P51149 (RAB7A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-7a

Gene names

Name:	RAB7A
Synonyms:	RAB7

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	207 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in late endocytic transport. Contributes to the maturation of phagosomes (acidification). Ref.8 Ref.10
Subunit structure	Interacts with RILP. Interacts with PSMA7. Interacts with RNF115. Interacts with FYCO1. Ref.8 Ref.11 Ref.12 Ref.15 Ref.19
Subcellular location	Late endosome. Lysosome. Cytoplasmic vesicle › phagosome. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.9 Ref.10 Ref.14
Tissue specificity	Widely expressed; high expression found in skeletal muscle. Ref.22
Involvement in disease	Defects in RAB7A are the cause of Charcot-Marie-Tooth disease type 2B (CMT2B) [MIM:600882]; also known as hereditary motor and sensory neuropathy II (HMSN2). CMT2B is a form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathy or CMT1, and primary peripheral axonal neuropathy or CMT2. Neuropathies of the CMT2 group are characterized by signs of axonal regeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. CMT2B is clinically characterized by marked distal muscle weakness and a high frequency of foot ulcers, infections and amputations of the toes. CMT2B inheritance is autosomal dominant. Ref.22 Ref.23 Ref.24
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.
Sequence caution	The sequence BAA91390.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame. The sequence BAF83410.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame. The sequence EAW79303.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cytoplasmic vesicle Endosome Lysosome
Disease	Charcot-Marie-Tooth disease Disease mutation Neuropathy
Ligand	GTP-binding Nucleotide-binding
PTM	Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	endocytosis Traceable author statement. Source: ProtInc endosome to lysosome transport Inferred from mutant phenotype. Source: BHF-UCL epidermal growth factor catabolic process Inferred from mutant phenotype. Source: BHF-UCL protein transport Inferred from electronic annotation. Source: UniProtKB-KW small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA late endosome Inferred from direct assay. Source: MGI lysosome Inferred from direct assay. Source: MGI melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell phagocytic vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	GDP binding Inferred from direct assay. Source: BHF-UCL GTP binding Inferred from direct assay. Source: BHF-UCL GTPase activity Inferred from direct assay. Source: BHF-UCL protein binding Inferred from physical interaction Ref.15Ref.19. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 207

207

Ras-related protein Rab-7a

PRO_0000121121

Regions

Nucleotide binding

15 – 22

8

GTP By similarity

Nucleotide binding

63 – 67

5

GTP By similarity

Nucleotide binding

125 – 128

4

GTP By similarity

Motif

37 – 45

9

Effector region By similarity

Amino acid modifications

Modified residue

72

1

Phosphoserine Ref.17 Ref.18

Modified residue

183

1

Phosphotyrosine Ref.13 Ref.16

Modified residue

207

1

Cysteine methyl ester By similarity

Lipidation

205

1

S-geranylgeranyl cysteine By similarity

Lipidation

207

1

S-geranylgeranyl cysteine By similarity

Natural variations

Natural variant

32

1

K → E.
Corresponds to variant rs11549759 [ dbSNP | Ensembl ].

VAR_037886

Natural variant

129

1

L → F in CMT2B. Ref.22

VAR_018722

Natural variant

157

1

K → N in CMT2B. Ref.24

VAR_037887

Natural variant

161

1

N → T in CMT2B. Ref.23

VAR_037888

Natural variant

162

1

V → M in CMT2B. Ref.22

VAR_018723

Experimental info

Mutagenesis

8

1

L → A: Abolishes interaction with RAB7 and reduces its localization to late endosomal/lysosomal compartments. Ref.21

Mutagenesis

10

1

K → A: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments. Ref.21

Mutagenesis

22

1

T → N: Abolishes localization on late endosomes, lysosomes and phagosomes and reduces phagosomal fusions. Abolishes association of RILP with the phagosomes. Ref.10

Mutagenesis

67

1

Q → L: Does not abolish localization on late endosomes, lysosomes and phagosomes and does not reduce phagosomal fusions. Ref.10

Mutagenesis

180

1

V → A: Abolishes interaction with RAB7 and localization to late endosomal/lysosomal compartments. Ref.21

Mutagenesis

182

1

L → A: Does not abolish interaction with RAB7 and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RAB7 and localization to late endosomal/lysosomal compartments; when associated with A-183. Ref.21

Mutagenesis

183

1

Y → A: Does not abolish interaction with RAB7 and localization to late endosomal/lysosomal compartments. Does not abolish interaction with RAB7 and localization to late endosomal/lysosomal compartments; when associated with A-182. Ref.21

Sequence conflict

47

1

T → I in AAD02565. Ref.3

Sequence conflict

108

1

I → V in AAA86640. Ref.2

Sequence conflict

127

1

I → V in AAA86640. Ref.2

Sequence conflict

180

1

V → E in AAD02565. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

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.

.

207

Helix Strand Turn

Details...

Beta strand

8 – 14

7

Helix

21 – 30

10

Beta strand

42 – 54

13

Beta strand

56 – 64

9

Helix

68 – 70

3

Beta strand

82 – 89

8

Helix

93 – 97

5

Helix

99 – 110

12

Helix

115 – 117

3

Beta strand

120 – 125

6

Helix

136 – 145

10

Beta strand

151 – 153

3

Turn

156 – 159

4

Helix

162 – 181

20

Sequences

	Sequence		Length	Mass (Da)
	P51149 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: A2AF33B16A672971	FASTA	207	23,490
	10 20 30 40 50 60 MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV MVDDRLVTMQ 70 80 90 100 110 120 IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD SWRDEFLIQA SPRDPENFPF 130 140 150 160 170 180 VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP YFETSAKEAI NVEQAFQTIA RNALKQETEV 190 200 ELYNEFPEPI KLDKNDRAKA SAESCSC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression analysis of the human Rab7 GTP-ase complementary deoxyribonucleic acid." Vitelli R., Chiariello M., Lattero D., Bruni C.B., Bucci C. Biochem. Biophys. Res. Commun. 229:887-890(1996) [PubMed: 8954989] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Cloning and mapping of human Rab7 and Rab9 cDNA sequences and identification of a Rab9 pseudogene." Davies J.P., Cotter P.D., Ioannou Y.A. Genomics 41:131-134(1997) [PubMed: 9126495] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	Kim J.Y., Park Y.B. Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"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]. Tissue: Brain.
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[6]	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].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[8]	"Rab-interacting lysosomal protein (RILP): the Rab7 effector required for transport to lysosomes." Cantalupo G., Alifano P., Roberti V., Bruni C.B., Bucci C. EMBO J. 20:683-693(2001) [PubMed: 11179213] [Abstract] Cited for: FUNCTION IN LATE ENDOCYTOSIS, INTERACTION WITH RILP.
[9]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E. J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[10]	"Phagosomes fuse with late endosomes and/or lysosomes by extension of membrane protrusions along microtubules: role of Rab7 and RILP." Harrison R.E., Bucci C., Vieira O.V., Schroer T.A., Grinstein S. Mol. Cell. Biol. 23:6494-6506(2003) [PubMed: 12944476] [Abstract] Cited for: FUNCTION IN PHAGOSOMAL BIOGENESIS, MUTAGENESIS OF THR-22 AND GLN-67, SUBCELLULAR LOCATION.
[11]	"The proteasome alpha-subunit XAPC7 interacts specifically with Rab7 and late endosomes." Dong J., Chen W., Welford A., Wandinger-Ness A. J. Biol. Chem. 279:21334-21342(2004) [PubMed: 14998988] [Abstract] Cited for: INTERACTION WITH PSMA7.
[12]	"A unique region of RILP distinguishes it from its related proteins in its regulation of lysosomal morphology and interaction with Rab7 and Rab34." Wang T., Wong K.K., Hong W. Mol. Biol. Cell 15:815-826(2004) [PubMed: 14668488] [Abstract] Cited for: INTERACTION WITH RILP.
[13]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-183, MASS SPECTROMETRY.
[14]	"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: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[15]	"Novel RING E3 ubiquitin ligases in breast cancer." Burger A., Amemiya Y., Kitching R., Seth A.K. Neoplasia 8:689-695(2006) [PubMed: 16925951] [Abstract] Cited for: INTERACTION WITH RNF115.
[16]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-183, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[17]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-72, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport." Pankiv S., Alemu E.A., Brech A., Bruun J.A., Lamark T., Overvatn A., Bjorkoy G., Johansen T. J. Cell Biol. 188:253-269(2010) [PubMed: 20100911] [Abstract] Cited for: INTERACTION WITH FYCO1.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"Structural basis for recruitment of RILP by small GTPase Rab7." Wu M., Wang T., Loh E., Hong W., Song H. EMBO J. 24:1491-1501(2005) [PubMed: 15933719] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH RILP, MUTAGENESIS OF LEU-8; LYS-10; VAL-180; LEU-182 AND TYR-183.
[22]	"Mutations in the small GTP-ase late endosomal protein RAB7 cause Charcot-Marie-Tooth type 2B neuropathy." Verhoeven K., De Jonghe P., Coen K., Verpoorten N., Auer-Grumbach M., Kwon J.M., FitzPatrick D., Schmedding E., De Vriendt E., Jacobs A., Van Gerwen V., Wagner K., Hartung H.-P., Timmerman V. Am. J. Hum. Genet. 72:722-727(2003) [PubMed: 12545426] [Abstract] Cited for: VARIANTS CMT2B PHE-129 AND MET-162, TISSUE SPECIFICITY.
[23]	"A novel RAB7 mutation associated with ulcero-mutilating neuropathy." Houlden H., King R.H.M., Muddle J.R., Warner T.T., Reilly M.M., Orrell R.W., Ginsberg L. Ann. Neurol. 56:586-590(2004) [PubMed: 15455439] [Abstract] Cited for: VARIANT CMT2B THR-161.
[24]	"Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene." Meggouh F., Bienfait H.M.E., Weterman M.A.J., de Visser M., Baas F. Neurology 67:1476-1478(2006) [PubMed: 17060578] [Abstract] Cited for: VARIANT CMT2B ASN-157.
+	Additional computationally mapped references.

Web resources

Inherited peripheral neuropathies mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X93499 mRNA. Translation: CAA63763.1.
U44104 mRNA. Translation: AAA86640.1.
AF050175 Genomic DNA. Translation: AAD02565.1.
AF498942 mRNA. Translation: AAM21090.1.
AK000826 mRNA. Translation: BAA91390.1. Sequence problems.
AK290721 mRNA. Translation: BAF83410.1. Sequence problems.
BC008721 mRNA. Translation: AAH08721.2.
CH471052 Genomic DNA. Translation: EAW79303.1. Sequence problems.

IPI

IPI00016342.

PIR

JC5268.

RefSeq

NP_004628.4. NM_004637.5.

UniGene

Hs.15738.
Hs.728150.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T91	X-ray	1.90	A/B/C/D	1-207	[»]
1YHN	X-ray	3.00	A	1-207	[»]
3LAW	X-ray	2.80	A/B/C/D/E	1-207	[»]

ProteinModelPortal

P51149.

SMR

P51149. Positions 7-190.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39879N.

IntAct

P51149. 4 interactions.

MINT

MINT-4999676.

STRING

P51149.

PTM databases

PhosphoSite

P51149.

Polymorphism databases

DMDM

1709999.

Proteomic databases

PeptideAtlas

P51149.

PRIDE

P51149.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265062; ENSP00000265062; ENSG00000075785.
ENST00000430113; ENSP00000415956; ENSG00000075785.

GeneID

7879.

KEGG

hsa:7879.

UCSC

uc003eks.1. human.

Organism-specific databases

CTD

7879.

GeneCards

GC03P128444.

H-InvDB

HIX0003657.

HGNC

HGNC:9788. RAB7A.

HPA

HPA006964.

MIM

600882. phenotype.
602298. gene.

neXtProt

NX_P51149.

Orphanet

99936. Autosomal dominant Charcot-Marie-Tooth disease type 2B.

PharmGKB

PA162400619.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16295.

GeneTree

ENSGT00600000084038.

HOGENOM

HBG745225.

HOVERGEN

HBG009351.

InParanoid

P51149.

OMA

SPRDPEH.

OrthoDB

EOG4QFWF4.

PhylomeDB

P51149.

Enzyme and pathway databases

Pathway_Interaction_DB

il12_2pathway. IL12-mediated signaling events.

Gene expression databases

ArrayExpress

P51149.

Bgee

P51149.

CleanEx

HS_RAB7A.

Genevestigator

P51149.

GermOnline

ENSG00000075785. Homo sapiens.

Family and domain databases

InterPro

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

KO

K07897.

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

NextBio

30336.

SOURCE

Search...

Entry information

Entry name

RAB7A_HUMAN

Accession

Primary (citable) accession number: P51149
Secondary accession number(s): A8K3V6, Q9NWJ0, Q9UPB0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 129 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.