Q08188 (TGM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein-glutamine gamma-glutamyltransferase E
EC=2.3.2.13

Alternative name(s):
Transglutaminase E
Short name=TG(E)
Short name=TGE
Short name=TGase E
Transglutaminase-3
Short name=TGase-3

Cleaved into the following 2 chains:

1. Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain
2. Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain

Gene names

Name:

TGM3

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	693 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	Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold By similarity. In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath.
Catalytic activity	Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.
Cofactor	Binds 1 calcium ion per subunit By similarity.
Subunit structure	Consists of two polypeptide chains, which are synthesized as a precursor form of a single polypeptide.
Post-translational modification	Activated by proteolytic processing. In vitro activation is commonly achieved by cleavage with dispase, a neutral bacterial protease. Dispase cleavage site was proposed to lie between Ser-470 and Ser-471 (Ref.1) or between Pro-465 and Phe-466 (Ref.8). Physiological activation may be catalyzed by CTSL and, to a lesser extent, by CTSS, but not by CTSB, CTSD nor CTSV (Ref.8).
Sequence similarities	Belongs to the transglutaminase superfamily. Transglutaminase family.

Ontologies

Keywords
Biological process	Keratinization
Coding sequence diversity	Polymorphism
Ligand	Calcium Metal-binding
Molecular function	Acyltransferase Transferase
PTM	Acetylation Phosphoprotein Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell envelope organization Inferred from direct assay PubMed 24643. Source: UniProtKB hair follicle morphogenesis Traceable author statement PubMed 15193648. Source: UniProtKB keratinization Inferred from electronic annotation. Source: UniProtKB-KW keratinocyte differentiation Inferred from expression pattern PubMed 12850301. Source: UniProtKB peptide cross-linking Inferred from direct assay PubMed 24643. Source: UniProtKB protein tetramerization Inferred from direct assay PubMed 5038456. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay PubMed 12850301. Source: UniProtKB extrinsic to internal side of plasma membrane Inferred from direct assay PubMed 5038456. Source: UniProtKB
Molecular_function	GDP binding Inferred from direct assay PubMed 14645372. Source: UniProtKB GTP binding Inferred from direct assay PubMed 14645372. Source: UniProtKB GTPase activity Inferred from direct assay PubMed 14645372. Source: UniProtKB calcium ion binding Inferred from direct assay PubMed 14645372. Source: UniProtKB magnesium ion binding Inferred from direct assay PubMed 14645372. Source: UniProtKB protein-glutamine gamma-glutamyltransferase activity Inferred from direct assay PubMed 14645372Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 467

466

Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain

PRO_0000033652

Chain

468 – 693

226

Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain

PRO_0000033653

Sites

Active site

273

1

By similarity

Active site

331

1

By similarity

Active site

354

1

By similarity

Metal binding

394

1

Calcium By similarity

Metal binding

396

1

Calcium By similarity

Metal binding

444

1

Calcium By similarity

Metal binding

449

1

Calcium By similarity

Site

467 – 468

2

Cleavage; by CTSL

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7

Modified residue

111

1

Phosphotyrosine Ref.9

Modified residue

112

1

Phosphothreonine Ref.9

Natural variations

Natural variant

13

1

T → K. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6 Ref.7
Corresponds to variant rs214803 [ dbSNP | Ensembl ].

VAR_040067

Natural variant

163

1

I → L. Ref.3
Corresponds to variant rs6048066 [ dbSNP | Ensembl ].

VAR_040068

Natural variant

249

1

S → N. Ref.3
Corresponds to variant rs214814 [ dbSNP | Ensembl ].

VAR_040069

Natural variant

562

1

K → R. Ref.1
Corresponds to variant rs1042617 [ dbSNP | Ensembl ].

VAR_040070

Natural variant

654

1

G → R. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs214830 [ dbSNP | Ensembl ].

VAR_040071

Natural variant

687

1

L → M. Ref.3
Corresponds to variant rs45581032 [ dbSNP | Ensembl ].

VAR_055360

Experimental info

Sequence conflict

58 – 59

2

VS → DT in AAA61155. Ref.1

Sequence conflict

251

1

N → G in AAA61155. Ref.1

Sequence conflict

324

1

S → G in BAF84040. Ref.2

Sequence conflict

346

1

S → P in AAA61155. Ref.1

Sequence conflict

674

1

D → G in BAF84040. Ref.2

Secondary structure

1

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693

Helix Strand Turn

Details...

Beta strand

6 – 10

5

Helix

13 – 19

7

Beta strand

31 – 33

3

Beta strand

38 – 46

9

Beta strand

53 – 59

7

Beta strand

61 – 63

3

Turn

66 – 69

4

Beta strand

70 – 79

10

Beta strand

82 – 92

11

Beta strand

95 – 101

7

Beta strand

109 – 119

11

Beta strand

122 – 134

13

Helix

149 – 155

7

Beta strand

160 – 167

8

Beta strand

170 – 177

8

Helix

185 – 193

9

Helix

197 – 201

5

Helix

203 – 208

6

Helix

209 – 211

3

Helix

213 – 223

11

Turn

227 – 229

3

Beta strand

231 – 235

5

Helix

247 – 249

3

Helix

253 – 262

10

Beta strand

268 – 271

4

Helix

273 – 287

15

Beta strand

291 – 300

10

Beta strand

305 – 313

9

Turn

322 – 325

4

Beta strand

326 – 337

12

Turn

341 – 343

3

Helix

345 – 347

3

Beta strand

349 – 353

5

Beta strand

356 – 359

4

Helix

372 – 377

6

Turn

383 – 385

3

Helix

386 – 394

9

Beta strand

396 – 403

8

Turn

404 – 407

4

Beta strand

408 – 426

19

Beta strand

433 – 435

3

Helix

437 – 440

4

Beta strand

444 – 446

3

Helix

447 – 460

14

Beta strand

482 – 489

8

Beta strand

499 – 507

9

Beta strand

509 – 511

3

Beta strand

513 – 524

12

Beta strand

530 – 543

14

Beta strand

548 – 555

8

Helix

557 – 560

4

Turn

561 – 563

3

Beta strand

569 – 577

9

Beta strand

584 – 591

8

Beta strand

597 – 603

7

Beta strand

611 – 618

8

Beta strand

621 – 623

3

Beta strand

627 – 633

7

Turn

635 – 637

3

Beta strand

638 – 640

3

Beta strand

642 – 646

5

Beta strand

654 – 661

8

Beta strand

667 – 677

11

Beta strand

680 – 692

13

Sequences

	Sequence		Length	Mass (Da)
	Q08188 [UniParc]. Last modified September 1, 2009. Version 4. Checksum: EAFAC0C9A8AA5FD6	FASTA	693	76,632
	10 20 30 40 50 60 MAALGVQSIN WQTAFNRQAH HTDKFSSQEL ILRRGQNFQV LMIMNKGLGS NERLEFIVST 70 80 90 100 110 120 GPYPSESAMT KAVFPLSNGS SGGWSAVLQA SNGNTLTISI SSPASAPIGR YTMALQIFSQ 130 140 150 160 170 180 GGISSVKLGT FILLFNPWLN VDSVFMGNHA EREEYVQEDA GIIFVGSTNR IGMIGWNFGQ 190 200 210 220 230 240 FEEDILSICL SILDRSLNFR RDAATDVASR NDPKYVGRVL SAMINSNDDN GVLAGNWSGT 250 260 270 280 290 300 YTGGRDPRSW NGSVEILKNW KKSGFSPVRY GQCWVFAGTL NTALRSLGIP SRVITNFNSA 310 320 330 340 350 360 HDTDRNLSVD VYYDPMGNPL DKGSDSVWNF HVWNEGWFVR SDLGPSYGGW QVLDATPQER 370 380 390 400 410 420 SQGVFQCGPA SVIGVREGDV QLNFDMPFIF AEVNADRITW LYDNTTGKQW KNSVNSHTIG 430 440 450 460 470 480 RYISTKAVGS NARMDVTDKY KYPEGSDQER QVFQKALGKL KPNTPFAATS SMGLETEEQE 490 500 510 520 530 540 PSIIGKLKVA GMLAVGKEVN LVLLLKNLSR DTKTVTVNMT AWTIIYNGTL VHEVWKDSAT 550 560 570 580 590 600 MSLDPEEEAE HPIKISYAQY EKYLKSDNMI RITAVCKVPD ESEVVVERDI ILDNPTLTLE 610 620 630 640 650 660 VLNEARVRKP VNVQMLFSNP LDEPVRDCVL MVEGSGLLLG NLKIDVPTLG PKEGSRVRFD 670 680 690 ILPSRSGTKQ LLADFSCNKF PAIKAMLSID VAE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The deduced sequence of the novel protransglutaminase E (TGase3) of human and mouse." Kim I.-G., Gorman J.J., Park S.-C., Chung S.-I., Steinert P.M. J. Biol. Chem. 268:12682-12690(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LYS-13; ARG-562 AND ARG-654. Tissue: Foreskin.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LYS-13 AND ARG-654. Tissue: Tongue.
[3]	NIEHS SNPs program Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LYS-13; LEU-163; ASN-249; ARG-654 AND MET-687.
[4]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS LYS-13 AND ARG-654.
[6]	"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], VARIANTS LYS-13 AND ARG-654.
[7]	Bienvenut W.V., Bensaad K., Vousden K.H. Submitted (FEB-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13 AND 670-684, VARIANT LYS-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Osteosarcoma.
[8]	"Cystatin M/E is a high affinity inhibitor of cathepsin V and cathepsin L by a reactive site that is distinct from the legumain-binding site. A novel clue for the role of cystatin M/E in epidermal cornification." Cheng T., Hitomi K., van Vlijmen-Willems I.M., de Jongh G.J., Yamamoto K., Nishi K., Watts C., Reinheckel T., Schalkwijk J., Zeeuwen P.L. J. Biol. Chem. 281:15893-15899(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 468-479, PROTEOLYTIC CLEAVAGE BY CTSL.
[9]	"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 TYR-111 AND THR-112, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"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].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L10386 mRNA. Translation: AAA61155.1.
AK290324 mRNA. Translation: BAF83013.1.
AK291351 mRNA. Translation: BAF84040.1.
AK315236 mRNA. Translation: BAG37663.1.
EF102483 Genomic DNA. Translation: ABK41960.1.
AL031678 Genomic DNA. Translation: CAB37633.1.
CH471133 Genomic DNA. Translation: EAX10601.1.
CH471133 Genomic DNA. Translation: EAX10602.1.
BC109075 mRNA. Translation: AAI09076.1.
BC109076 mRNA. Translation: AAI09077.1.

IPI

IPI00300376.

PIR

A45991.

RefSeq

NP_003236.3. NM_003245.3.

UniGene

Hs.2022.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1L9M	X-ray	2.10	A/B	2-693	[»]
1L9N	X-ray	2.10	A/B	2-693	[»]
1NUD	X-ray	2.70	A/B	2-693	[»]
1NUF	X-ray	2.70	A	2-693	[»]
1NUG	X-ray	2.40	A/B	2-693	[»]
1RLE	X-ray	2.10	A/B	2-693	[»]
1SGX	X-ray	2.00	A/B	2-693	[»]
1VJJ	X-ray	1.90	A/B	2-693	[»]

ProteinModelPortal

Q08188.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q08188. 6 interactions.

STRING

9606.ENSP00000370867.

PTM databases

PhosphoSite

Q08188.

Polymorphism databases

DMDM

257051080.

Proteomic databases

PaxDb

Q08188.

PeptideAtlas

Q08188.

PRIDE

Q08188.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000381458; ENSP00000370867; ENSG00000125780.

GeneID

7053.

KEGG

hsa:7053.

UCSC

uc002wfx.4. human.

Organism-specific databases

CTD

7053.

GeneCards

GC20P002224.

HGNC

HGNC:11779. TGM3.

HPA

HPA004728.

MIM

600238. gene.

neXtProt

NX_Q08188.

PharmGKB

PA36492.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG80379.

HOVERGEN

HBG004342.

InParanoid

Q08188.

KO

K05620.

OMA

LVHEVWK.

OrthoDB

EOG4GMTWG.

PhylomeDB

Q08188.

Gene expression databases

Bgee

Q08188.

CleanEx

HS_TGM3.

Genevestigator

Q08188.

GermOnline

ENSG00000125780. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

IPR023608. Gln_gamma-glutamylTfrase_euk.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002931. Transglutaminase-like.
IPR008958. Transglutaminase_C.
IPR013808. Transglutaminase_CS.
IPR001102. Transglutaminase_N.
[Graphical view]

PANTHER

PTHR11590. PTHR11590. 1 hit.

Pfam

PF00927. Transglut_C. 2 hits.
PF01841. Transglut_core. 1 hit.
PF00868. Transglut_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000459. TGM_EBP42. 1 hit.

SMART

SM00460. TGc. 1 hit.
[Graphical view]

SUPFAM

SSF81296. Ig_E-set. 1 hit.
SSF49309. Transglut_C. 2 hits.

PROSITE

PS00547. TRANSGLUTAMINASES. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL3363.

DrugBank

DB00130. L-Glutamine.

EvolutionaryTrace

Q08188.

GenomeRNAi

7053.

NextBio

27579.

SOURCE

Search...

Entry information

Entry name

TGM3_HUMAN

Accession

Primary (citable) accession number: Q08188
Secondary accession number(s): A8K5N6 , B2RCR6, D3DVX1, O95933, Q32ML9, Q32MM0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	September 1, 2009
Last modified:	May 1, 2013
This is version 131 of the entry and version 4 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.