Q06210 (GFPT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1
EC=2.6.1.16

Alternative name(s):
D-fructose-6-phosphate amidotransferase 1
Glutamine:fructose-6-phosphate amidotransferase 1
Short name=GFAT 1
Short name=GFAT1
Hexosephosphate aminotransferase 1

Gene names

Name:	GFPT1
Synonyms:	GFAT, GFPT

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	699 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	Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
Catalytic activity	L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.
Pathway	Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.
Subunit structure	Homotetramer Potential.
Tissue specificity	Isoform 1 is predominantly expressed in skeletal muscle. Not expressed in brain. Seems to be selectively expressed in striated muscle. Ref.4
Involvement in disease	Myasthenic syndrome, congenital, with tubular aggregates, 1 (CMSTA1) [MIM:610542]: A congenital myasthenic syndrome characterized by onset of proximal muscle weakness in the first decade. Individuals with this condition have a recognizable pattern of weakness of shoulder and pelvic girdle muscles, and sparing of ocular or facial muscles. EMG classically shows a decremental response to repeated nerve stimulation, a sign of neuromuscular junction dysfunction. Affected individuals show a favorable response to acetylcholinesterase (AChE) inhibitors. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14
Sequence similarities	Contains 1 glutamine amidotransferase type-2 domain. Contains 2 SIS domains.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Disease	Congenital myasthenic syndrome Disease mutation
Domain	Glutamine amidotransferase Repeat
Molecular function	Aminotransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine biosynthetic process Traceable author statement. Source: Reactome activation of signaling protein activity involved in unfolded protein response Traceable author statement. Source: Reactome carbohydrate biosynthetic process Inferred from electronic annotation. Source: InterPro cellular response to insulin stimulus Inferred from electronic annotation. Source: Compara dolichol-linked oligosaccharide biosynthetic process Traceable author statement. Source: Reactome energy reserve metabolic process Traceable author statement Ref.1. Source: ProtInc fructose 6-phosphate metabolic process Traceable author statement PubMed 8144040. Source: ProtInc glucosamine biosynthetic process Inferred from electronic annotation. Source: Compara glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of glycogen biosynthetic process Inferred from electronic annotation. Source: Compara post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome protein homotetramerization Inferred from electronic annotation. Source: Compara response to sucrose stimulus Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	amino acid binding Inferred from electronic annotation. Source: Compara carbohydrate binding Inferred from electronic annotation. Source: InterPro glutamine-fructose-6-phosphate transaminase (isomerizing) activity Traceable author statement PubMed 8144040. Source: ProtInc
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q06210-1)

Also known as: GFAT1m;

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: Q06210-2)

The sequence of this isoform differs from the canonical sequence as follows:
     229-246: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 699

698

Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

PRO_0000135280

Regions

Domain

2 – 305

304

Glutamine amidotransferase type-2

Domain

377 – 516

140

SIS 1

Domain

548 – 689

142

SIS 2

Sites

Active site

2

1

For GATase activity By similarity

Amino acid modifications

Modified residue

261

1

Phosphoserine Ref.6 Ref.7 Ref.10

Natural variations

Alternative sequence

229 – 246

18

Missing in isoform 2.

VSP_007497

Natural variant

15

1

T → A in CMSTA1. Ref.14

VAR_065339

Natural variant

15

1

T → M in CMSTA1. Ref.14

VAR_065340

Natural variant

43

1

D → V in CMSTA1. Ref.14

VAR_065341

Natural variant

111

1

R → C in CMSTA1. Ref.14

VAR_065342

Natural variant

121

1

I → T in CMSTA1. Ref.14

VAR_065343

Natural variant

199

1

V → F in CMSTA1. Ref.14

VAR_065344

Natural variant

366

1

D → Y in CMSTA1. Ref.14

VAR_065345

Natural variant

403

1

R → H in CMSTA1. Ref.14

VAR_065346

Natural variant

452

1

R → H in CMSTA1. Ref.14

VAR_065347

Natural variant

509

1

M → T in CMSTA1. Ref.14

VAR_065348

Natural variant

510

1

M → T in CMSTA1. Ref.14

VAR_065349

Natural variant

514

1

R → W in CMSTA1. Ref.14

VAR_065350

Natural variant

530

1

R → W in CMSTA1. Ref.14

VAR_065351

Secondary structure

1

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699

Helix Strand Turn

Details...

Beta strand

339 – 341

3

Helix

342 – 348

7

Helix

350 – 358

9

Turn

359 – 361

3

Turn

364 – 367

4

Helix

372 – 374

3

Turn

375 – 377

3

Helix

378 – 383

6

Beta strand

385 – 391

7

Helix

393 – 410

18

Beta strand

414 – 418

5

Helix

419 – 424

6

Beta strand

433 – 442

10

Helix

445 – 456

12

Beta strand

460 – 466

7

Helix

471 – 475

5

Beta strand

476 – 481

6

Beta strand

489 – 491

3

Helix

494 – 510

17

Turn

511 – 513

3

Helix

515 – 517

3

Helix

518 – 539

22

Helix

542 – 552

11

Beta strand

556 – 562

7

Helix

564 – 566

3

Helix

567 – 581

15

Beta strand

584 – 589

6

Helix

590 – 595

6

Helix

597 – 600

4

Beta strand

602 – 605

4

Beta strand

607 – 611

5

Helix

617 – 629

13

Beta strand

635 – 639

5

Helix

643 – 648

6

Beta strand

650 – 655

6

Turn

660 – 662

3

Helix

663 – 667

5

Helix

669 – 681

13

Beta strand

686 – 688

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (GFAT1m) [UniParc]. Last modified January 23, 2007. Version 3. Checksum: F0533A7B762C7B98	FASTA	699	78,806
	10 20 30 40 50 60 MCGIFAYLNY HVPRTRREIL ETLIKGLQRL EYRGYDSAGV GFDGGNDKDW EANACKIQLI 70 80 90 100 110 120 KKKGKVKALD EEVHKQQDMD LDIEFDVHLG IAHTRWATHG EPSPVNSHPQ RSDKNNEFIV 130 140 150 160 170 180 IHNGIITNYK DLKKFLESKG YDFESETDTE TIAKLVKYMY DNRESQDTSF TTLVERVIQQ 190 200 210 220 230 240 LEGAFALVFK SVHFPGQAVG TRRGSPLLIG VRSEHKLSTD HIPILYRTAR TQIGSKFTRW 250 260 270 280 290 300 GSQGERGKDK KGSCNLSRVD STTCLFPVEE KAVEYYFASD ASAVIEHTNR VIFLEDDDVA 310 320 330 340 350 360 AVVDGRLSIH RIKRTAGDHP GRAVQTLQME LQQIMKGNFS SFMQKEIFEQ PESVVNTMRG 370 380 390 400 410 420 RVNFDDYTVN LGGLKDHIKE IQRCRRLILI ACGTSYHAGV ATRQVLEELT ELPVMVELAS 430 440 450 460 470 480 DFLDRNTPVF RDDVCFFLSQ SGETADTLMG LRYCKERGAL TVGITNTVGS SISRETDCGV 490 500 510 520 530 540 HINAGPEIGV ASTKAYTSQF VSLVMFALMM CDDRISMQER RKEIMLGLKR LPDLIKEVLS 550 560 570 580 590 600 MDDEIQKLAT ELYHQKSVLI MGRGYHYATC LEGALKIKEI TYMHSEGILA GELKHGPLAL 610 620 630 640 650 660 VDKLMPVIMI IMRDHTYAKC QNALQQVVAR QGRPVVICDK EDTETIKNTK RTIKVPHSVD 670 680 690 CLQGILSVIP LQLLAFHLAV LRGYDVDFPR NLAKSVTVE
	Isoform 2 [UniParc]. Checksum: 5CB56FDB5E4F76FA	FASTA	681	76,759
	10 20 30 40 50 60 MCGIFAYLNY HVPRTRREIL ETLIKGLQRL EYRGYDSAGV GFDGGNDKDW EANACKIQLI 70 80 90 100 110 120 KKKGKVKALD EEVHKQQDMD LDIEFDVHLG IAHTRWATHG EPSPVNSHPQ RSDKNNEFIV 130 140 150 160 170 180 IHNGIITNYK DLKKFLESKG YDFESETDTE TIAKLVKYMY DNRESQDTSF TTLVERVIQQ 190 200 210 220 230 240 LEGAFALVFK SVHFPGQAVG TRRGSPLLIG VRSEHKLSTD HIPILYRTGK DKKGSCNLSR 250 260 270 280 290 300 VDSTTCLFPV EEKAVEYYFA SDASAVIEHT NRVIFLEDDD VAAVVDGRLS IHRIKRTAGD 310 320 330 340 350 360 HPGRAVQTLQ MELQQIMKGN FSSFMQKEIF EQPESVVNTM RGRVNFDDYT VNLGGLKDHI 370 380 390 400 410 420 KEIQRCRRLI LIACGTSYHA GVATRQVLEE LTELPVMVEL ASDFLDRNTP VFRDDVCFFL 430 440 450 460 470 480 SQSGETADTL MGLRYCKERG ALTVGITNTV GSSISRETDC GVHINAGPEI GVASTKAYTS 490 500 510 520 530 540 QFVSLVMFAL MMCDDRISMQ ERRKEIMLGL KRLPDLIKEV LSMDDEIQKL ATELYHQKSV 550 560 570 580 590 600 LIMGRGYHYA TCLEGALKIK EITYMHSEGI LAGELKHGPL ALVDKLMPVI MIIMRDHTYA 610 620 630 640 650 660 KCQNALQQVV ARQGRPVVIC DKEDTETIKN TKRTIKVPHS VDCLQGILSV IPLQLLAFHL 670 680 AVLRGYDVDF PRNLAKSVTV E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase." McKnight G.L., Mudri S.L., Mathewes S.L., Traxinger R.R., Marshall S., Sheppard P.O., O'Hara P.J. J. Biol. Chem. 267:25208-25212(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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 2).
[4]	"A novel variant of glutamine:fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle." DeHaven J.E., Robinson K.A., Nelson B.A., Buse M.G. Diabetes 50:2419-2424(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 124-275 (ISOFORM 1), TISSUE SPECIFICITY.
[5]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Liver.
[9]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"Hexosamine biosynthetic pathway mutations cause neuromuscular transmission defect." Senderek J., Muller J.S., Dusl M., Strom T.M., Guergueltcheva V., Diepolder I., Laval S.H., Maxwell S., Cossins J., Krause S., Muelas N., Vilchez J.J., Colomer J., Mallebrera C.J., Nascimento A., Nafissi S., Kariminejad A., Nilipour Y. , Bozorgmehr B., Najmabadi H., Rodolico C., Sieb J.P., Steinlein O.K., Schlotter B., Schoser B., Kirschner J., Herrmann R., Voit T., Oldfors A., Lindbergh C., Urtizberea A., von der Hagen M., Hubner A., Palace J., Bushby K., Straub V., Beeson D., Abicht A., Lochmuller H. Am. J. Hum. Genet. 88:162-172(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMSTA1 ALA-15; MET-15; VAL-43; CYS-111; THR-121; PHE-199; TYR-366; HIS-403; HIS-452; THR-509; THR-510; TRP-514 AND TRP-530.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M90516 mRNA. Translation: AAA58502.1.
AC114772 Genomic DNA. Translation: AAY14827.1.
BC045641 mRNA. Translation: AAH45641.1.
AF334737 mRNA. Translation: AAK15342.1.

IPI

IPI00217952.
IPI00299506.

PIR

A45055.

RefSeq

NP_001231639.1. NM_001244710.1.
NP_002047.2. NM_002056.3.

UniGene

Hs.580300.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V4M	X-ray	2.29	A/B/C/D	332-699	[»]
2ZJ3	X-ray	1.90	A	332-699	[»]
2ZJ4	X-ray	2.20	A	332-699	[»]

ProteinModelPortal

Q06210.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q06210. 3 interactions.

STRING

9606.ENSP00000354347.

Protein family/group databases

MEROPS

C44.970.

PTM databases

PhosphoSite

Q06210.

Polymorphism databases

DMDM

30923274.

Proteomic databases

PaxDb

Q06210.

PRIDE

Q06210.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000357308; ENSP00000349860; ENSG00000198380.
ENST00000361060; ENSP00000354347; ENSG00000198380.

GeneID

2673.

KEGG

hsa:2673.

UCSC

uc002sfh.3. human.
uc002sfi.2. human.

Organism-specific databases

CTD

2673.

GeneCards

GC02M069546.

HGNC

HGNC:4241. GFPT1.

HPA

HPA047240.

MIM

138292. gene.
610542. phenotype.

neXtProt

NX_Q06210.

Orphanet

590. Congenital myasthenic syndromes.

PharmGKB

PA28651.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0449.

HOGENOM

HOG000258898.

HOVERGEN

HBG051724.

InParanoid

Q06210.

KO

K00820.

OMA

HLVHWEL.

OrthoDB

EOG4DV5KT.

PhylomeDB

Q06210.

Enzyme and pathway databases

BioCyc

MetaCyc:HS09974-MONOMER.

Reactome

REACT_116125. Disease.
REACT_17015. Metabolism of proteins.

UniPathway

UPA00113; UER00528.

Gene expression databases

Bgee

Q06210.

CleanEx

HS_GFPT1.

Genevestigator

Q06210.

GermOnline

ENSG00000198380. Homo sapiens.

Family and domain databases

InterPro

IPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR001347. SIS.
[Graphical view]

Pfam

PF00310. GATase_2. 2 hits.
PF01380. SIS. 2 hits.
[Graphical view]

TIGRFAMs

TIGR01135. glmS. 1 hit.

PROSITE

PS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q06210.

ChEMBL

CHEMBL1909481.

ChiTaRS

GFPT1. human.

EvolutionaryTrace

Q06210.

GenomeRNAi

2673.

NextBio

10550.

SOURCE

Search...

Entry information

Entry name

GFPT1_HUMAN

Accession

Primary (citable) accession number: Q06210
Secondary accession number(s): Q53QE6, Q9BXF8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 128 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.