Reviewed, UniProtKB/Swiss-Prot Q96HE7 (ERO1A_HUMAN)

Names and origin

Protein names

Recommended name:
    ERO1-like protein alpha
      Short name=ERO1-L-alpha
      Short name=ERO1-L
    EC=1.8.4.-
Alternative name(s):
    Oxidoreductin-1-L-alpha
    Endoplasmic oxidoreductin-1-like protein

Gene names

Name:	ERO1L
ORF Names:	UNQ434/PRO865

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. Required for the folding of immunoglobulin proteins. Responsible for the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. Ref.1 Ref.7 Ref.9 Ref.11 Ref.17 Ref.18
Cofactor	FAD. Ref.18
Enzyme regulation	Enzyme activity is tighly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between the active site Cys-94 and Cys-131, and between Cys-99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum. Ref.17 Ref.18 Ref.15
Subunit structure	Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT. Ref.9 Ref.18 Ref.10 Ref.16
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. Note: The association with ERP44 is essential for its retention in the endoplasmic reticulum. Ref.1 Ref.13
Tissue specificity	Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. Ref.8
Induction	Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. Ref.12
Post-translational modification	N-glycosylated. Ref.1 Ref.7 Ref.20 The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-394/Cys-397 By similarity.
Sequence similarities	Belongs to the EROs family.

Ontologies

Keywords
Biological process	Electron transport Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Redox-active center Signal
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	chaperone mediated protein folding requiring cofactor Ref.9 Inferred from direct assay. Source: UniProtKB electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW protein thiol-disulfide exchange Inferred from electronic annotation. Source: InterPro response to temperature stimulus Ref.1 Traceable author statement. Source: ProtInc transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: InterPro microsome Ref.1 Traceable author statement. Source: ProtInc
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on sulfur group of donors, disulfide as acceptor Inferred from electronic annotation. Source: InterPro protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23
	Chain	24 – 468	445	ERO1-like protein alpha		PRO_0000008415
Sites
	Binding site	187	1	FAD By similarity
	Binding site	189	1	FAD By similarity
	Binding site	200	1	FAD By similarity
	Binding site	252	1	FAD By similarity
	Binding site	255	1	FAD By similarity
	Binding site	287	1	FAD By similarity
Amino acid modifications
	Glycosylation	280	1	N-linked (GlcNAc...) Ref.20
	Glycosylation	384	1	N-linked (GlcNAc...) Potential
	Disulfide bond	35 ↔ 46		Or C-35 with C-48 Ref.17 Ref.18
	Disulfide bond	37 ↔ 48		Or C-35 with C-46 Ref.17 Ref.18
	Disulfide bond	85 ↔ 391		Ref.17 Ref.18
	Disulfide bond	94 ↔ 131		Alternate Ref.17 Ref.18
	Disulfide bond	94 ↔ 99		Redox-active Ref.17 Ref.18
	Disulfide bond	99 ↔ 104		Alternate Ref.17 Ref.18
	Disulfide bond	208 ↔ 241		Ref.17 Ref.18
	Disulfide bond	394 ↔ 397		Redox-active Ref.17 Ref.18
Experimental info
	Mutagenesis	85	1	C → A: Alters protein folding and stability. Loss of regulatory disulfide bond formation and increased activity towards PDI; when associated with A-131. Ref.18 Ref.14
	Mutagenesis	85	1	C → S: Induces a decrease in activity. Ref.18 Ref.14
	Mutagenesis	94	1	C → S: Induces a decrease in activity towards thioredoxin. Loss of activity towards thioredoxin and loss of regulatory disulfide bond formation; when associated with A-99. Ref.18 Ref.14
	Mutagenesis	99	1	C → A: Acts as a weak dominant-negative mutant. Loss of activity towards thioredoxin. Loss of regulatory disulfide bond formation; when associated with A-94. Ref.18 Ref.14
	Mutagenesis	104	1	C → A: No effect. Strongly increased activity towards PDI; when associated with A-131. Ref.18 Ref.14
	Mutagenesis	104	1	C → S: No effect. Ref.18 Ref.14
	Mutagenesis	131	1	C → A: Loss of regulatory disulfide bond formation and increased activity towards PDI. Loss of regulatory disulfide bond formation and strongly increased activity towards PDI; when associated with A-85. Loss of regulatory disulfide bond formation and strongly increased activity towards PDI; when associated with A-104. Ref.17 Ref.18 Ref.14
	Mutagenesis	166	1	C → A: No effect. Ref.18 Ref.14
	Mutagenesis	208	1	C → A or S: No effect. Ref.18 Ref.14
	Mutagenesis	241	1	C → A or S: No effect. Ref.18 Ref.14
	Mutagenesis	280	1	N → A: No effect on activity. Ref.14
	Mutagenesis	384	1	N → A: No effect on activity. Ref.14
	Mutagenesis	391	1	C → A: Alters protein folding. Prevents formation of regulatory disulfide bond and down-regulation of activity. Decreases association with P4HB. Ref.1 Ref.7 Ref.14
	Mutagenesis	394	1	C → A: Retains activity towards PDI. Does not act as a dominant negative mutant. Induces defects in folding. Remains associated with P4HB. Ref.1 Ref.7 Ref.9 Ref.17 Ref.14
	Mutagenesis	397	1	C → A: Acts as a dominant negative mutant; does not induce defects in folding; remains associated with P4HB. Ref.7 Ref.9 Ref.14
	Sequence conflict	456	1	E → K in AAH08674. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q96HE7-1 [UniParc]. Last modified July 19, 2004. Version 2. Checksum: 92ECE6531C9CCA33	FASTA	468	54,393
	10 20 30 40 50 60 MGRGWGFLFG LLGAVWLLSS GHGEEQPPET AAQRCFCQVS GYLDDCTCDV ETIDRFNNYR 70 80 90 100 110 120 LFPRLQKLLE SDYFRYYKVN LKRPCPFWND ISQCGRRDCA VKPCQSDEVP DGIKSASYKY 130 140 150 160 170 180 SEEANNLIEE CEQAERLGAV DESLSEETQK AVLQWTKHDD SSDNFCEADD IQSPEAEYVD 190 200 210 220 230 240 LLLNPERYTG YKGPDAWKIW NVIYEENCFK PQTIKRPLNP LASGQGTSEE NTFYSWLEGL 250 260 270 280 290 300 CVEKRAFYRL ISGLHASINV HLSARYLLQE TWLEKKWGHN ITEFQQRFDG ILTEGEGPRR 310 320 330 340 350 360 LKNLYFLYLI ELRALSKVLP FFERPDFQLF TGNKIQDEEN KMLLLEILHE IKSFPLHFDE 370 380 390 400 410 420 NSFFAGDKKE AHKLKEDFRL HFRNISRIMD CVGCFKCRLW GKLQTQGLGT ALKILFSEKL 430 440 450 460 IANMPESGPS YEFHLTRQEI VSLFNAFGRI STSVKELENF RNLLQNIH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum." Cabibbo A., Pagani M., Fabbri M., Rocchi M., Farmery M.R., Bulleid N.J., Sitia R. J. Biol. Chem. 275:4827-4833(2000) [PubMed: 10671517] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF CYS-391 AND CYS-394. Tissue: Embryonic carcinoma.
[2]	"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: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Trachea.
[4]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye.
[6]	"The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function." Pagani M., Pilati S., Bertoli G., Valsasina B., Sitia R. FEBS Lett. 508:117-120(2001) [PubMed: 11707280] [Abstract] Cited for: PROTEIN SEQUENCE OF N-TERMINUS, MASS SPECTROMETRY.
[7]	"The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha." Benham A.M., Cabibbo A., Fassio A., Bulleid N., Sitia R., Braakman I. EMBO J. 19:4493-4502(2000) [PubMed: 10970843] [Abstract] Cited for: FUNCTION, GLYCOSYLATION, MUTAGENESIS OF CYS-391; CYS-394 AND CYS-397.
[8]	"Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response." Pagani M., Fabbri M., Benedetti C., Fassio A., Pilati S., Bulleid N.J., Cabibbo A., Sitia R. J. Biol. Chem. 275:23685-23692(2000) [PubMed: 10818100] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Manipulation of oxidative protein folding and PDI redox state in mammalian cells." Mezghrani A., Fassio A., Benham A., Simmen T., Braakman I., Sitia R. EMBO J. 20:6288-6296(2001) [PubMed: 11707400] [Abstract] Cited for: FUNCTION, POTENTIAL HOMODIMERIZATION, ASSOCIATION WITH P4HB, LACK OF ASSOCIATION WITH GRP58, MUTAGENESIS OF CYS-394 AND CYS-397.
[10]	"ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family." Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A., Sitia R. EMBO J. 21:835-844(2002) [PubMed: 11847130] [Abstract] Cited for: INTERACTION WITH ERP44.
[11]	"Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1." Tsai B., Rapoport T.A. J. Cell Biol. 159:207-216(2002) [PubMed: 12403808] [Abstract] Cited for: FUNCTION.
[12]	"The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha." Gess B., Hofbauer K.H., Wenger R.H., Lohaus C., Meyer H.E., Kurtz A. Eur. J. Biochem. 270:2228-2235(2003) [PubMed: 12752442] [Abstract] Cited for: INDUCTION.
[13]	"Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44." Anelli T., Alessio M., Bachi A., Bergamelli L., Bertoli G., Camerini S., Mezghrani A., Ruffato E., Simmen T., Sitia R. EMBO J. 22:5015-5022(2003) [PubMed: 14517240] [Abstract] Cited for: SUBCELLULAR LOCATION.
[14]	"Two conserved cysteine triads in human Ero1alpha cooperate forefficient disulfide bond formation in the ER." Bertoli G., Simmen T., Anelli T., Nerini Molteni S., Fesce R., Sitia R. J. Biol. Chem. 279:30047-30052(2004) [PubMed: 15136577] [Abstract] Cited for: MUTAGENESIS OF CYS-85; CYS-94; CYS-99; CYS-104; CYS-131; CYS-166; CYS-208; CYS-241; ASN-280; ASN-384; CYS-391; CYS-394 AND CYS-397.
[15]	"Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum." Nerini Molteni S., Fassio A., Ciriolo M.R., Filomeni G., Pasqualetto E., Fagioli C., Sitia R. J. Biol. Chem. 279:32667-32673(2004) [PubMed: 15161913] [Abstract] Cited for: ENZYME REGULATION.
[16]	"PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum." van Lith M., Hartigan N., Hatch J., Benham A.M. J. Biol. Chem. 280:1376-1383(2005) [PubMed: 15475357] [Abstract] Cited for: INTERACTION WITH PDILT.
[17]	"A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells." Appenzeller-Herzog C., Riemer J., Christensen B., Soerensen E.S., Ellgaard L. EMBO J. 27:2977-2987(2008) [PubMed: 18833192] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, DISULFIDE BONDS, MUTAGENESIS OF CYS-131 AND CYS-394, MASS SPECTROMETRY.
[18]	"Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation." Baker K.M., Chakravarthi S., Langton K.P., Sheppard A.M., Lu H., Bulleid N.J. EMBO J. 27:2988-2997(2008) [PubMed: 18971943] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, COFACTOR, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-85; CYS-94; CYS-99; CYS-104; CYS-131; CYS-166; CYS-208 AND CYS-241.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-280, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF081886 mRNA. Translation: AAF35260.1. AF123887 mRNA. Translation: AAF06104.1. AY358463 mRNA. Translation: AAQ88828.1. AK292839 mRNA. Translation: BAF85528.1. AL133453 Genomic DNA. No translation available. BC008674 mRNA. Translation: AAH08674.1. BC012941 mRNA. Translation: AAH12941.1.
IPI	IPI00386755.
RefSeq	NP_055399.1.
UniGene	Hs.592304
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q96HE7.
Proteomic databases
PeptideAtlas	Q96HE7.
PRIDE	Q96HE7.
Genome annotation databases
Ensembl	ENST00000395686; ENSP00000379042; ENSG00000197930; Homo sapiens. [Genome view]
GeneID	30001.
KEGG	hsa:30001.
UCSC	uc001wzv.1. human.
Organism-specific databases
CTD	30001.
GeneCards	GC14M052178.
H-InvDB	HIX0011660.
HGNC	HGNC:13280. ERO1L.
HPA	HPA026653.
PharmGKB	PA27862.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG521237.
HOVERGEN	Q96HE7.
OMA	DDIQSPD.
OrthoDB	EOG9RBT4J.
Enzyme and pathway databases
BioCyc	CATTLE:ENSBTAG00000015716-MON.
Reactome	REACT_15380. Diabetes pathways.
Gene expression databases
ArrayExpress	Q96HE7.
Bgee	Q96HE7.
CleanEx	HS_ERO1L.
Genevestigator	Q96HE7.
GermOnline	ENSG00000197930. Homo sapiens.
Family and domain databases
InterPro	IPR007266. ERO1. [Graphical view]
PANTHER	PTHR12613. ERO1. 1 hit.
Pfam	PF04137. ERO1. 1 hit. [Graphical view]
PIRSF	PIRSF017205. ERO1. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	52816.

Entry information

Entry name

ERO1A_HUMAN

Accession

Primary (citable) accession number: Q96HE7
Secondary accession number(s): A8K9X4 , A8MYW1, Q7LD45, Q9P1Q9, Q9UKV6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	December 15, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.