Q9BSQ5 (CCM2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malcavernin

Alternative name(s):
Cerebral cavernous malformations 2 protein

Gene names

Name:	CCM2
Synonyms:	C7orf22
ORF Names:	PP10187

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

General annotation (Comments)

Function	Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May act through the stabilization of endothelial cell junctions By similarity. May function as a scaffold protein for MAP2K3-MAP3K3 signaling. Seems to play a major role in the modulation of MAP3K3-dependent p38 activation induced by hyperosmotic shock By similarity.
Subunit structure	Part of a complex with MAP2K3, MAP3K3 and RAC1. Binds RAC1 directly and independently of its nucleotide-bound state By similarity. Interacts with HEG1 and KRIT1; KRIT1 greatly facilitates the interaction with HEG1 By similarity. Interacts with PDCD10. Ref.10 Ref.11
Subcellular location	Cytoplasm By similarity.
Domain	The C-terminal region constitutes an independently folded domain that has structural similarity with the USH1C (harmonin) N-terminus, despite very low sequence similarity. Ref.11
Involvement in disease	Cerebral cavernous malformations 2 (CCM2) [MIM:603284]: A congenital vascular anomaly of the central nervous system that can result in hemorrhagic stroke, seizures, recurrent headaches, and focal neurologic deficits. The lesions are characterized by grossly enlarged blood vessels consisting of a single layer of endothelium and without any intervening neural tissue, ranging in diameter from a few millimeters to several centimeters. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.12 Ref.13
Sequence similarities	Belongs to the CCM2 family. Contains 1 PID domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	endothelial tube morphogenesis Inferred from mutant phenotype PubMed 19151727. Source: MGI integrin-mediated signaling pathway Traceable author statement PubMed 16037064. Source: UniProtKB stress-activated MAPK cascade Traceable author statement PubMed 16037064. Source: UniProtKB vasculogenesis Inferred from mutant phenotype Ref.12. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay PubMed 16037064. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KRIT1	O00522	3	EBI-1573056,EBI-1573121
PDCD10	Q9BUL8	4	EBI-1573056,EBI-740195

Alternative products

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

Isoform 1 (identifier: Q9BSQ5-1)

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: Q9BSQ5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-10: MEEEGKKGKK → MHSSCRQRRNQNLSKEIPQTEFHTGYSMENE

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 444

444

Malcavernin

PRO_0000089424

Regions

Domain

59 – 248

190

PID

Region

283 – 376

94

Harmonin homology domain

Amino acid modifications

Modified residue

384

1

Phosphoserine Ref.9

Natural variations

Alternative sequence

1 – 10

10

MEEEGKKGKK → MHSSCRQRRNQNLSKEIPQT EFHTGYSMENE in isoform 2.

VSP_024402

Natural variant

53

1

V → I. Ref.12
Corresponds to variant rs2107732 [ dbSNP | Ensembl ].

VAR_023575

Natural variant

120

1

V → I. Ref.12
Corresponds to variant rs11552377 [ dbSNP | Ensembl ].

VAR_023576

Natural variant

198

1

L → R in CCM2. Ref.12

VAR_023577

Natural variant

215

1

Q → H in CCM2; associated with Q-229. Ref.13

VAR_067352

Natural variant

229

1

L → Q in CCM2; associated with H-215. Ref.13

VAR_067353

Natural variant

289

1

S → N.
Corresponds to variant rs2289366 [ dbSNP | Ensembl ].

VAR_050768

Experimental info

Sequence conflict

268

1

F → C in BAG53562. Ref.1

Sequence conflict

440

1

D → A in AAQ15228. Ref.2

Sequence conflict

444

1

A → ALWTVDGGAPTPSAQLS in AAQ15228. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

444

Helix Strand Turn

Details...

Helix

288 – 291

4

Helix

293 – 306

14

Turn

307 – 309

3

Helix

312 – 326

15

Helix

331 – 342

12

Helix

344 – 356

13

Helix

359 – 371

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 43F9C153B4DE460E	FASTA	444	48,837
	10 20 30 40 50 60 MEEEGKKGKK PGIVSPFKRV FLKGEKSRDK KAHEKVTERR PLHTVVLSLP ERVEPDRLLS 70 80 90 100 110 120 DYIEKEVKYL GQLTSIPGYL NPSSRTEILH FIDNAKRAHQ LPGHLTQEHD AVLSLSAYNV 130 140 150 160 170 180 KLAWRDGEDI ILRVPIHDIA AVSYVRDDAA HLVVLKTAQD PGISPSQSLC AESSRGLSAG 190 200 210 220 230 240 SLSESAVGPV EACCLVILAA ESKVAAEELC CLLGQVFQVV YTESTIDFLD RAIFDGASTP 250 260 270 280 290 300 THHLSLHSDD SSTKVDIKET YEVEASTFCF PESVDVGGAS PHSKTISESE LSASATELLQ 310 320 330 340 350 360 DYMLTLRTKL SSQEIQQFAA LLHEYRNGAS IHEFCINLRQ LYGDSRKFLL LGLRPFIPEK 370 380 390 400 410 420 DSQHFENFLE TIGVKDGRGI ITDSFGRHRR ALSTTSSSTT NGNRATGSSD DRSAPSEGDE 430 440 WDRMISDISS DIEALGCSMD QDSA
	Isoform 2 [UniParc]. Checksum: DA0E03C39B7DABE3	FASTA	465	51,413
	10 20 30 40 50 60 MHSSCRQRRN QNLSKEIPQT EFHTGYSMEN EPGIVSPFKR VFLKGEKSRD KKAHEKVTER 70 80 90 100 110 120 RPLHTVVLSL PERVEPDRLL SDYIEKEVKY LGQLTSIPGY LNPSSRTEIL HFIDNAKRAH 130 140 150 160 170 180 QLPGHLTQEH DAVLSLSAYN VKLAWRDGED IILRVPIHDI AAVSYVRDDA AHLVVLKTAQ 190 200 210 220 230 240 DPGISPSQSL CAESSRGLSA GSLSESAVGP VEACCLVILA AESKVAAEEL CCLLGQVFQV 250 260 270 280 290 300 VYTESTIDFL DRAIFDGAST PTHHLSLHSD DSSTKVDIKE TYEVEASTFC FPESVDVGGA 310 320 330 340 350 360 SPHSKTISES ELSASATELL QDYMLTLRTK LSSQEIQQFA ALLHEYRNGA SIHEFCINLR 370 380 390 400 410 420 QLYGDSRKFL LLGLRPFIPE KDSQHFENFL ETIGVKDGRG IITDSFGRHR RALSTTSSST 430 440 450 460 TNGNRATGSS DDRSAPSEGD EWDRMISDIS SDIEALGCSM DQDSA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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 2). Tissue: Thymus.
[2]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [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].
[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] (ISOFORM 1). Tissue: Brain and Kidney.
[7]	"Mutations in a gene encoding a novel protein containing a phosphotyrosine-binding domain cause type 2 cerebral cavernous malformations." Liquori C.L., Berg M.J., Siegel A.M., Huang E., Zawistowski J.S., Stoffer T., Verlaan D., Balogun F., Hughes L., Leedom T.P., Plummer N.W., Cannella M., Maglione V., Squitieri F., Johnson E.W., Rouleau G.A., Ptacek L., Marchuk D.A. Am. J. Hum. Genet. 73:1459-1464(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CCM2.
[8]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[9]	"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-384, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Crystal structure of CCM3, a cerebral cavernous malformation protein critical for vascular integrity." Li X., Zhang R., Zhang H., He Y., Ji W., Min W., Boggon T.J. J. Biol. Chem. 285:24099-24107(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PDCD10.
[11]	"Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus." Fisher O.S., Zhang R., Li X., Murphy J.W., Demeler B., Boggon T.J. FEBS Lett. 587:272-277(2013) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 283-379, PARTIAL PROTEIN SEQUENCE, DOMAIN, INTERACTION WITH PDCD10.
[12]	"Mutations within the MGC4607 gene cause cerebral cavernous malformations." Denier C., Goutagny S., Labauge P., Krivosic V., Arnoult M., Cousin A., Benabid A.L., Comoy J., Frerebeau P., Gilbert B., Houtteville J.P., Jan M., Lapierre F., Loiseau H., Menei P., Mercier P., Moreau J.J., Nivelon-Chevallier A. , Parker F., Redondo A.M., Scarabin J.M., Tremoulet M., Zerah M., Maciazek J., Tournier-Lasserve E. Am. J. Hum. Genet. 74:326-337(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CCM2 ARG-198, VARIANTS ILE-53 AND ILE-120.
[13]	"De Novo MGC4607 gene heterozygous missense variants in a child with multiple cerebral cavernous malformations." Mosca L., Pileggi S., Avemaria F., Tarlarini C., Cigoli M.S., Capra V., De Marco P., Pavanello M., Marocchi A., Penco S. J. Mol. Neurosci. 47:475-480(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CCM2 HIS-215 AND GLN-229.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK098005 mRNA. Translation: BAG53562.1.
AF370392 mRNA. Translation: AAQ15228.1.
AC004847 Genomic DNA. No translation available.
AC013416 Genomic DNA. No translation available.
CH236960 Genomic DNA. Translation: EAL23746.1.
CH471128 Genomic DNA. Translation: EAW61061.1.
CH471128 Genomic DNA. Translation: EAW61064.1.
BC004903 mRNA. Translation: AAH04903.1.
BC008859 mRNA. Translation: AAH08859.1.
BC016832 mRNA. Translation: AAH16832.1.
BC025958 mRNA. Translation: AAH25958.1.

IPI

IPI00465425.
IPI00619952.

RefSeq

NP_001025006.1. NM_001029835.2.
NP_001161407.1. NM_001167935.1.
NP_113631.1. NM_031443.3.

UniGene

Hs.148272.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4FQN	X-ray	1.90	A/B/C/D	283-379	[»]

ProteinModelPortal

Q9BSQ5.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BSQ5. 3 interactions.

STRING

9606.ENSP00000370503.

PTM databases

PhosphoSite

Q9BSQ5.

Polymorphism databases

DMDM

74733042.

Proteomic databases

PaxDb

Q9BSQ5.

PRIDE

Q9BSQ5.

Protocols and materials databases

DNASU

83605.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000258781; ENSP00000258781; ENSG00000136280.
ENST00000381112; ENSP00000370503; ENSG00000136280.

GeneID

83605.

KEGG

hsa:83605.

UCSC

uc003tmo.3. human.

Organism-specific databases

CTD

83605.

GeneCards

GC07P045039.

HGNC

HGNC:21708. CCM2.

HPA

HPA020273.
HPA021669.

MIM

603284. phenotype.
607929. gene.

neXtProt

NX_Q9BSQ5.

Orphanet

221061. Hereditary cerebral cavernous malformation.

PharmGKB

PA26145.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG39125.

HOGENOM

HOG000231916.

HOVERGEN

HBG054451.

OMA

AVSYIRD.

OrthoDB

EOG4RFKSP.

PhylomeDB

Q9BSQ5.

Enzyme and pathway databases

Pathway_Interaction_DB

p38_mkk3_6pathway. p38 MAPK signaling pathway.
p38alphabetapathway. Regulation of p38-alpha and p38-beta.

Gene expression databases

ArrayExpress

Q9BSQ5.

Bgee

Q9BSQ5.

CleanEx

HS_CCM2.

Genevestigator

Q9BSQ5.

GermOnline

ENSG00000136280. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR026159. Malcavernin.
IPR011993. PH_like_dom.
IPR006020. PTyr_interaction_dom.
[Graphical view]

PANTHER

PTHR21642. PTHR21642. 1 hit.

PROSITE

PS01179. PID. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

83605.

NextBio

35470159.

SOURCE

Search...

Entry information

Entry name

CCM2_HUMAN

Accession

Primary (citable) accession number: Q9BSQ5
Secondary accession number(s): A4D2L4 , B3KUV0, D3DVL4, E9PDJ3, Q71RE5, Q8TAT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2005
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 97 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.