P49760 (CLK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dual specificity protein kinase CLK2
EC=2.7.12.1

Alternative name(s):
CDC-like kinase 2

Gene names

Name:

CLK2

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

General annotation (Comments)

Function	Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Ref.5 Ref.6 Ref.7 Ref.12
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	5,6-dichloro-1-b-D-ribofuranosylbenzimidazole (DRB) inhibits autophosphorylation. TG003 inhibits its kinase activity and affects the regulation of alternative splicing mediated by phosphorylation of SR proteins By similarity.
Subunit structure	Interacts with RBMX. Interacts with AKT1 and UBL5. Ref.8 Ref.13 Ref.15
Subcellular location	Isoform 1: Nucleus. Nucleus speckle. Note: Inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle By similarity. Ref.6 Isoform 2: Nucleus speckle. Note: Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles. Ref.6
Tissue specificity	Endothelial cells. Ref.12
Post-translational modification	Autophosphorylates on all three types of residues. Phosphorylation on Ser-34 and Thr-127 by AKT1 is induced by ionizing radiation or insulin. Phosphorylation plays a critical role in cell proliferation following low dose radiation and prevents cell death following high dose radiation. Phosphorylation at Thr-344 by PKB/AKT2 induces its kinase activity which is required for its stability. The phosphorylation status at Ser-142 influences its subnuclear localization; inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle.
Sequence similarities	Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. Lammer subfamily. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of gluconeogenesis Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-tyrosine phosphorylation Inferred from electronic annotation. Source: Compara protein autophosphorylation Inferred from sequence or structural similarity. Source: UniProtKB regulation of RNA splicing Inferred from direct assay Ref.6. Source: UniProtKB response to ionizing radiation Inferred from mutant phenotype Ref.15. Source: UniProtKB response to retinoic acid Inferred from electronic annotation. Source: Compara
Cellular_component	nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.6. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from direct assay Ref.7. Source: UniProtKB protein serine/threonine/tyrosine kinase activity Inferred from electronic annotation. Source: EC protein tyrosine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SNRNP70	P08621	2	EBI-750020,EBI-1049228

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P49760-1)

Also known as: Long;

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: P49760-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     134-139: QHSSRR → MKSLAP
     140-499: Missing.

Note: Lacks the kinase domain. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 3 (identifier: P49760-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 499

499

Dual specificity protein kinase CLK2

PRO_0000085868

Regions

Domain

163 – 479

317

Protein kinase

Nucleotide binding

169 – 177

9

ATP By similarity

Sites

Active site

290

1

Proton acceptor By similarity

Binding site

193

1

ATP By similarity

Amino acid modifications

Modified residue

34

1

Phosphoserine; by PKB/AKT1 Ref.15

Modified residue

98

1

Phosphoserine; by autocatalysis

Modified residue

99

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

127

1

Phosphothreonine; by PKB/AKT1 Ref.15

Modified residue

142

1

Phosphoserine; by autocatalysis Ref.10 Ref.11 Ref.14

Modified residue

153

1

Phosphotyrosine Ref.14

Modified residue

344

1

Phosphothreonine; by PKB/AKT2 By similarity

Natural variations

Alternative sequence

134 – 139

6

QHSSRR → MKSLAP in isoform 2.

VSP_004856

Alternative sequence

134

1

Missing in isoform 3.

VSP_038744

Alternative sequence

140 – 499

360

Missing in isoform 2.

VSP_004857

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

499

Helix Strand Turn

Details...

Turn

146 – 149

4

Turn

160 – 162

3

Beta strand

163 – 172

10

Beta strand

175 – 182

8

Turn

183 – 187

5

Beta strand

189 – 195

7

Helix

199 – 218

20

Beta strand

229 – 235

7

Beta strand

238 – 244

7

Helix

250 – 256

7

Turn

257 – 259

3

Helix

264 – 283

20

Helix

293 – 295

3

Beta strand

296 – 299

4

Beta strand

317 – 319

3

Beta strand

323 – 325

3

Beta strand

332 – 336

5

Helix

345 – 347

3

Helix

350 – 353

4

Helix

361 – 376

16

Helix

386 – 397

12

Helix

402 – 407

6

Helix

411 – 413

3

Helix

426 – 434

9

Helix

438 – 441

4

Helix

447 – 459

13

Turn

464 – 466

3

Helix

470 – 475

6

Helix

477 – 479

3

Helix

480 – 483

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified October 1, 1996. Version 1. Checksum: E43BBF3BAD6EF991	FASTA	499	60,090
	10 20 30 40 50 60 MPHPRRYHSS ERGSRGSYRE HYRSRKHKRR RSRSWSSSSD RTRRRRREDS YHVRSRSSYD 70 80 90 100 110 120 DRSSDRRVYD RRYCGSYRRN DYSRDRGDAY YDTDYRHSYE YQRENSSYRS QRSSRRKHRR 130 140 150 160 170 180 RRRRSRTFSR SSSQHSSRRA KSVEDDAEGH LIYHVGDWLQ ERYEIVSTLG EGTFGRVVQC 190 200 210 220 230 240 VDHRRGGARV ALKIIKNVEK YKEAARLEIN VLEKINEKDP DNKNLCVQMF DWFDYHGHMC 250 260 270 280 290 300 ISFELLGLST FDFLKDNNYL PYPIHQVRHM AFQLCQAVKF LHDNKLTHTD LKPENILFVN 310 320 330 340 350 360 SDYELTYNLE KKRDERSVKS TAVRVVDFGS ATFDHEHHST IVSTRHYRAP EVILELGWSQ 370 380 390 400 410 420 PCDVWSIGCI IFEYYVGFTL FQTHDNREHL AMMERILGPI PSRMIRKTRK QKYFYRGRLD 430 440 450 460 470 480 WDENTSAGRY VRENCKPLRR YLTSEAEEHH QLFDLIESML EYEPAKRLTL GEALQHPFFA 490 RLRAEPPNKL WDSSRDISR
	Isoform 2 (Short) [UniParc]. Checksum: CC9C9C63B3B07667	FASTA	139	17,569
	10 20 30 40 50 60 MPHPRRYHSS ERGSRGSYRE HYRSRKHKRR RSRSWSSSSD RTRRRRREDS YHVRSRSSYD 70 80 90 100 110 120 DRSSDRRVYD RRYCGSYRRN DYSRDRGDAY YDTDYRHSYE YQRENSSYRS QRSSRRKHRR 130 RRRRSRTFSR SSSMKSLAP
	Isoform 3 [UniParc]. Checksum: 0A21FC66FD22DBC6	FASTA	498	59,962
	10 20 30 40 50 60 MPHPRRYHSS ERGSRGSYRE HYRSRKHKRR RSRSWSSSSD RTRRRRREDS YHVRSRSSYD 70 80 90 100 110 120 DRSSDRRVYD RRYCGSYRRN DYSRDRGDAY YDTDYRHSYE YQRENSSYRS QRSSRRKHRR 130 140 150 160 170 180 RRRRSRTFSR SSSHSSRRAK SVEDDAEGHL IYHVGDWLQE RYEIVSTLGE GTFGRVVQCV 190 200 210 220 230 240 DHRRGGARVA LKIIKNVEKY KEAARLEINV LEKINEKDPD NKNLCVQMFD WFDYHGHMCI 250 260 270 280 290 300 SFELLGLSTF DFLKDNNYLP YPIHQVRHMA FQLCQAVKFL HDNKLTHTDL KPENILFVNS 310 320 330 340 350 360 DYELTYNLEK KRDERSVKST AVRVVDFGSA TFDHEHHSTI VSTRHYRAPE VILELGWSQP 370 380 390 400 410 420 CDVWSIGCII FEYYVGFTLF QTHDNREHLA MMERILGPIP SRMIRKTRKQ KYFYRGRLDW 430 440 450 460 470 480 DENTSAGRYV RENCKPLRRY LTSEAEEHHQ LFDLIESMLE YEPAKRLTLG EALQHPFFAR 490 LRAEPPNKLW DSSRDISR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization by cDNA cloning of two new human protein kinases. Evidence by sequence comparison of a new family of mammalian protein kinases." Hanes J.J., der Kammer H., Klaudiny J.J., Scheit K.H. J. Mol. Biol. 244:665-672(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]	"Identification of three additional genes contiguous to the glucocerebrosidase locus on chromosome 1q21: implications for Gaucher disease." Winfield S.L., Tayebi N., Martin B.M., Ginns E.I., Sidransky E. Genome Res. 7:1020-1026(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[3]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] (ISOFORMS 1 AND 3). Tissue: Lung and Ovary.
[5]	"Activity and autophosphorylation of LAMMER protein kinases." Lee K., Du C., Horn M., Rabinow L. J. Biol. Chem. 271:27299-27303(1996) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"The Clk2 and Clk3 dual-specificity protein kinases regulate the intranuclear distribution of SR proteins and influence pre-mRNA splicing." Duncan P.I., Stojdl D.F., Marius R.M., Scheit K.H., Bell J.C. Exp. Cell Res. 241:300-308(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[7]	"The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B." Moeslein F.M., Myers M.P., Landreth G.E. J. Biol. Chem. 274:26697-26704(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Beacon interacts with cdc2/cdc28-like kinases." Kantham L., Kerr-Bayles L., Godde N., Quick M., Webb R., Sunderland T., Bond J., Walder K., Augert G., Collier G. Biochem. Biophys. Res. Commun. 304:125-129(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBL5.
[9]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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-142, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Cdc2-like kinases and DNA topoisomerase I regulate alternative splicing of tissue factor in human endothelial cells." Eisenreich A., Bogdanov V.Y., Zakrzewicz A., Pries A., Antoniak S., Poller W., Schultheiss H.P., Rauch U. Circ. Res. 104:589-599(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[13]	"Heterogeneous nuclear ribonucleoprotein G regulates splice site selection by binding to CC(A/C)-rich regions in pre-mRNA." Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M., Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R., Stamm S. J. Biol. Chem. 284:14303-14315(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RBMX.
[14]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142 AND TYR-153, MASS SPECTROMETRY.
[15]	"Phosphorylation of CLK2 at serine 34 and threonine 127 by AKT controls cell survival after ionizing radiation." Nam S.Y., Seo H.H., Park H.S., An S., Kim J.Y., Yang K.H., Kim C.S., Jeong M., Jin Y.W. J. Biol. Chem. 285:31157-31163(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-34 AND THR-127, INTERACTION WITH AKT1.
[16]	"Structure of human cdc2-like kinase 2 (clk2)." Structural genomics consortium (SGC) Submitted (AUG-2010) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 135-496.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L29218 mRNA. Translation: AAA61482.1.
L29216 mRNA. Translation: AAA61481.1.
AF023268 Genomic DNA. Translation: AAC51817.1.
AL713999 Genomic DNA. Translation: CAI95098.1.
BC014067 mRNA. Translation: AAH14067.1.
BC053603 mRNA. Translation: AAH53603.1.

IPI

IPI00028071.
IPI00643082.
IPI00937288.

PIR

S53637.
S53638.

RefSeq

NP_003984.2. NM_003993.2.

UniGene

Hs.73986.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3NR9	X-ray	2.89	A/B/C	135-496	[»]

ProteinModelPortal

P49760.

ModBase

Search...

Protein-protein interaction databases

IntAct

P49760. 4 interactions.

MINT

MINT-1683264.

STRING

9606.ENSP00000354856.

PTM databases

PhosphoSite

P49760.

Polymorphism databases

DMDM

1705919.

Proteomic databases

PaxDb

P49760.

PRIDE

P49760.

Protocols and materials databases

DNASU

1196.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361168; ENSP00000354856; ENSG00000176444.
ENST00000368361; ENSP00000357345; ENSG00000176444.
ENST00000536801; ENSP00000441023; ENSG00000176444.
ENST00000572269; ENSP00000459461; ENSG00000261893.
ENST00000574445; ENSP00000460443; ENSG00000261893.

GeneID

1196.

KEGG

hsa:1196.

UCSC

uc001fjw.3. human.
uc001fjx.3. human.

Organism-specific databases

CTD

1196.

GeneCards

GC01M155232.

H-InvDB

HIX0001112.

HGNC

HGNC:2069. CLK2.

HPA

HPA055366.

MIM

602989. gene.

neXtProt

NX_P49760.

PharmGKB

PA26595.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000203417.

HOVERGEN

HBG107720.

InParanoid

P49760.

KO

K08823.

OMA

RYRSRKH.

OrthoDB

EOG46DM2S.

Enzyme and pathway databases

BRENDA

2.7.12.1. 2681.

Gene expression databases

ArrayExpress

P49760.

Bgee

P49760.

CleanEx

HS_CLK2.

Genevestigator

P49760.

GermOnline

ENSG00000176444. Homo sapiens.

Family and domain databases

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
[Graphical view]

SMART

SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P49760.

ChEMBL

CHEMBL4225.

ChiTaRS

CLK2. human.

EvolutionaryTrace

P49760.

GenomeRNAi

1196.

NextBio

4940.

SOURCE

Search...

Entry information

Entry name

CLK2_HUMAN

Accession

Primary (citable) accession number: P49760
Secondary accession number(s): B1AVS9, B5MBX6, Q96CQ0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 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.