P11021 (GRP78_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
78 kDa glucose-regulated protein
Short name=GRP-78

Alternative name(s):
Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
Heat shock 70 kDa protein 5
Immunoglobulin heavy chain-binding protein
Short name=BiP

Gene names

Name:	HSPA5
Synonyms:	GRP78

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	654 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	Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Ref.12
Subunit structure	Interacts with DNAJC1 (via J domain) By similarity. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Part a large chaperone multiprotein complex comprising DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with TMEM132A and TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1. Ref.16 Ref.20 Ref.21
Subcellular location	Endoplasmic reticulum lumen. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.17 Ref.18
Involvement in disease	Note=Autoantigen in rheumatoid arthritis. Ref.10
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ER-associated protein catabolic process Traceable author statement. Source: BHF-UCL anti-apoptosis Inferred from mutant phenotype. Source: UniProtKB cellular response to glucose starvation Inferred from direct assay. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome regulation of protein folding in endoplasmic reticulum Traceable author statement. Source: BHF-UCL
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB endoplasmic reticulum chaperone complex Inferred from direct assay. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: UniProtKB endoplasmic reticulum-Golgi intermediate compartment Inferred from direct assay. Source: UniProtKB integral to endoplasmic reticulum membrane Inferred from direct assay. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell midbody Inferred from direct assay. Source: UniProtKB nucleus Inferred from direct assay. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Non-traceable author statement. Source: UniProtKB ATPase activity Inferred from sequence or structural similarity. Source: UniProtKB calcium ion binding Traceable author statement. Source: UniProtKB chaperone binding Traceable author statement. Source: BHF-UCL cysteine-type endopeptidase inhibitor activity involved in apoptotic process Inferred from direct assay. Source: UniProtKB misfolded protein binding Inferred from direct assay. Source: UniProtKB protein binding, bridging Non-traceable author statement. Source: UniProtKB protein domain specific binding Inferred from physical interaction. Source: UniProtKB ubiquitin protein ligase binding Inferred from physical interaction. Source: UniProtKB unfolded protein binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PAWR	Q96IZ0	8	EBI-354921,EBI-595869
Pawr	Q62627	4	EBI-354921,EBI-1187240	From a different organism.
RAF1	P04049	4	EBI-354921,EBI-365996

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 18

18

Ref.12 Ref.13

Chain

19 – 654

636

78 kDa glucose-regulated protein

PRO_0000013566

Regions

Motif

651 – 654

4

Prevents secretion from ER

Amino acid modifications

Modified residue

166

1

Phosphothreonine By similarity

Modified residue

268

1

N6-acetyllysine Ref.22

Modified residue

466

1

Phosphotyrosine Ref.19

Modified residue

571

1

Phosphoserine By similarity

Natural variations

Natural variant

543

1

N → H. Ref.5
Corresponds to variant rs35356639 [ dbSNP | Ensembl ].

VAR_025815

Experimental info

Sequence conflict

297

1

Missing Ref.1

Sequence conflict

297

1

Missing Ref.2

Sequence conflict

418

1

D → H Ref.1

Sequence conflict

418

1

D → H Ref.2

Sequence conflict

439

1

R → S Ref.1

Sequence conflict

439

1

R → S Ref.2

Sequence conflict

447

1

K → N Ref.1

Sequence conflict

447

1

K → N Ref.2

Secondary structure

1

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654

Helix Strand Turn

Details...

Beta strand

39 – 41

3

Beta strand

61 – 63

3

Beta strand

65 – 68

4

Helix

81 – 83

3

Beta strand

84 – 86

3

Helix

88 – 90

3

Beta strand

91 – 93

3

Helix

95 – 98

4

Helix

106 – 112

7

Beta strand

116 – 122

7

Beta strand

125 – 131

7

Beta strand

137 – 140

4

Helix

142 – 160

19

Beta strand

167 – 172

6

Helix

178 – 186

9

Beta strand

194 – 201

8

Helix

202 – 208

7

Beta strand

218 – 225

8

Beta strand

231 – 237

7

Beta strand

242 – 248

7

Helix

257 – 273

17

Helix

282 – 298

17

Turn

299 – 301

3

Beta strand

302 – 311

10

Beta strand

318 – 323

6

Helix

324 – 330

7

Helix

332 – 336

5

Helix

339 – 348

10

Helix

353 – 355

3

Beta strand

358 – 362

5

Helix

369 – 378

10

Turn

390 – 395

6

Turn

399 – 401

3

Sequences

	Sequence		Length	Mass (Da)
	P11021 [UniParc]. Last modified July 11, 2001. Version 2. Checksum: 59B7D8D85BC32A00	FASTA	654	72,333
	10 20 30 40 50 60 MKLSLVAAML LLLSAARAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV EIIANDQGNR 70 80 90 100 110 120 ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG RTWNDPSVQQ DIKFLPFKVV 130 140 150 160 170 180 EKKTKPYIQV DIGGGQTKTF APEEISAMVL TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ 190 200 210 220 230 240 RQATKDAGTI AGLNVMRIIN EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG 250 260 270 280 290 300 VFEVVATNGD THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS 310 320 330 340 350 360 SQHQARIEIE SFYEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD LKKSDIDEIV 370 380 390 400 410 420 LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV QAGVLSGDQD TGDLVLLDVC 430 440 450 460 470 480 PLTLGIETVG GVMTKLIPRN TVVPTKKSQI FSTASDNQPT VTIKVYEGER PLTKDNHLLG 490 500 510 520 530 540 TFDLTGIPPA PRGVPQIEVT FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER 550 560 570 580 590 600 MVNDAEKFAE EDKKLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE 610 620 630 640 650 KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTAE KDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation." Ting J., Lee A.S. DNA 7:275-286(1988) [PubMed: 2840249] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Chao C.C.K. Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Cervix carcinoma.
[3]	"Grp78 is involved in the quality control of the LDL-receptor." Hansen J.J., Nielsen M.N., Jorgensen M.M., Gregersen N., Bolund L. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast.
[4]	"Sequence differences between human grp78/BiP isolated from HeLa cells and previously reported human sequences." Bermudez-Fajardo A., Llewellyn D.H., Campbell A.K., Errington R.R. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	NIEHS SNPs program Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-543.
[6]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle.
[9]	"A direct-repeat sequence of the human BiP gene is required for A23187-mediated inducibility and an inducible nuclear factor binding." Chao C.C.K., Lin-Chao S. Nucleic Acids Res. 20:6481-6485(1992) [PubMed: 1480470] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
[10]	"The human endoplasmic reticulum molecular chaperone BiP is an autoantigen for rheumatoid arthritis and prevents the induction of experimental arthritis." Corrigall V.M., Bodman-Smith M.D., Fife M.S., Canas B., Myers L.K., Wooley P., Soh C., Staines N.A., Pappin D.J.C., Berlo S.E., van Eden W., van Der Zee R., Lanchbury J.S., Panayi G.S. J. Immunol. 166:1492-1498(2001) [PubMed: 11160188] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-650, DISEASE. Tissue: Articular cartilage.
[11]	"Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2." Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., Dorow D.S. Electrophoresis 18:588-598(1997) [PubMed: 9150946] [Abstract] Cited for: PROTEIN SEQUENCE OF 22-38. Tissue: Mammary carcinoma.
[12]	"Heat shock proteins bind calcitonin." Dana R.C., Welch W.J., Deftos L.J. Endocrinology 126:672-674(1990) [PubMed: 2294010] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-39, FUNCTION.
[13]	"A two-dimensional gel database of human colon carcinoma proteins." Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J. Electrophoresis 18:605-613(1997) [PubMed: 9150948] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-40. Tissue: Colon carcinoma.
[14]	Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 61-74; 82-96; 102-113; 124-152; 164-181; 186-214; 307-336; 353-367; 448-464; 475-492; 563-573; 602-617 AND 622-654, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[15]	"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins." Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M. Mol. Biol. Cell 13:4456-4469(2002) [PubMed: 12475965] [Abstract] Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[16]	"Association of stress proteins with autoantigens: a possible mechanism for triggering autoimmunity?" Purcell A.W., Todd A., Kinoshita G., Lynch T.A., Keech C.L., Gething M.J., Gordon T.P. Clin. Exp. Immunol. 132:193-200(2003) [PubMed: 12699405] [Abstract] Cited for: INTERACTION WITH TRIM21.
[17]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E. J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[18]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[19]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-466, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[20]	"Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP." Hosokawa N., Wada I., Nagasawa K., Moriyama T., Okawa K., Nagata K. J. Biol. Chem. 283:20914-20924(2008) [PubMed: 18502753] [Abstract] Cited for: INTERACTION WITH ERLEC1; OS9; SEL1L AND SYVN1.
[21]	"OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD." Christianson J.C., Shaler T.A., Tyler R.E., Kopito R.R. Nat. Cell Biol. 10:272-282(2008) [PubMed: 18264092] [Abstract] Cited for: INTERACTION WITH ERLEC1; OS9; SEL1L AND SYVN1.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-268, MASS SPECTROMETRY.
[23]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M19645 Genomic DNA. Translation: AAA52614.1.
X87949 mRNA. Translation: CAA61201.1.
AJ271729 mRNA. Translation: CAB71335.1.
AF216292 mRNA. Translation: AAF42836.1.
DQ385847 Genomic DNA. Translation: ABD04090.1.
AL354710 Genomic DNA. Translation: CAQ08732.1.
CH471090 Genomic DNA. Translation: EAW87620.1.
BC020235 mRNA. Translation: AAH20235.1.
X59969 Genomic DNA. Translation: CAA42595.1.
AF188611 mRNA. Translation: AAF13605.1. Sequence problems.

IPI

IPI00003362.

PIR

A29821.

RefSeq

NP_005338.1. NM_005347.4.

UniGene

Hs.605502.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3IUC	X-ray	2.40	A/C	26-410	[»]
3LDL	X-ray	2.30	A/B	26-407	[»]
3LDN	X-ray	2.20	A/B	26-407	[»]
3LDO	X-ray	1.95	A/B	26-407	[»]
3LDP	X-ray	2.20	A/B	26-407	[»]

ProteinModelPortal

P11021.

SMR

P11021. Positions 26-635.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33189N.

IntAct

P11021. 46 interactions.

MINT

MINT-1135308.

STRING

P11021.

PTM databases

PhosphoSite

P11021.

Polymorphism databases

DMDM

14916999.

2D gel databases

SWISS-2DPAGE

P11021.

DOSAC-COBS-2DPAGE

P11021.

OGP

P11021.

PHCI-2DPAGE

P11021.

PMMA-2DPAGE

P11021.

REPRODUCTION-2DPAGE

P11021.

Siena-2DPAGE

P11021.

UCD-2DPAGE

P11021.

Proteomic databases

PRIDE

P11021.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324460; ENSP00000324173; ENSG00000044574.

GeneID

3309.

KEGG

hsa:3309.

UCSC

uc004bpn.1. human.

Organism-specific databases

CTD

3309.

GeneCards

GC09M127997.

H-InvDB

HIX0008382.

HGNC

HGNC:5238. HSPA5.

HPA

CAB005221.
CAB019420.
HPA038845.
HPA038846.

MIM

138120. gene.

neXtProt

NX_P11021.

PharmGKB

PA29504.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14855.

HOVERGEN

HBG051845.

InParanoid

P11021.

OMA

NQLTTNP.

OrthoDB

EOG444KJV.

PhylomeDB

P11021.

Enzyme and pathway databases

Reactome

REACT_15380. Diabetes pathways.
REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P11021.

Bgee

P11021.

CleanEx

HS_HSPA5.

Genevestigator

P11021.

GermOnline

ENSG00000044574. Homo sapiens.

Family and domain databases

InterPro

IPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]

KO

K09490.

PANTHER

PTHR19375. Hsp70. 1 hit.

Pfam

PF00012. HSP70. 1 hit.
[Graphical view]

PRINTS

PR00301. HEATSHOCK70.

PROSITE

PS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00025. Antihemophilic Factor.

NextBio

13123.

SOURCE

Search...

Entry information

Entry name

GRP78_HUMAN

Accession

Primary (citable) accession number: P11021
Secondary accession number(s): B0QZ61 , Q2EF78, Q9NPF1, Q9UK02

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	July 11, 2001
Last modified:	January 25, 2012
This is version 142 of the entry and version 2 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.