_046682

Natural variant

575

1

D → N. Ref.2 Ref.5 Ref.7
Corresponds to variant rs10050860 [ dbSNP | Ensembl ].

VAR_021555

Natural variant

725

1

R → Q. Ref.2 Ref.5 Ref.7
Corresponds to variant rs17482078 [ dbSNP | Ensembl ].

VAR_021556

Natural variant

730

1

Q → E. Ref.2 Ref.3 Ref.5 Ref.7
Corresponds to variant rs27044 [ dbSNP | Ensembl ].

VAR_012784

Experimental info

Mutagenesis

438

1

Y → F: Loss of enzyme activity. Ref.16

Sequence conflict

12

1

T → I in AAF07395. Ref.1

Sequence conflict

12

1

T → I in AAK37777. Ref.2

Sequence conflict

12

1

T → I in AAK37778. Ref.2

Sequence conflict

514

1

G → R in AAF20384. Ref.3

Secondary structure

1

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941

Helix Strand Turn

Details...

Beta strand

56 – 70

15

Turn

71 – 74

4

Beta strand

75 – 88

14

Beta strand

90 – 96

7

Beta strand

101 – 109

9

Beta strand

116 – 119

4

Beta strand

121 – 125

5

Turn

126 – 129

4

Beta strand

130 – 139

10

Beta strand

145 – 154

10

Beta strand

156 – 168

13

Beta strand

174 – 181

8

Turn

183 – 186

4

Helix

187 – 190

4

Beta strand

201 – 209

9

Beta strand

214 – 219

6

Beta strand

221 – 228

8

Beta strand

231 – 236

6

Helix

244 – 246

3

Beta strand

249 – 252

4

Beta strand

255 – 260

6

Beta strand

266 – 271

6

Turn

273 – 275

3

Helix

276 – 278

3

Helix

280 – 296

17

Beta strand

303 – 313

11

Beta strand

315 – 319

5

Beta strand

324 – 328

5

Helix

329 – 331

3

Turn

336 – 338

3

Helix

341 – 356

16

Turn

357 – 359

3

Turn

361 – 363

3

Beta strand

364 – 368

5

Helix

369 – 372

4

Helix

373 – 390

18

Helix

392 – 394

3

Helix

396 – 399

4

Helix

400 – 411

12

Helix

426 – 431

6

Helix

435 – 451

17

Helix

454 – 468

15

Beta strand

471 – 473

3

Helix

475 – 483

9

Helix

517 – 525

9

Beta strand

530 – 538

9

Beta strand

541 – 549

9

Beta strand

565 – 573

9

Beta strand

578 – 582

5

Beta strand

584 – 590

7

Beta strand

598 – 606

9

Beta strand

609 – 611

3

Helix

613 – 627

15

Helix

628 – 630

3

Helix

633 – 648

16

Helix

654 – 661

8

Helix

662 – 666

5

Helix

670 – 687

18

Helix

693 – 713

21

Beta strand

716 – 718

3

Helix

722 – 737

16

Helix

741 – 756

16

Turn

757 – 759

3

Helix

765 – 767

3

Helix

768 – 775

8

Helix

779 – 791

13

Helix

795 – 805

11

Helix

811 – 823

13

Beta strand

824 – 827

4

Helix

829 – 831

3

Helix

832 – 840

9

Turn

843 – 845

3

Helix

846 – 864

19

Helix

869 – 877

9

Turn

878 – 881

4

Helix

885 – 896

12

Turn

897 – 900

4

Turn

902 – 904

3

Helix

906 – 941

36

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 24, 2007. Version 3. Checksum: 22A0795C90155F04	FASTA	941	107,235
	10 20 30 40 50 60 MVFLPLKWSL ATMSFLLSSL LALLTVSTPS WCQSTEASPK RSDGTPFPWN KIRLPEYVIP 70 80 90 100 110 120 VHYDLLIHAN LTTLTFWGTT KVEITASQPT STIILHSHHL QISRATLRKG AGERLSEEPL 130 140 150 160 170 180 QVLEHPRQEQ IALLAPEPLL VGLPYTVVIH YAGNLSETFH GFYKSTYRTK EGELRILAST 190 200 210 220 230 240 QFEPTAARMA FPCFDEPAFK ASFSIKIRRE PRHLAISNMP LVKSVTVAEG LIEDHFDVTV 250 260 270 280 290 300 KMSTYLVAFI ISDFESVSKI TKSGVKVSVY AVPDKINQAD YALDAAVTLL EFYEDYFSIP 310 320 330 340 350 360 YPLPKQDLAA IPDFQSGAME NWGLTTYRES ALLFDAEKSS ASSKLGITMT VAHELAHQWF 370 380 390 400 410 420 GNLVTMEWWN DLWLNEGFAK FMEFVSVSVT HPELKVGDYF FGKCFDAMEV DALNSSHPVS 430 440 450 460 470 480 TPVENPAQIR EMFDDVSYDK GACILNMLRE YLSADAFKSG IVQYLQKHSY KNTKNEDLWD 490 500 510 520 530 540 SMASICPTDG VKGMDGFCSR SQHSSSSSHW HQEGVDVKTM MNTWTLQKGF PLITITVRGR 550 560 570 580 590 600 NVHMKQEHYM KGSDGAPDTG YLWHVPLTFI TSKSDMVHRF LLKTKTDVLI LPEEVEWIKF 610 620 630 640 650 660 NVGMNGYYIV HYEDDGWDSL TGLLKGTHTA VSSNDRASLI NNAFQLVSIG KLSIEKALDL 670 680 690 700 710 720 SLYLKHETEI MPVFQGLNEL IPMYKLMEKR DMNEVETQFK AFLIRLLRDL IDKQTWTDEG 730 740 750 760 770 780 SVSERMLRSQ LLLLACVHNY QPCVQRAEGY FRKWKESNGN LSLPVDVTLA VFAVGAQSTE 790 800 810 820 830 840 GWDFLYSKYQ FSLSSTEKSQ IEFALCRTQN KEKLQWLLDE SFKGDKIKTQ EFPQILTLIG 850 860 870 880 890 900 RNPVGYPLAW QFLRKNWNKL VQKFELGSSS IAHMVMGTTN QFSTRTRLEE VKGFFSSLKE 910 920 930 940 NGSQLRCVQQ TIETIEENIG WMDKNFDKIR VWLQSEKLER M
	Isoform 2 [UniParc]. Checksum: B7DEE159B1D591EE	FASTA	948	107,841
	10 20 30 40 50 60 MVFLPLKWSL ATMSFLLSSL LALLTVSTPS WCQSTEASPK RSDGTPFPWN KIRLPEYVIP 70 80 90 100 110 120 VHYDLLIHAN LTTLTFWGTT KVEITASQPT STIILHSHHL QISRATLRKG AGERLSEEPL 130 140 150 160 170 180 QVLEHPRQEQ IALLAPEPLL VGLPYTVVIH YAGNLSETFH GFYKSTYRTK EGELRILAST 190 200 210 220 230 240 QFEPTAARMA FPCFDEPAFK ASFSIKIRRE PRHLAISNMP LVKSVTVAEG LIEDHFDVTV 250 260 270 280 290 300 KMSTYLVAFI ISDFESVSKI TKSGVKVSVY AVPDKINQAD YALDAAVTLL EFYEDYFSIP 310 320 330 340 350 360 YPLPKQDLAA IPDFQSGAME NWGLTTYRES ALLFDAEKSS ASSKLGITMT VAHELAHQWF 370 380 390 400 410 420 GNLVTMEWWN DLWLNEGFAK FMEFVSVSVT HPELKVGDYF FGKCFDAMEV DALNSSHPVS 430 440 450 460 470 480 TPVENPAQIR EMFDDVSYDK GACILNMLRE YLSADAFKSG IVQYLQKHSY KNTKNEDLWD 490 500 510 520 530 540 SMASICPTDG VKGMDGFCSR SQHSSSSSHW HQEGVDVKTM MNTWTLQKGF PLITITVRGR 550 560 570 580 590 600 NVHMKQEHYM KGSDGAPDTG YLWHVPLTFI TSKSDMVHRF LLKTKTDVLI LPEEVEWIKF 610 620 630 640 650 660 NVGMNGYYIV HYEDDGWDSL TGLLKGTHTA VSSNDRASLI NNAFQLVSIG KLSIEKALDL 670 680 690 700 710 720 SLYLKHETEI MPVFQGLNEL IPMYKLMEKR DMNEVETQFK AFLIRLLRDL IDKQTWTDEG 730 740 750 760 770 780 SVSERMLRSQ LLLLACVHNY QPCVQRAEGY FRKWKESNGN LSLPVDVTLA VFAVGAQSTE 790 800 810 820 830 840 GWDFLYSKYQ FSLSSTEKSQ IEFALCRTQN KEKLQWLLDE SFKGDKIKTQ EFPQILTLIG 850 860 870 880 890 900 RNPVGYPLAW QFLRKNWNKL VQKFELGSSS IAHMVMGTTN QFSTRTRLEE VKGFFSSLKE 910 920 930 940 NGSQLRCVQQ TIETIEENIG WMDKNFDKIR VWLQSEKLEH DPEADATG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Liver.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00165949.
IPI00477831.

RefSeq

NP_001035548.1. NM_001040458.1.
NP_001185470.1. NM_001198541.1.
NP_057526.3. NM_016442.3.

UniGene

Hs.666524.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9NZ08.

ModBase

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Protein-protein interaction databases

IntAct

Q9NZ08. 3 interactions.

STRING

9606.ENSP00000296754.

Protein family/group databases

MEROPS

M01.018.

PTM databases

PhosphoSite

Q9NZ08.

Polymorphism databases

DMDM

158937334.

Proteomic databases

PaxDb

Q9NZ08.

PRIDE

Q9NZ08.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000296754; ENSP00000296754; ENSG00000164307.
ENST00000414384; ENSP00000414374; ENSG00000164307.
ENST00000443439; ENSP00000406304; ENSG00000164307.

GeneID

51752.

KEGG

hsa:51752.

UCSC

uc003kml.3. human.
uc003kmm.3. human.

Organism-specific databases

CTD

51752.

GeneCards

GC05M096124.

H-InvDB

HIX0164377.

HGNC

HGNC:18173. ERAP1.

HPA

CAB025095.

MIM

606832. gene.

neXtProt

NX_Q9NZ08.

PharmGKB

PA162385163.

HUGE

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GenAtlas

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Phylogenomic databases

eggNOG

COG0308.

HOVERGEN

HBG108296.

InParanoid

Q9NZ08.

KO

K09604.

OMA

FAVGAQT.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9NZ08.

Bgee

Q9NZ08.

CleanEx

HS_ERAP1.

Genevestigator

Q9NZ08.

GermOnline

ENSG00000164307. Homo sapiens.

Family and domain databases

InterPro

IPR024571. DUF3358.
IPR001930. Peptidase_M1.
IPR014782. Peptidase_M1_N.
[Graphical view]

PANTHER

PTHR11533. PTHR11533. 1 hit.

Pfam

PF11838. DUF3358. 1 hit.
PF01433. Peptidase_M1. 1 hit.
[Graphical view]

PRINTS

PR00756. ALADIPTASE.

PROSITE

PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

ProtoNet

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Other

ChEMBL

CHEMBL5939.

EvolutionaryTrace

Q9NZ08.

GenomeRNAi

51752.

NextBio

55845.

SOURCE

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Entry information

Entry name

ERAP1_HUMAN

Accession

Primary (citable) accession number: Q9NZ08
Secondary accession number(s): O60278 , Q6UWY6, Q8NEL4, Q8TAD0, Q9UHF8, Q9UKY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 5, 2002
Last sequence update:	July 24, 2007
Last modified:	May 1, 2013
This is version 126 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.