Q9UNF0 (PACN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein kinase C and casein kinase substrate in neurons protein 2

Alternative name(s):
Syndapin 2
Syndapin-II

Gene names

Name:

PACSIN2

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

General annotation (Comments)

Function	Plays a role in the formation of normal, flask-shaped caveolae at the cell membrane. Recruits DNM2 to caveolae, and thereby plays a role in caveola-mediated endocytosis. Plays a role in intracellular vesicle-mediated transport. Binds to membranes via its F-BAR domain and promotes membrane tubulation. Plays a role in the internalization of cell-surface receptors. Is not required for internalization of EGFR after EGF stimulus, but contributes to the internalization of EGFR in the absence of EGF stimulus. Ref.12 Ref.13 Ref.15 Ref.16
Subunit structure	Homodimer. May form heterooligomers with other PACSINs. Interacts (via SH3 domain) with DNM1, SYN1, SYNJ1 and WASL. Interacts with EHD1 and EHD3. Interacts with CAV1 By similarity. Interacts with RAC1. Ref.13
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection By similarity. Membrane › caveola. Note: Detected at the neck of flask-shaped caveolae. Ref.12 Ref.13 Ref.15
Tissue specificity	Widely expressed. Ref.7 Ref.8
Domain	The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain. Ref.12 Ref.16 Ref.17 Ref.18
Post-translational modification	Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC) By similarity.
Sequence similarities	Belongs to the PACSIN family. Contains 1 FCH domain. Contains 1 SH3 domain.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell membrane Cell projection Cytoplasm Cytoplasmic vesicle Cytoskeleton Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil SH3 domain
Ligand	Lipid-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton organization Traceable author statement Ref.1. Source: ProtInc caveola assembly Inferred from mutant phenotype Ref.12. Source: UniProtKB caveolin-mediated endocytosis Inferred from mutant phenotype Ref.12. Source: UniProtKB cell projection morphogenesis Inferred from sequence or structural similarity. Source: UniProtKB membrane tubulation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of endocytosis Inferred from electronic annotation. Source: Compara
Cellular_component	caveola Inferred from direct assay Ref.12. Source: UniProtKB cytoplasm Traceable author statement Ref.1. Source: ProtInc cytosol Inferred from electronic annotation. Source: Compara extrinsic to membrane Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	transporter activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9UNF0-1)

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: Q9UNF0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     344-384: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 486

486

Protein kinase C and casein kinase substrate in neurons protein 2

PRO_0000161795

Regions

Domain

11 – 75

65

FCH

Domain

426 – 486

61

SH3

Region

1 – 306

306

F-BAR domain

Coiled coil

25 – 274

250

Natural variations

Alternative sequence

344 – 384

41

Missing in isoform 2.

VSP_004517

Natural variant

175

1

N → S.
Corresponds to variant rs35383004 [ dbSNP | Ensembl ].

VAR_053555

Natural variant

294

1

M → I.
Corresponds to variant rs2746984 [ dbSNP | Ensembl ].

VAR_013711

Natural variant

324

1

V → F.
Corresponds to variant rs1062913 [ dbSNP | Ensembl ].

VAR_013712

Experimental info

Sequence conflict

182

1

L → F in AAD41781. Ref.1

Sequence conflict

256

1

D → N in AAD41781. Ref.1

Sequence conflict

309

1

N → I in AAD41781. Ref.1

Sequence conflict

336

1

S → F in AAD41781. Ref.1

Sequence conflict

378 – 380

3

DDT → EDI in AAD41781. Ref.1

Secondary structure

1

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486

Helix Strand Turn

Details...

Turn

21 – 24

4

Helix

25 – 72

48

Helix

77 – 106

30

Helix

108 – 119

12

Beta strand

126 – 128

3

Helix

129 – 169

41

Helix

172 – 177

6

Helix

185 – 188

4

Helix

189 – 191

3

Turn

192 – 195

4

Helix

197 – 255

59

Helix

257 – 259

3

Helix

263 – 275

13

Helix

279 – 290

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 13, 2002. Version 2. Checksum: 821DBEF65DAD1AA8	FASTA	486	55,739
	10 20 30 40 50 60 MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCSD LMNCLHERAR IEKAYAQQLT 70 80 90 100 110 120 EWARRWRQLV EKGPQYGTVE KAWMAFMSEA ERVSELHLEV KASLMNDDFE KIKNWQKEAF 130 140 150 160 170 180 HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK EVEAAKKAHH AACKEEKLAI SREANSKADP 190 200 210 220 230 240 SLNPEQLKKL QDKIEKCKQD VLKTKEKYEK SLKELDQGTP QYMENMEQVF EQCQQFEEKR 250 260 270 280 290 300 LRFFREVLLE VQKHLDLSNV AGYKAIYHDL EQSIRAADAV EDLRWFRANH GPGMAMNWPQ 310 320 330 340 350 360 FEEWSADLNR TLSRREKKKA TDGVTLTGIN QTGDQSLPSK PSSTLNVPSN PAQSAQSQSS 370 380 390 400 410 420 YNPFEDEDDT GSTVSEKDDT KAKNVSSYEK TQSYPTDWSD DESNNPFSST DANGDSNPFD 430 440 450 460 470 480 DDATSGTEVR VRALYDYEGQ EHDELSFKAG DELTKMEDED EQGWCKGRLD NGQVGLYPAN YVEAIQ
	Isoform 2 [UniParc]. Checksum: 1DA87A2D42B5D5F9	FASTA	445	51,353
	10 20 30 40 50 60 MSVTYDDSVG VEVSSDSFWE VGNYKRTVKR IDDGHRLCSD LMNCLHERAR IEKAYAQQLT 70 80 90 100 110 120 EWARRWRQLV EKGPQYGTVE KAWMAFMSEA ERVSELHLEV KASLMNDDFE KIKNWQKEAF 130 140 150 160 170 180 HKQMMGGFKE TKEAEDGFRK AQKPWAKKLK EVEAAKKAHH AACKEEKLAI SREANSKADP 190 200 210 220 230 240 SLNPEQLKKL QDKIEKCKQD VLKTKEKYEK SLKELDQGTP QYMENMEQVF EQCQQFEEKR 250 260 270 280 290 300 LRFFREVLLE VQKHLDLSNV AGYKAIYHDL EQSIRAADAV EDLRWFRANH GPGMAMNWPQ 310 320 330 340 350 360 FEEWSADLNR TLSRREKKKA TDGVTLTGIN QTGDQSLPSK PSSVSSYEKT QSYPTDWSDD 370 380 390 400 410 420 ESNNPFSSTD ANGDSNPFDD DATSGTEVRV RALYDYEGQE HDELSFKAGD ELTKMEDEDE 430 440 QGWCKGRLDN GQVGLYPANY VEAIQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"PACSIN 2, a novel member of the PACSIN family of cytoplasmic adapter proteins." Ritter B., Modregger J., Paulsson M., Plomann M. FEBS Lett. 454:356-362(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain and Retina.
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Testis.
[3]	"A genome annotation-driven approach to cloning the human ORFeome." Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I. Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The DNA sequence of human chromosome 22." Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H. Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: Skin.
[6]	The European IMAGE consortium Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 335-486 (ISOFORM 2).
[7]	"All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis." Modregger J., Ritter B., Witter B., Paulsson M., Plomann M. J. Cell Sci. 113:4511-4521(2000) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family." Sumoy L., Pluvinet R., Andreu N., Estivill X., Escarceller M. Gene 262:199-205(2001) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"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.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"Essential role of PACSIN2/syndapin-II in caveolae membrane sculpting." Senju Y., Itoh Y., Takano K., Hamada S., Suetsugu S. J. Cell Sci. 124:2032-2040(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN, SUBCELLULAR LOCATION.
[13]	"The F-BAR domain protein PACSIN2 associates with Rac1 and regulates cell spreading and migration." de Kreuk B.J., Nethe M., Fernandez-Borja M., Anthony E.C., Hensbergen P.J., Deelder A.M., Plomann M., Hordijk P.L. J. Cell Sci. 124:2375-2388(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAC1.
[14]	"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].
[15]	"The F-BAR protein PACSIN2 regulates epidermal growth factor receptor internalization." de Kreuk B.J., Anthony E.C., Geerts D., Hordijk P.L. J. Biol. Chem. 287:43438-43453(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]	"Versatile membrane deformation potential of activated pacsin." Goh S.L., Wang Q., Byrnes L.J., Sondermann H. PLoS ONE 7:E51628-E51628(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DOMAIN.
[17]	"Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin." Wang Q., Navarro M.V., Peng G., Molinelli E., Goh S.L., Judson B.L., Rajashankar K.R., Sondermann H. Proc. Natl. Acad. Sci. U.S.A. 106:12700-12705(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.78 ANGSTROMS), DOMAIN.
[18]	"Mapping of the basic amino-acid residues responsible for tubulation and cellular protrusion by the EFC/F-BAR domain of pacsin2/Syndapin II." Shimada A., Takano K., Shirouzu M., Hanawa-Suetsugu K., Terada T., Toyooka K., Umehara T., Yamamoto M., Yokoyama S., Suetsugu S. FEBS Lett. 584:1111-1118(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-305, DOMAIN.
[19]	"Rigidity of wedge loop in PACSIN 3 protein is a key factor in dictating diameters of tubules." Bai X., Meng G., Luo M., Zheng X. J. Biol. Chem. 287:22387-22396(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 16-304.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF128536 mRNA. Translation: AAD41781.1.
AL136845 mRNA. Translation: CAB66779.1.
CR456536 mRNA. Translation: CAG30422.1.
AL022476, AL049758 Genomic DNA. Translation: CAI20163.1.
AL049758, AL022476 Genomic DNA. Translation: CAI20948.1.
BC008037 mRNA. Translation: AAH08037.1.
AL389984 mRNA. Translation: CAB97538.1.

IPI

IPI00027009.
IPI00221111.

RefSeq

NP_001171899.1. NM_001184970.1.
NP_001171900.1. NM_001184971.1.
NP_009160.2. NM_007229.3.

UniGene

Hs.162877.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ABH	X-ray	2.00	A/B	1-305	[»]
3ACO	X-ray	2.70	A/B	1-343	[»]
3HAJ	X-ray	2.78	A/B	1-486	[»]
3Q0K	X-ray	2.60	A/B/C/D	16-304	[»]

ProteinModelPortal

Q9UNF0.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UNF0. 5 interactions.

MINT

MINT-5005738.

STRING

9606.ENSP00000263246.

PTM databases

PhosphoSite

Q9UNF0.

Polymorphism databases

DMDM

22256968.

Proteomic databases

PaxDb

Q9UNF0.

PRIDE

Q9UNF0.

Protocols and materials databases

DNASU

11252.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263246; ENSP00000263246; ENSG00000100266.
ENST00000337959; ENSP00000338379; ENSG00000100266.
ENST00000402229; ENSP00000385040; ENSG00000100266.
ENST00000403744; ENSP00000385372; ENSG00000100266.
ENST00000407585; ENSP00000385952; ENSG00000100266.

GeneID

11252.

KEGG

hsa:11252.

UCSC

uc003bdg.4. human.

Organism-specific databases

CTD

11252.

GeneCards

GC22M043243.

HGNC

HGNC:8571. PACSIN2.

HPA

CAB009929.
HPA028852.
HPA049854.

MIM

604960. gene.

neXtProt

NX_Q9UNF0.

PharmGKB

PA32897.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG283356.

HOGENOM

HOG000007245.

HOVERGEN

HBG053486.

InParanoid

Q9UNF0.

OMA

SYPTDWS.

PhylomeDB

Q9UNF0.

Gene expression databases

ArrayExpress

Q9UNF0.

Bgee

Q9UNF0.

Genevestigator

Q9UNF0.

GermOnline

ENSG00000100266. Homo sapiens.

Family and domain databases

InterPro

IPR001060. FCH_dom.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF00611. FCH. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00452. SH3DOMAIN.

SMART

SM00055. FCH. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50133. FCH. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PACSIN2. human.

EvolutionaryTrace

Q9UNF0.

GenomeRNAi

11252.

NextBio

42818.

SOURCE

Search...

Entry information

Entry name

PACN2_HUMAN

Accession

Primary (citable) accession number: Q9UNF0
Secondary accession number(s): O95921 , Q96HV9, Q9H0D3, Q9NPN1, Q9Y4V2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 2002
Last sequence update:	August 13, 2002
Last modified:	May 29, 2013
This is version 112 of the entry and version 2 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.