P49354 (FNTA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
EC=2.5.1.58
EC=2.5.1.59

Alternative name(s):
CAAX farnesyltransferase subunit alpha
FTase-alpha
Ras proteins prenyltransferase subunit alpha
Type I protein geranyl-geranyltransferase subunit alpha
Short name=GGTase-I-alpha

Gene names

Name:

FNTA

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	379 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of a farnesyl or geranyl-geranyl moiety from farnesyl or geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. The alpha subunit is thought to participate in a stable complex with the substrate. The beta subunit binds the peptide substrate. Through RAC1 prenylation and activation may positively regulate neuromuscular junction development downstream of MUSK By similarity.
Catalytic activity	Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate. Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.
Enzyme regulation	Activated by the AGRIN-induced phosphorylation which is mediated by MUSK By similarity.
Subunit structure	Heterodimer of an alpha and a beta subunit. Interacts with MUSK; the interaction is direct and mediates AGRIN-induced phosphorylation of FNTA By similarity. Ref.14 Ref.15 Ref.16
Post-translational modification	Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA By similarity.
Sequence similarities	Belongs to the protein prenyltransferase subunit alpha family. Contains 5 PFTA repeats.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Domain	Repeat
Molecular function	Prenyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome neurotransmitter receptor metabolic process Inferred from electronic annotation. Source: Compara positive regulation of deacetylase activity Inferred from direct assay PubMed 19228685. Source: BHF-UCL positive regulation of tubulin deacetylation Inferred from direct assay PubMed 19228685. Source: BHF-UCL protein farnesylation Inferred from direct assay PubMed 19228685. Source: BHF-UCL protein geranylgeranylation Traceable author statement PubMed 8106351. Source: ProtInc transforming growth factor beta receptor signaling pathway Traceable author statement PubMed 8599089. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome microtubule associated complex Inferred from direct assay PubMed 19228685. Source: BHF-UCL
Molecular_function	CAAX-protein geranylgeranyltransferase activity Inferred from electronic annotation. Source: EC Rab geranylgeranyltransferase activity Inferred from electronic annotation. Source: Compara acetylcholine receptor regulator activity Inferred from electronic annotation. Source: Compara alpha-tubulin binding Inferred from direct assay PubMed 19228685. Source: BHF-UCL microtubule binding Inferred from direct assay PubMed 19228685. Source: BHF-UCL protein farnesyltransferase activity Traceable author statement Ref.1. Source: ProtInc protein geranylgeranyltransferase activity Traceable author statement PubMed 8106351. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FNTB	P49356	7	EBI-602336,EBI-602349

Alternative products

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

Isoform 1 (identifier: P49354-1)

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: P49354-2)

The sequence of this isoform differs from the canonical sequence as follows:
     68-134: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 379

379

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

PRO_0000119746

Regions

Repeat

112 – 146

35

PFTA 1

Repeat

147 – 180

34

PFTA 2

Repeat

181 – 215

35

PFTA 3

Repeat

216 – 249

34

PFTA 4

Repeat

255 – 289

35

PFTA 5

Compositional bias

22 – 31

10

Pro-rich

Amino acid modifications

Modified residue

373

1

Phosphoserine Ref.10 Ref.11

Natural variations

Alternative sequence

68 – 134

67

Missing in isoform 2.

VSP_036468

Experimental info

Mutagenesis

164

1

K → N: Reduced activity. Ref.2

Mutagenesis

199

1

N → K: Reduced catalytic efficiency. Ref.3

Sequence conflict

241

1

Y → H Ref.2

Secondary structure

1

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379

Helix Strand Turn

Details...

Helix

66 – 68

3

Helix

70 – 72

3

Beta strand

87 – 90

4

Helix

94 – 109

16

Helix

114 – 126

13

Helix

131 – 143

13

Helix

148 – 161

14

Helix

166 – 179

14

Helix

185 – 195

11

Helix

200 – 213

14

Helix

216 – 218

3

Helix

219 – 229

11

Helix

234 – 246

13

Helix

253 – 269

17

Helix

274 – 284

11

Turn

285 – 287

3

Helix

289 – 291

3

Helix

293 – 302

10

Turn

303 – 305

3

Helix

309 – 324

16

Helix

330 – 346

17

Helix

350 – 352

3

Helix

353 – 367

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: E933CBA874AB92B9	FASTA	379	44,409
	10 20 30 40 50 60 MAATEGVGEA AQGGEPGQPA QPPPQPHPPP PQQQHKEEMA AEAGEAVASP MDDGFVSLDS 70 80 90 100 110 120 PSYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSDKFRDVY DYFRAVLQRD ERSERAFKLT 130 140 150 160 170 180 RDAIELNAAN YTVWHFRRVL LKSLQKDLHE EMNYITAIIE EQPKNYQVWH HRRVLVEWLR 190 200 210 220 230 240 DPSQELEFIA DILNQDAKNY HAWQHRQWVI QEFKLWDNEL QYVDQLLKED VRNNSVWNQR 250 260 270 280 290 300 YFVISNTTGY NDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS KYPNLLNQLL 310 320 330 340 350 360 DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG 370 RSLQSKHSTE NDSPTNVQQ
	Isoform 2 [UniParc]. Checksum: 789D43774B90D5DA	FASTA	312	36,493
	10 20 30 40 50 60 MAATEGVGEA AQGGEPGQPA QPPPQPHPPP PQQQHKEEMA AEAGEAVASP MDDGFVSLDS 70 80 90 100 110 120 PSYVLYRHFR RVLLKSLQKD LHEEMNYITA IIEEQPKNYQ VWHHRRVLVE WLRDPSQELE 130 140 150 160 170 180 FIADILNQDA KNYHAWQHRQ WVIQEFKLWD NELQYVDQLL KEDVRNNSVW NQRYFVISNT 190 200 210 220 230 240 TGYNDRAVLE REVQYTLEMI KLVPHNESAW NYLKGILQDR GLSKYPNLLN QLLDLQPSHS 250 260 270 280 290 300 SPYLIAFLVD IYEDMLENQC DNKEDILNKA LELCEILAKE KDTIRKEYWR YIGRSLQSKH 310 STENDSPTNV QQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of the two subunits of human CAAX farnesyltransferase and chromosomal mapping of FNTA and FNTB loci and related sequences." Andres D.A., Milatovich A., Ozcelik T., Wenzlau J.M., Brown M.S., Goldstein J.L., Francke U. Genomics 18:105-112(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Retina.
[2]	"Mutational analysis of alpha-subunit of protein farnesyltransferase. Evidence for a catalytic role." Andres D.A., Goldstein J.L., Ho Y.K., Brown M.S. J. Biol. Chem. 268:1383-1390(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF LYS-164.
[3]	"Characterization of recombinant human farnesyl-protein transferase: cloning, expression, farnesyl diphosphate binding, and functional homology with yeast prenyl-protein transferases." Omer C.A., Kral A.M., Diehl R.E., Prendergast G.C., Powers S., Allen C.M., Gibbs J.B., Kohl N.E. Biochemistry 32:5167-5176(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF ASN-199. Tissue: Placenta.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"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] (ISOFORM 1). Tissue: Synovium.
[6]	"DNA sequence and analysis of human chromosome 8." Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S. Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Colon and Lung.
[8]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-261 (ISOFORM 2).
[9]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"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-373, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, MASS SPECTROMETRY. 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]	"The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics." Long S.B., Hancock P.J., Kral A.M., Hellinga H.W., Beese L.S. Proc. Natl. Acad. Sci. U.S.A. 98:12948-12953(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT; FARNESYL DIPHOSPHATE AND INHIBITOR L-739,750.
[15]	"3-aminopyrrolidinone farnesyltransferase inhibitors: design of macrocyclic compounds with improved pharmacokinetics and excellent cell potency." Bell I.M., Gallicchio S.N., Abrams M., Beese L.S., Beshore D.C., Bhimnathwala H., Bogusky M.J., Buser C.A., Culberson J.C., Davide J., Ellis-Hutchings M., Fernandes C., Gibbs J.B., Graham S.L., Hamilton K.A., Hartman G.D., Heimbrook D.C., Homnick C.F. , Huber H.E., Huff J.R., Kassahun K., Koblan K.S., Kohl N.E., Lobell R.B., Lynch J.J. Jr., Robinson R., Rodrigues A.D., Taylor J.S., Walsh E.S., Williams T.M., Zartman C.B. J. Med. Chem. 45:2388-2409(2002) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT; FARNESYL DIPHOSPHATE AND INHIBITORS.
[16]	"Dual protein farnesyltransferase-geranylgeranyltransferase-I inhibitors as potential cancer chemotherapeutic agents." deSolms S.J., Ciccarone T.M., MacTough S.C., Shaw A.W., Buser C.A., Ellis-Hutchings M., Fernandes C., Hamilton K.A., Huber H.E., Kohl N.E., Lobell R.B., Robinson R.G., Tsou N.N., Walsh E.S., Graham S.L., Beese L.S., Taylor J.S. J. Med. Chem. 46:2973-2984(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT; FARNESYL DIPHOSPHATE AND INHIBITOR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L10413 mRNA. Translation: AAA86285.1.
L00634 mRNA. Translation: AAA35853.1.
AC110275 Genomic DNA. No translation available.
BT009854 mRNA. Translation: AAP88856.1.
AK292121 mRNA. Translation: BAF84810.1.
AC113191 Genomic DNA. No translation available.
BC017029 mRNA. Translation: AAH17029.2.
BC084566 mRNA. Translation: AAH84566.1.
AL698961 mRNA. No translation available.

IPI

IPI00026813.
IPI00607601.

PIR

A47659.

RefSeq

NP_002018.1. NM_002027.2.

UniGene

Hs.370312.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JCQ	X-ray	2.30	A	1-379	[»]
1LD7	X-ray	2.00	A	1-379	[»]
1LD8	X-ray	1.80	A	1-379	[»]
1MZC	X-ray	2.00	A	1-379	[»]
1S63	X-ray	1.90	A	1-379	[»]
1SA4	X-ray	2.10	A	1-379	[»]
1TN6	X-ray	1.80	A	1-379	[»]
2F0Y	X-ray	2.70	A	1-379	[»]
2H6F	X-ray	1.50	A	1-379	[»]
2H6G	X-ray	1.85	A	1-379	[»]
2H6H	X-ray	1.80	A	1-379	[»]
2H6I	X-ray	3.00	A	1-379	[»]
2IEJ	X-ray	1.80	A	1-379	[»]
3E37	X-ray	1.80	A	1-379	[»]

ProteinModelPortal

P49354.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49354. 10 interactions.

MINT

MINT-238861.

STRING

9606.ENSP00000303423.

PTM databases

PhosphoSite

P49354.

Polymorphism databases

DMDM

1346694.

Proteomic databases

PaxDb

P49354.

PRIDE

P49354.

Protocols and materials databases

DNASU

2339.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302279; ENSP00000303423; ENSG00000168522.
ENST00000342116; ENSP00000343931; ENSG00000168522.

GeneID

2339.

KEGG

hsa:2339.

UCSC

uc003xps.3. human.

Organism-specific databases

CTD

2339.

GeneCards

GC08P042928.

HGNC

HGNC:3782. FNTA.

HPA

CAB010149.
HPA018830.

MIM

134635. gene.

neXtProt

NX_P49354.

PharmGKB

PA28199.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5536.

HOGENOM

HOG000188957.

HOVERGEN

HBG004498.

InParanoid

P49354.

KO

K05955.

OMA

HRRFIVE.

OrthoDB

EOG46DM39.

PhylomeDB

P49354.

Enzyme and pathway databases

Reactome

REACT_578. Apoptosis.

Gene expression databases

ArrayExpress

P49354.

Bgee

P49354.

CleanEx

HS_FNTA.

Genevestigator

P49354.

GermOnline

ENSG00000168522. Homo sapiens.

Family and domain databases

InterPro

IPR002088. Prenyl_trans_a.
[Graphical view]

Pfam

PF01239. PPTA. 5 hits.
[Graphical view]

PROSITE

PS51147. PFTA. 5 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P49354.

ChEMBL

CHEMBL271.

EvolutionaryTrace

P49354.

GenomeRNAi

2339.

NextBio

9495.

PMAP-CutDB

P49354.

SOURCE

Search...

Entry information

Entry name

FNTA_HUMAN

Accession

Primary (citable) accession number: P49354
Secondary accession number(s): A6NJW0, Q53XJ9, Q9UDC1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 1, 2013
This is version 135 of the entry and version 1 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.