Q9NV58 (RN19A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase RNF19A
EC=6.3.2.-

Alternative name(s):
Double ring-finger protein
Short name=Dorfin
RING finger protein 19A
p38

Gene names

Name:	RNF19A
Synonyms:	RNF19

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

General annotation (Comments)

Function	E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as SNCAIP or CASR. Specifically ubiquitinates pathogenic SOD1 variants, which leads to their proteasomal degradation and to neuronal protection. Ref.1 Ref.7 Ref.8 Ref.9 Ref.10
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with UBE2L3 and UBE2L6. Interacts with transcription factor Sp1. Interacts with VCP, CASR, SNCAIP and with some SOD1 variants which cause amyotrophic lateral sclerosis, but not with wild-type SOD1. Ref.1 Ref.5 Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Membrane; Multi-pass membrane protein Potential. Cytoplasm › cytoskeleton › centrosome. Note: Present in the hyaline inclusion bodies specifically found in motor neurons from amyotrophic lateral sclerosis patients. Present in the Lewy bodies specifically found in neurons from Parkinson disease patients. Ref.1 Ref.7 Ref.8 Ref.9
Tissue specificity	Widely expressed, with highest levels in heart. Ubiquitously expressed in the central nervous system. Ref.1
Sequence similarities	Belongs to the RBR family. RNF19 subfamily. Contains 1 IBR-type zinc finger. Contains 2 RING-type zinc fingers.
Sequence caution	The sequence BAB14581.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB15647.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Transmembrane Transmembrane helix Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein modification process Non-traceable author statement. Source: UniProtKB microtubule cytoskeleton organization Traceable author statement Ref.1. Source: UniProtKB protein ubiquitination Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	centrosome Traceable author statement Ref.1. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ligase activity Inferred from electronic annotation. Source: UniProtKB-KW transcription factor binding Traceable author statement Ref.5. Source: UniProtKB zinc ion binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NV58-1)

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: Q9NV58-2)

The sequence of this isoform differs from the canonical sequence as follows:
     572-604: RYSLSGESGTVSLGTVSDNASTKAMAGSILNSY → AAVAAAGRWAYSPATLRCRRSEELKNIHDSS
     605-838: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: Q9NV58-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 838	838	E3 ubiquitin-protein ligase RNF19A		PRO_0000056061
Regions
	Transmembrane	368 – 388	21	Helical; Potential
	Transmembrane	424 – 444	21	Helical; Potential
	Zinc finger	132 – 179	48	RING-type 1
	Zinc finger	199 – 264	66	IBR-type
	Zinc finger	301 – 332	32	RING-type 2
	Region	660 – 838	179	Interaction with CASR
Amino acid modifications
	Modified residue	631	1	Phosphoserine Ref.12
Natural variations
	Alternative sequence	1 – 31	31	Missing in isoform 3.		VSP_028631
	Alternative sequence	572 – 604	33	RYSLS…ILNSY → AAVAAAGRWAYSPATLRCRR SEELKNIHDSS in isoform 2.		VSP_021010
	Alternative sequence	605 – 838	234	Missing in isoform 2.		VSP_021011
	Natural variant	835	1	Q → H. Corresponds to variant rs9642785 [ dbSNP | Ensembl ].		VAR_028045
Experimental info
	Mutagenesis	132	1	C → S: Abolishes interaction with VCP and E3 ligase activity toward mutant SOD1; when associated with S-135. Ref.9
	Mutagenesis	135	1	C → S: Abolishes interaction with VCP and E3 ligase activity toward mutant SOD1; when associated with S-132. Ref.9
	Sequence conflict	645	1	H → Y in BAB39353. Ref.1
	Sequence conflict	744	1	S → R in CAB53700. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 00A7DED5023FDC06	FASTA	838	90,696
	10 20 30 40 50 60 MQEQEIGFIS KYNEGLCVNT DPVSILTSIL DMSLHRQMGS DRDLQSSASS VSLPSVKKAP 70 80 90 100 110 120 KKRRISIGSL FRRKKDNKRK SRELNGGVDG IASIESIHSE MCTDKNSIFS TNTSSDNGLT 130 140 150 160 170 180 SISKQIGDFI ECPLCLLRHS KDRFPDIMTC HHRSCVDCLR QYLRIEISES RVNISCPECT 190 200 210 220 230 240 ERFNPHDIRL ILSDDVLMEK YEEFMLRRWL VADPDCRWCP APDCGYAVIA FGCASCPKLT 250 260 270 280 290 300 CGREGCGTEF CYHCKQIWHP NQTCDAARQE RAQSLRLRTI RSSSISYSQE SGAAADDIKP 310 320 330 340 350 360 CPRCAAYIIK MNDGSCNHMT CAVCGCEFCW LCMKEISDLH YLSPSGCTFW GKKPWSRKKK 370 380 390 400 410 420 ILWQLGTLVG APVGIALIAG IAIPAMIIGI PVYVGRKIHN RYEGKDVSKH KRNLAIAGGV 430 440 450 460 470 480 TLSVIVSPVV AAVTVGIGVP IMLAYVYGVV PISLCRSGGC GVSAGNGKGV RIEFDDENDI 490 500 510 520 530 540 NVGGTNTAVD TTSVAEARHN PSIGEGSVGG LTGSLSASGS HMDRIGAIRD NLSETASTMA 550 560 570 580 590 600 LAGASITGSL SGSAMVNCFN RLEVQADVQK ERYSLSGESG TVSLGTVSDN ASTKAMAGSI 610 620 630 640 650 660 LNSYIPLDKE GNSMEVQVDI ESKPSKFRHN SGSSSVDDGS ATRSHAGGSS SGLPEGKSSA 670 680 690 700 710 720 TKWSKEATAG KKSKSGKLRK KGNMKINETR EDMDAQLLEQ QSTNSSEFEA PSLSDSMPSV 730 740 750 760 770 780 ADSHSSHFSE FSCSDLESMK TSCSHGSSDY HTRFATVNIL PEVENDRLEN SPHQCSISVV 790 800 810 820 830 TQTASCSEVS QLNHIAEEHG NNGIKPNVDL YFGDALKETN NNHSHQTMEL KVAIQTEI
	Isoform 2 [UniParc]. Checksum: 0B210220B7C0F623	FASTA	602	65,416
	10 20 30 40 50 60 MQEQEIGFIS KYNEGLCVNT DPVSILTSIL DMSLHRQMGS DRDLQSSASS VSLPSVKKAP 70 80 90 100 110 120 KKRRISIGSL FRRKKDNKRK SRELNGGVDG IASIESIHSE MCTDKNSIFS TNTSSDNGLT 130 140 150 160 170 180 SISKQIGDFI ECPLCLLRHS KDRFPDIMTC HHRSCVDCLR QYLRIEISES RVNISCPECT 190 200 210 220 230 240 ERFNPHDIRL ILSDDVLMEK YEEFMLRRWL VADPDCRWCP APDCGYAVIA FGCASCPKLT 250 260 270 280 290 300 CGREGCGTEF CYHCKQIWHP NQTCDAARQE RAQSLRLRTI RSSSISYSQE SGAAADDIKP 310 320 330 340 350 360 CPRCAAYIIK MNDGSCNHMT CAVCGCEFCW LCMKEISDLH YLSPSGCTFW GKKPWSRKKK 370 380 390 400 410 420 ILWQLGTLVG APVGIALIAG IAIPAMIIGI PVYVGRKIHN RYEGKDVSKH KRNLAIAGGV 430 440 450 460 470 480 TLSVIVSPVV AAVTVGIGVP IMLAYVYGVV PISLCRSGGC GVSAGNGKGV RIEFDDENDI 490 500 510 520 530 540 NVGGTNTAVD TTSVAEARHN PSIGEGSVGG LTGSLSASGS HMDRIGAIRD NLSETASTMA 550 560 570 580 590 600 LAGASITGSL SGSAMVNCFN RLEVQADVQK EAAVAAAGRW AYSPATLRCR RSEELKNIHD SS
	Isoform 3 [UniParc]. Checksum: F50D47C3EA851842	FASTA	807	87,256
	10 20 30 40 50 60 MSLHRQMGSD RDLQSSASSV SLPSVKKAPK KRRISIGSLF RRKKDNKRKS RELNGGVDGI 70 80 90 100 110 120 ASIESIHSEM CTDKNSIFST NTSSDNGLTS ISKQIGDFIE CPLCLLRHSK DRFPDIMTCH 130 140 150 160 170 180 HRSCVDCLRQ YLRIEISESR VNISCPECTE RFNPHDIRLI LSDDVLMEKY EEFMLRRWLV 190 200 210 220 230 240 ADPDCRWCPA PDCGYAVIAF GCASCPKLTC GREGCGTEFC YHCKQIWHPN QTCDAARQER 250 260 270 280 290 300 AQSLRLRTIR SSSISYSQES GAAADDIKPC PRCAAYIIKM NDGSCNHMTC AVCGCEFCWL 310 320 330 340 350 360 CMKEISDLHY LSPSGCTFWG KKPWSRKKKI LWQLGTLVGA PVGIALIAGI AIPAMIIGIP 370 380 390 400 410 420 VYVGRKIHNR YEGKDVSKHK RNLAIAGGVT LSVIVSPVVA AVTVGIGVPI MLAYVYGVVP 430 440 450 460 470 480 ISLCRSGGCG VSAGNGKGVR IEFDDENDIN VGGTNTAVDT TSVAEARHNP SIGEGSVGGL 490 500 510 520 530 540 TGSLSASGSH MDRIGAIRDN LSETASTMAL AGASITGSLS GSAMVNCFNR LEVQADVQKE 550 560 570 580 590 600 RYSLSGESGT VSLGTVSDNA STKAMAGSIL NSYIPLDKEG NSMEVQVDIE SKPSKFRHNS 610 620 630 640 650 660 GSSSVDDGSA TRSHAGGSSS GLPEGKSSAT KWSKEATAGK KSKSGKLRKK GNMKINETRE 670 680 690 700 710 720 DMDAQLLEQQ STNSSEFEAP SLSDSMPSVA DSHSSHFSEF SCSDLESMKT SCSHGSSDYH 730 740 750 760 770 780 TRFATVNILP EVENDRLENS PHQCSISVVT QTASCSEVSQ LNHIAEEHGN NGIKPNVDLY 790 800 FGDALKETNN NHSHQTMELK VAIQTEI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity." Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G. Biochem. Biophys. Res. Commun. 281:706-713(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH UBE2L3 AND UBE2L6, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Spinal cord.
[2]	"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.
[3]	"Expression and promoter activity of MaLR element of Dorfin gene related to Parkinson disease." Kim T., Huh J., Kim H. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-89 (ISOFORM 3).
[4]	"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] OF 426-838 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-838 (ISOFORM 2). Tissue: Hepatoma, Ovarian carcinoma and Placenta.
[5]	"A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening." Gunther M., Laithier M., Brison O. Mol. Cell. Biochem. 210:131-142(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 422-824 (ISOFORM 1), INTERACTION WITH SP1. Tissue: Colon.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 524-838 (ISOFORM 1). Tissue: Fetal kidney and Testis.
[7]	"Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity." Niwa J., Ishigaki S., Hishikawa N., Yamamoto M., Doyu M., Murata S., Tanaka K., Taniguchi N., Sobue G. J. Biol. Chem. 277:36793-36798(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SOD1.
[8]	"Dorfin localizes to Lewy bodies and ubiquitylates synphilin-1." Ito T., Niwa J., Hishikawa N., Ishigaki S., Doyu M., Sobue G. J. Biol. Chem. 278:29106-29114(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNCAIP.
[9]	"Physical and functional interaction between dorfin and valosin-containing protein that are colocalized in ubiquitylated inclusions in neurodegenerative disorders." Ishigaki S., Hishikawa N., Niwa J., Iemura S., Natsume T., Hori S., Kakizuka A., Tanaka K., Sobue G. J. Biol. Chem. 279:51376-51385(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH VCP, MUTAGENESIS OF CYS-132 AND CYS-135, SUBCELLULAR LOCATION.
[10]	"Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin." Huang Y., Niwa J., Sobue G., Breitwieser G.E. J. Biol. Chem. 281:11610-11617(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH CASR AND VCP.
[11]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[12]	"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-631, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB029316 mRNA. Translation: BAB39353.1. BC093938 mRNA. Translation: AAH93938.1. BC093940 mRNA. Translation: AAH93940.1. AB271914 mRNA. Translation: BAF48117.1. AK001774 mRNA. Translation: BAA91900.1. AK023455 mRNA. Translation: BAB14581.1. Different initiation. AK027070 mRNA. Translation: BAB15647.1. Different initiation. AJ242975 mRNA. Translation: CAB45132.1. AL110253 mRNA. Translation: CAB53700.1. AL122096 mRNA. Translation: CAB59264.1.
IPI	IPI00019056. IPI00793570. IPI00869122.
PIR	T34528.
RefSeq	NP_056250.3. NM_015435.3. NP_904355.1. NM_183419.2.
UniGene	Hs.292882.
3D structure databases
ProteinModelPortal	Q9NV58.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NV58. 1 interaction.
STRING	9606.ENSP00000342667.
PTM databases
PhosphoSite	Q9NV58.
Polymorphism databases
DMDM	116242764.
Proteomic databases
PaxDb	Q9NV58.
PRIDE	Q9NV58.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341084; ENSP00000342667; ENSG00000034677. ENST00000517584; ENSP00000429161; ENSG00000034677. ENST00000519449; ENSP00000428968; ENSG00000034677.
GeneID	25897.
KEGG	hsa:25897.
UCSC	uc003yjj.1. human.
Organism-specific databases
CTD	25897.
GeneCards	GC08M101269.
HGNC	HGNC:13432. RNF19A.
HPA	CAB011455. HPA023652.
MIM	607119. gene.
neXtProt	NX_Q9NV58.
PharmGKB	PA162401601.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG245345.
HOVERGEN	HBG052073.
InParanoid	Q9NV58.
KO	K11972.
OMA	SNMKINE.
OrthoDB	EOG41JZBM.
PhylomeDB	Q9NV58.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q9NV58.
Bgee	Q9NV58.
CleanEx	HS_RNF19A.
Genevestigator	Q9NV58.
GermOnline	ENSG00000034677. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR002867. Znf_C6HC. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
Pfam	PF01485. IBR. 2 hits. [Graphical view]
SMART	SM00647. IBR. 2 hits. SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. False negative. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RNF19A. human.
GenomeRNAi	25897.
NextBio	47345.
SOURCE	Search...

Entry information

Entry name

RN19A_HUMAN

Accession

Primary (citable) accession number: Q9NV58
Secondary accession number(s): A3KCU9 , Q52LG1, Q9H5H9, Q9H8M8, Q9UFG0, Q9UFX6, Q9Y4Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2001
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 121 of the entry and version 3 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.