Q15286 (RAB35_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-35

Alternative name(s):
GTP-binding protein RAY
Ras-related protein Rab-1C

Gene names

Name:	RAB35
Synonyms:	RAB1C, RAY

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

General annotation (Comments)

Function	In the process of endocytosis, essential rate-limiting regulator of a fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. Ref.9
Subunit structure	Interacts with DENND1A and DENND1B in a nucleotide-dependent manner. The low binding to DENND1C is nucleotide-independent. All 3 DENND1 act as GEFs for RAB35 and thus activate the protein. Ref.11 Ref.13 Ref.14
Subcellular location	Cell membrane; Lipid-anchor; Cytoplasmic side Potential. Membrane › clathrin-coated pit. Cytoplasmic vesicle › clathrin-coated vesicle. Endosome. Melanosome. Note: Present on sorting endosomes and endosomal tubules. Tends to be enriched in PIP2-positive cell membrane domains. During mitosis, associated with the plasma membrane and present at the ingressing furrow during early cytokinesis as well as at the intercellular bridge later during cytokinesis. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.9 Ref.10
Post-translational modification	AMPylation at Tyr-77 by L.pneumophila DrrA occurs in the switch 2 region and leads to moderate inactivation of the GTPase activity. It appears to prolong the lifetime of the GTP state of RAB1B by restricting access of GTPase effectors to switch 2 and blocking effector-stimulated GTP hydrolysis, thereby rendering RAB35 constitutively active. Phosphocholinated by L.pneumophila AnkX. Both GDP-bound and GTP-bound forms can be phosphocholinated. Phosphocholination inhibits the GEF activity of DENND1A.
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell membrane Coated pit Cytoplasmic vesicle Endosome Membrane
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokinesis Inferred from mutant phenotype Ref.9. Source: UniProtKB endosomal transport Inferred from mutant phenotype Ref.9. Source: UniProtKB protein localization Inferred from mutant phenotype Ref.9. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cell projection membrane Inferred from direct assay Ref.9. Source: UniProtKB clathrin-coated endocytic vesicle Inferred from direct assay Ref.9. Source: UniProtKB coated pit Inferred from direct assay Ref.9. Source: UniProtKB endosome Inferred from electronic annotation. Source: UniProtKB-SubCell intercellular bridge Inferred from direct assay Ref.9. Source: UniProtKB melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	GDP binding Inferred from direct assay PubMed 20937701. Source: UniProtKB GTP binding Inferred from direct assay PubMed 20937701. Source: UniProtKB GTPase activity Traceable author statement Ref.1. Source: ProtInc phosphatidylinositol-4,5-bisphosphate binding Inferred from direct assay Ref.9. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q15286-1)

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: Q15286-2)

The sequence of this isoform differs from the canonical sequence as follows:
     118-201: VGNKNDDPER...KNSKRKKRCC → DVQLHHGAGPPSKERQPGKTAAATTERCGEAHEEQ

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 201

201

Ras-related protein Rab-35

PRO_0000121245

Regions

Nucleotide binding

15 – 22

8

GTP By similarity

Nucleotide binding

63 – 67

5

GTP By similarity

Nucleotide binding

120 – 123

4

GTP By similarity

Motif

37 – 45

9

Effector region By similarity

Amino acid modifications

Modified residue

75

1

O-(2-cholinephosphoryl)serine; by Legionella AnkX Probable

Modified residue

77

1

O-AMP-tyrosine; by Legionella DrrA Probable

Lipidation

200

1

S-geranylgeranyl cysteine By similarity

Lipidation

201

1

S-geranylgeranyl cysteine By similarity

Natural variations

Alternative sequence

118 – 201

84

VGNKN…KKRCC → DVQLHHGAGPPSKERQPGKT AAATTERCGEAHEEQ in isoform 2.

VSP_042918

Experimental info

Mutagenesis

22

1

S → N: Destabilization of the intercellular bridge during cytokinesis. Strong reduction in fast recycling. Ref.9

Mutagenesis

67

1

Q → L: Loss of GTPase activity. Increased fast recycling. Ref.9

Secondary structure

1

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201

Helix Strand Turn

Details...

Beta strand

7 – 14

8

Helix

21 – 28

8

Turn

38 – 40

3

Beta strand

41 – 52

12

Beta strand

55 – 64

10

Helix

67 – 69

3

Helix

75 – 78

4

Beta strand

82 – 89

8

Helix

93 – 109

17

Beta strand

113 – 120

8

Helix

125 – 127

3

Helix

132 – 142

11

Beta strand

146 – 148

3

Turn

151 – 154

4

Helix

157 – 175

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 31EB15D6D42E076E	FASTA	201	23,025
	10 20 30 40 50 60 MARDYDHLFK LLIIGDSGVG KSSLLLRFAD NTFSGSYITT IGVDFKIRTV EINGEKVKLQ 70 80 90 100 110 120 IWDTAGQERF RTITSTYYRG THGVIVVYDV TSAESFVNVK RWLHEINQNC DDVCRILVGN 130 140 150 160 170 180 KNDDPERKVV ETEDAYKFAG QMGIQLFETS AKENVNVEEM FNCITELVLR AKKDNLAKQQ 190 200 QQQQNDVVKL TKNSKRKKRC C
	Isoform 2 [UniParc]. Checksum: 711F975E26440998	FASTA	152	17,058
	10 20 30 40 50 60 MARDYDHLFK LLIIGDSGVG KSSLLLRFAD NTFSGSYITT IGVDFKIRTV EINGEKVKLQ 70 80 90 100 110 120 IWDTAGQERF RTITSTYYRG THGVIVVYDV TSAESFVNVK RWLHEINQNC DDVCRILDVQ 130 140 150 LHHGAGPPSK ERQPGKTAAA TTERCGEAHE EQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of two small GTP-binding proteins from human skeletal muscle." Zhu A.X., Zhao Y., Flier J.S. Biochem. Biophys. Res. Commun. 205:1875-1882(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Muscle.
[2]	"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)." Puhl H.L. III, Ikeda S.R., Aronstam R.S. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) 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] (ISOFORMS 1 AND 2). Tissue: Tongue and Uterus.
[6]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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].
[8]	"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: Uterus.
[9]	"Rab35 regulates an endocytic recycling pathway essential for the terminal steps of cytokinesis." Kouranti I., Sachse M., Arouche N., Goud B., Echard A. Curr. Biol. 16:1719-1725(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-22 AND GLN-67.
[10]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[11]	"The connecdenn family, Rab35 guanine nucleotide exchange factors interfacing with the clathrin machinery." Marat A.L., McPherson P.S. J. Biol. Chem. 285:10627-10637(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DENND1A; DENND1B AND DENND1C.
[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]	"Modulation of Rab GTPase function by a protein phosphocholine transferase." Mukherjee S., Liu X., Arasaki K., McDonough J., Galan J.E., Roy C.R. Nature 477:103-106(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH L.PNEUMOPHILA ANKX AND DRRA, AMPYLATION AT TYR-77, CHOLINEPHOSPHORYLATION AT SER-75.
[14]	"Reversible phosphocholination of Rab proteins by Legionella pneumophila effector proteins." Goody P.R., Heller K., Oesterlin L.K., Muller M.P., Itzen A., Goody R.S. EMBO J. 31:1774-1784(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH L.PNEUMOPHILA ANKX AND DRRA, AMPYLATION, CHOLINEPHOSPHORYLATION.
[15]	"Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate." Wu X., Bradley M.J., Cai Y., Kummel D., De La Cruz E.M., Barr F.A., Reinisch K.M. Proc. Natl. Acad. Sci. U.S.A. 108:18672-18677(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-180 IN COMPLEX WITH DENND1B.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X79781 mRNA. Translation: CAA56177.1.
AF498960 mRNA. Translation: AAM21108.1.
BT020024 mRNA. Translation: AAV38827.1.
CR536486 mRNA. Translation: CAG38725.1.
CR541683 mRNA. Translation: CAG46484.1.
AK304620 mRNA. Translation: BAG65402.1.
AK312538 mRNA. Translation: BAG35437.1.
AC004812 Genomic DNA. Translation: AAC83182.1.
CH471054 Genomic DNA. Translation: EAW98163.1.
CH471054 Genomic DNA. Translation: EAW98164.1.
BC015931 mRNA. Translation: AAH15931.1.

IPI

IPI00300096.
IPI00953892.

PIR

JC2488.

RefSeq

NP_001161078.1. NM_001167606.1.
NP_006852.1. NM_006861.6.

UniGene

Hs.524788.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3TW8	X-ray	2.10	B/D	1-180	[»]

ProteinModelPortal

Q15286.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15286. 10 interactions.

MINT

MINT-1370578.

STRING

9606.ENSP00000229340.

PTM databases

PhosphoSite

Q15286.

Polymorphism databases

DMDM

3024525.

Proteomic databases

PaxDb

Q15286.

PRIDE

Q15286.

Protocols and materials databases

DNASU

11021.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000229340; ENSP00000229340; ENSG00000111737.
ENST00000534951; ENSP00000441883; ENSG00000111737.

GeneID

11021.

KEGG

hsa:11021.

UCSC

uc001txm.2. human.

Organism-specific databases

CTD

11021.

GeneCards

GC12M120532.

HGNC

HGNC:9774. RAB35.

HPA

HPA054146.

MIM

604199. gene.

neXtProt

NX_Q15286.

PharmGKB

PA34127.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1100.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

Q15286.

KO

K07876.

OMA

NCDVVNR.

OrthoDB

EOG4QVCD5.

Gene expression databases

ArrayExpress

Q15286.

Bgee

Q15286.

CleanEx

HS_RAB35.

Genevestigator

Q15286.

GermOnline

ENSG00000111737. Homo sapiens.

Family and domain databases

InterPro

IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]

Pfam

PF00071. Ras. 1 hit.
[Graphical view]

PRINTS

PR00449. RASTRNSFRMNG.

SMART

SM00175. RAB. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00231. small_GTP. 1 hit.

PROSITE

PS51419. RAB. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

11021.

NextBio

41874.

SOURCE

Search...

Entry information

Entry name

RAB35_HUMAN

Accession

Primary (citable) accession number: Q15286
Secondary accession number(s): B2R6E0, B4E390

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 124 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.