O75351 (VPS4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vacuolar protein sorting-associated protein 4B
EC=3.6.4.6

Alternative name(s):
Cell migration-inducing gene 1 protein
Suppressor of K(+) transport growth defect 1
Short name=Protein SKD1

Gene names

Name:	VPS4B
Synonyms:	SKD1, VPS42
ORF Names:	MIG1

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	Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Ref.1 Ref.8 Ref.16
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Proposed to be monomeric or homodimeric in nucleotide-free form and to oligomerize upon binding to ATP to form two stacked hexameric or heptameric rings with a central pore through which ESCRT-III substrates are translocated in an ATP-dependent manner. In vitro, associates on the inside of a helical tubular structure formed by a CHMP2A-CHMP3 polymer. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP4B and CHMP6. Interacts with VPS4A; the interaction suggests a heteromeric assembly with VPS4A. Interacts with VTA1. Ref.1 Ref.7 Ref.8 Ref.13 Ref.17 Ref.23 Ref.25
Subcellular location	Prevacuolar compartment membrane; Peripheral membrane protein. Late endosome membrane; Peripheral membrane protein Probable. Note: Membrane-associated in the prevacuolar endosomal compartment. Localized in HIV-1 particles purified from acutely infected cells. Ref.1 Ref.8
Tissue specificity	Ubiquitously expressed. Ref.1
Domain	The MIT domain serves as an adapter for ESCRT-III proteins. It forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT interacting motif) helices along the groove between MIT helices 2 and 3 present in a subset of ESCRT-III proteins thus establishing the canonical MIM-MIT interaction. In an extended conformation along the groove between helices 1 and 3, also binds to a type-2 MIT interacting motif (MIM2). Ref.22
Sequence similarities	Belongs to the AAA ATPase family. Contains 1 MIT domain.

Ontologies

Keywords
Biological process	Cell cycle Cell division Protein transport Transport
Cellular component	Endosome Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	ATP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cellular membrane organization Traceable author statement. Source: Reactome endosome organization Inferred from electronic annotation. Source: Compara endosome to lysosome transport via multivesicular body sorting pathway Inferred from mutant phenotype PubMed 15024011. Source: UniProtKB intracellular cholesterol transport Inferred from mutant phenotype PubMed 10637304. Source: UniProtKB potassium ion transport Inferred from electronic annotation. Source: Compara protein transport Inferred from electronic annotation. Source: UniProtKB-KW response to lipid Inferred from direct assay PubMed 16757520. Source: UniProtKB
Cellular_component	cytosol Inferred from direct assay PubMed 10637304. Source: UniProtKB early endosome Inferred from direct assay PubMed 10637304. Source: UniProtKB endosome membrane Inferred from direct assay PubMed 16757520. Source: UniProtKB late endosome Inferred from direct assay PubMed 10637304. Source: UniProtKB late endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell lysosome Inferred from direct assay PubMed 10637304. Source: UniProtKB nucleus Inferred from direct assay PubMed 16757520. Source: UniProtKB vacuolar membrane Inferred from direct assay PubMed 10637304. Source: UniProtKB
Molecular_function	ATP binding Inferred from mutant phenotype PubMed 10637304. Source: UniProtKB ATPase activity, coupled Non-traceable author statement PubMed 16174732. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 444

444

Vacuolar protein sorting-associated protein 4B

PRO_0000084767

Regions

Domain

4 – 82

79

MIT

Nucleotide binding

174 – 181

8

ATP Potential

Coiled coil

19 – 82

64

Potential

Amino acid modifications

Modified residue

93

1

Phosphoserine Ref.19

Modified residue

102

1

Phosphoserine Ref.9 Ref.12 Ref.14 Ref.15 Ref.19 Ref.21

Modified residue

108

1

Phosphoserine Ref.19

Natural variations

Natural variant

58

1

I → M Common polymorphism; induces thermal instability. Ref.22
Corresponds to variant rs17688948 [ dbSNP | Ensembl ].

VAR_023385

Experimental info

Mutagenesis

15

1

A → D: Reduces HIV-1 release 10-fold; when associated with D-66. Ref.11

Mutagenesis

15

1

A → D: Reduces HIV-1 release 2-fold. Ref.11

Mutagenesis

66

1

L → D: Reduces HIV-1 release 10-fold; when associated with D-15. Ref.11

Mutagenesis

66

1

L → D: Reduces HIV-1 release 3-fold. Ref.11

Mutagenesis

208 – 209

2

WL → AA: Strongly impairs HIV-1 release.

Mutagenesis

210

1

G → A: Impairs HIV-1 release. Ref.23

Mutagenesis

235

1

E → Q: Defective in vacuolar protein sorting. Ref.1

Mutagenesis

390 – 396

7

Missing: Abolishes interaction with VTA1. Ref.13

Sequence conflict

114

1

K → R in AAC39874. Ref.3

Sequence conflict

127

1

E → D in AAC39874. Ref.3

Sequence conflict

342

1

S → G in AAC39874. Ref.3

Secondary structure

1

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444

Helix Strand Turn

Details...

Turn

1 – 3

3

Helix

6 – 23

18

Helix

30 – 47

18

Helix

52 – 55

4

Helix

56 – 72

17

Turn

73 – 75

3

Beta strand

87 – 89

3

Beta strand

125 – 127

3

Helix

133 – 135

3

Helix

140 – 155

16

Helix

157 – 159

3

Beta strand

168 – 178

11

Helix

180 – 190

11

Beta strand

195 – 200

6

Helix

213 – 225

13

Beta strand

227 – 234

8

Turn

235 – 237

3

Helix

238 – 240

3

Beta strand

243 – 245

3

Helix

250 – 263

14

Beta strand

265 – 267

3

Beta strand

272 – 279

8

Turn

281 – 283

3

Helix

286 – 290

5

Beta strand

294 – 297

4

Helix

303 – 314

12

Helix

323 – 331

9

Helix

338 – 349

12

Helix

351 – 358

8

Beta strand

360 – 368

9

Beta strand

375 – 383

9

Beta strand

386 – 388

3

Beta strand

391 – 393

3

Helix

396 – 398

3

Helix

401 – 403

3

Helix

411 – 419

9

Helix

427 – 438

12

Sequences

	Sequence		Length	Mass (Da)
	O75351 [UniParc]. Last modified January 16, 2004. Version 2. Checksum: 9D565E4B20AF73FB	FASTA	444	49,302
	10 20 30 40 50 60 MSSTSPNLQK AIDLASKAAQ EDKAGNYEEA LQLYQHAVQY FLHVVKYEAQ GDKAKQSIRA 70 80 90 100 110 120 KCTEYLDRAE KLKEYLKNKE KKAQKPVKEG QPSPADEKGN DSDGEGESDD PEKKKLQNQL 130 140 150 160 170 180 QGAIVIERPN VKWSDVAGLE GAKEALKEAV ILPIKFPHLF TGKRTPWRGI LLFGPPGTGK 190 200 210 220 230 240 SYLAKAVATE ANNSTFFSIS SSDLVSKWLG ESEKLVKNLF QLARENKPSI IFIDEIDSLC 250 260 270 280 290 300 GSRSENESEA ARRIKTEFLV QMQGVGVDND GILVLGATNI PWVLDSAIRR RFEKRIYIPL 310 320 330 340 350 360 PEPHARAAMF KLHLGTTQNS LTEADFRELG RKTDGYSGAD ISIIVRDALM QPVRKVQSAT 370 380 390 400 410 420 HFKKVRGPSR ADPNHLVDDL LTPCSPGDPG AIEMTWMDVP GDKLLEPVVS MSDMLRSLSN 430 440 TKPTVNEHDL LKLKKFTEDF GQEG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mammalian cells express two VPS4 proteins both of which are involved in intracellular protein trafficking." Scheuring S., Roehricht R.A., Schoening-Burkhardt B., Beyer A., Mueller S., Abts H.F., Koehrer K. J. Mol. Biol. 312:469-480(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH VPS4A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLU-235.
[2]	"Comparative sequence and expression analyses of four mammalian VPS4 genes." Beyer A., Scheuring S., Mueller S., Mincheva A., Lichter P., Koehrer K. Gene 305:47-59(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Skin.
[3]	"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning." Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z. Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Umbilical cord blood.
[4]	"Identification of a human cell migration gene 1." Kim J.W. Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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 (JUL-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]. Tissue: Testis.
[7]	"CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins." Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M. J. Cell Sci. 114:2395-2404(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHMP2A.
[8]	"The protein network of HIV budding." von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y., Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A., Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I. Cell 114:701-713(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP1A; CHMP1B CHMP2A; CHMP4B AND CHMP6, SUBCELLULAR LOCATION.
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[11]	"Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding." Kieffer C., Skalicky J.J., Morita E., De Domenico I., Ward D.M., Kaplan J., Sundquist W.I. Dev. Cell 15:62-73(2008) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF ALA-15 AND LEU-66.
[12]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly." Shim S., Merrill S.A., Hanson P.I. Mol. Biol. Cell 19:2661-2672(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VTA1, MUTAGENESIS OF 390-GLY--TRP-396.
[14]	"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-102, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, MASS SPECTROMETRY. Tissue: Liver.
[16]	"Helical structures of ESCRT-III are disassembled by VPS4." Lata S., Schoehn G., Jain A., Pires R., Piehler J., Goettlinger H.G., Weissenhorn W. Science 321:1354-1357(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ASSOCIATION WITH THE CHMP2A-CHMP3 POLYMER, ELECTRON MICROSCOPY.
[17]	"Biochemical analyses of human IST1 and its function in cytokinesis." Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M., Sundquist W.I. Mol. Biol. Cell 20:1360-1373(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH IST1.
[18]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"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-93; SER-102 AND SER-108, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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].
[21]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, MASS SPECTROMETRY.
[22]	"Structural characterization of the MIT domain from human Vps4b." Takasu H., Jee J.G., Ohno A., Goda N., Fujiwara K., Tochio H., Shirakawa M., Hiroaki H. Biochem. Biophys. Res. Commun. 334:460-465(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-77, DOMAIN, VARIANT MET-58.
[23]	"Structural and mechanistic studies of VPS4 proteins." Scott A., Chung H.Y., Gonciarz-Swiatek M., Hill G.C., Whitby F.G., Gaspar J., Holton J.M., Viswanathan R., Ghaffarian S., Hill C.P., Sundquist W.I. EMBO J. 24:3658-3669(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 123-444, SUBUNIT, INTERACTION WITH VTA1, MUTAGENESIS OF 208-TRP-LEU-209 AND GLY-210.
[24]	"Solution structure of MIT domain from human SKD1." RIKEN structural genomics initiative (RSGI) Submitted (NOV-2005) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-108.
[25]	"ESCRT-III recognition by VPS4 ATPases." Stuchell-Brereton M.D., Skalicky J.J., Kieffer C., Karren M.A., Ghaffarian S., Sundquist W.I. Nature 449:740-744(2007) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-86 IN COMPLEX WITH CHMP2B, INTERACTION WITH CHMP1B.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF195514 mRNA. Translation: AAG33022.1.
AF282904 Genomic DNA. Translation: AAG01471.1.
AF038960 mRNA. Translation: AAC39874.1.
AY232629 mRNA. Translation: AAP59551.1.
CH471096 Genomic DNA. Translation: EAW63143.1.
BC039574 mRNA. Translation: AAH39574.1.

IPI

IPI00182728.

RefSeq

NP_004860.2. NM_004869.3.

UniGene

Hs.126550.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WR0	NMR	-	A	1-77	[»]
1XWI	X-ray	2.80	A	123-444	[»]
2CPT	NMR	-	A	1-104	[»]
2JQH	NMR	-	A	1-86	[»]
2JQK	NMR	-	A	1-86	[»]

ProteinModelPortal

O75351.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75351. 1 interaction.

STRING

9606.ENSP00000238497.

PTM databases

PhosphoSite

O75351.

Proteomic databases

PaxDb

O75351.

PeptideAtlas

O75351.

PRIDE

O75351.

Protocols and materials databases

DNASU

9525.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000238497; ENSP00000238497; ENSG00000119541.

GeneID

9525.

KEGG

hsa:9525.

UCSC

uc002lix.3. human.

Organism-specific databases

CTD

9525.

GeneCards

GC18M061056.

HGNC

HGNC:10895. VPS4B.

HPA

CAB046445.

MIM

609983. gene.

neXtProt

NX_O75351.

PharmGKB

PA35795.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0464.

HOGENOM

HOG000225146.

HOVERGEN

HBG057074.

InParanoid

O75351.

KO

K12196.

OMA

AKCAEYL.

OrthoDB

EOG4G1MGD.

PhylomeDB

O75351.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

Bgee

O75351.

CleanEx

HS_VPS4B.

Genevestigator

O75351.

GermOnline

ENSG00000119541. Homo sapiens.

Family and domain databases

InterPro

IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR015415. Vps4_C.
[Graphical view]

Pfam

PF00004. AAA. 1 hit.
PF04212. MIT. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]

SMART

SM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]

PROSITE

PS00674. AAA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O75351.

GenomeRNAi

9525.

NextBio

35700.

SOURCE

Search...

Entry information

Entry name

VPS4B_HUMAN

Accession

Primary (citable) accession number: O75351
Secondary accession number(s): Q69HW4, Q9GZS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 16, 2004
Last modified:	May 1, 2013
This is version 126 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.