Q13561 (DCTN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dynactin subunit 2

Alternative name(s):
50 kDa dynein-associated polypeptide
Dynactin complex 50 kDa subunit
Short name=DCTN-50
p50 dynamitin

Gene names

Name:	DCTN2
Synonyms:	DCTN50

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	401 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Modulates cytoplasmic dynein binding to an organelle, and plays a role in prometaphase chromosome alignment and spindle organization during mitosis. Involved in anchoring microtubules to centrosomes. May play a role in synapse formation during brain development.
Subunit structure	Subunit of dynactin, a multiprotein complex associated with dynein. Interacts with BICD2 and CEP135 By similarity. Interacts with DYNAP, ECM29 and MAPRE1. Ref.9 Ref.13 Ref.14
Subcellular location	Cytoplasm › cytoskeleton › centrosome. Membrane; Peripheral membrane protein Ref.1.
Sequence similarities	Belongs to the dynactin subunit 2 family.
Sequence caution	The sequence AAO34395.1 differs from that shown. Reason: Frameshift at position 381.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Dynein Membrane Microtubule
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome cell proliferation Inferred from mutant phenotype Ref.1. Source: UniProtKB mitosis Inferred from mutant phenotype Ref.1. Source: UniProtKB mitotic spindle organization Inferred from electronic annotation. Source: Compara
Cellular_component	centrosome Inferred from direct assay PubMed 21399614Ref.1. Source: UniProtKB cytosol Traceable author statement. Source: Reactome dynactin complex Inferred from direct assay Ref.1. Source: UniProtKB dynein complex Inferred from electronic annotation. Source: UniProtKB-KW growth cone Inferred from electronic annotation. Source: Compara kinetochore Inferred from direct assay Ref.1. Source: UniProtKB membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW vesicle Inferred from direct assay Ref.13. Source: UniProtKB
Molecular_function	motor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DISC1	Q9NRI5	3	EBI-715074,EBI-529989

Alternative products

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

Isoform 1 (identifier: Q13561-1)

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: Q13561-2)

The sequence of this isoform differs from the canonical sequence as follows:
     35-35: A → AFAQEL

Isoform 3 (identifier: Q13561-3)

The sequence of this isoform differs from the canonical sequence as follows:
     35-35: A → AEL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.6 Ref.7
	Chain	2 – 401	400	Dynactin subunit 2		PRO_0000079821
Regions
	Coiled coil	99 – 132	34	Potential
	Coiled coil	214 – 244	31	Potential
	Coiled coil	379 – 399	21	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
	Modified residue	6	1	Phosphotyrosine Ref.10
	Modified residue	83	1	Phosphoserine Ref.12
	Modified residue	86	1	Phosphotyrosine By similarity
Natural variations
	Alternative sequence	35	1	A → AFAQEL in isoform 2.		VSP_040485
	Alternative sequence	35	1	A → AEL in isoform 3.		VSP_040486

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: C2FF01A9739337B2	FASTA	401	44,231
	10 20 30 40 50 60 MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELTS TSVEHIIVNP NAAYDKFKDK 70 80 90 100 110 120 RVGTKGLDFS DRIGKTKRTG YESGEYEMLG EGLGVKETPQ QKYQRLLHEV QELTTEVEKI 130 140 150 160 170 180 KTTVKESATE EKLTPVLLAK QLAALKQQLV ASHLEKLLGP DAAINLTDPD GALAKRLLLQ 190 200 210 220 230 240 LEATKNSKGG SGGKTTGTPP DSSLVTYELH SRPEQDKFSQ AAKVAELEKR LTELETAVRC 250 260 270 280 290 300 DQDAQNPLSA GLQGACLMET VELLQAKVSA LDLAVLDQVE ARLQSVLGKV NEIAKHKASV 310 320 330 340 350 360 EDADTQSKVH QLYETIQRWS PIASTLPELV QRLVTIKQLH EQAMQFGQLL THLDTTQQMI 370 380 390 400 ANSLKDNTTL LTQVQTTMRE NLATVEGNFA SIDERMKKLG K
	Isoform 2 [UniParc]. Checksum: 1166997A6D07479D	FASTA	406	44,820
	10 20 30 40 50 60 MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAFAQEL EELTSTSVEH IIVNPNAAYD 70 80 90 100 110 120 KFKDKRVGTK GLDFSDRIGK TKRTGYESGE YEMLGEGLGV KETPQQKYQR LLHEVQELTT 130 140 150 160 170 180 EVEKIKTTVK ESATEEKLTP VLLAKQLAAL KQQLVASHLE KLLGPDAAIN LTDPDGALAK 190 200 210 220 230 240 RLLLQLEATK NSKGGSGGKT TGTPPDSSLV TYELHSRPEQ DKFSQAAKVA ELEKRLTELE 250 260 270 280 290 300 TAVRCDQDAQ NPLSAGLQGA CLMETVELLQ AKVSALDLAV LDQVEARLQS VLGKVNEIAK 310 320 330 340 350 360 HKASVEDADT QSKVHQLYET IQRWSPIAST LPELVQRLVT IKQLHEQAMQ FGQLLTHLDT 370 380 390 400 TQQMIANSLK DNTTLLTQVQ TTMRENLATV EGNFASIDER MKKLGK
	Isoform 3 [UniParc]. Checksum: 864FD68AF5433E22	FASTA	403	44,473
	10 20 30 40 50 60 MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAELEEL TSTSVEHIIV NPNAAYDKFK 70 80 90 100 110 120 DKRVGTKGLD FSDRIGKTKR TGYESGEYEM LGEGLGVKET PQQKYQRLLH EVQELTTEVE 130 140 150 160 170 180 KIKTTVKESA TEEKLTPVLL AKQLAALKQQ LVASHLEKLL GPDAAINLTD PDGALAKRLL 190 200 210 220 230 240 LQLEATKNSK GGSGGKTTGT PPDSSLVTYE LHSRPEQDKF SQAAKVAELE KRLTELETAV 250 260 270 280 290 300 RCDQDAQNPL SAGLQGACLM ETVELLQAKV SALDLAVLDQ VEARLQSVLG KVNEIAKHKA 310 320 330 340 350 360 SVEDADTQSK VHQLYETIQR WSPIASTLPE LVQRLVTIKQ LHEQAMQFGQ LLTHLDTTQQ 370 380 390 400 MIANSLKDNT TLLTQVQTTM RENLATVEGN FASIDERMKK LGK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis." Echeverri C.J., Paschal B.M., Vaughan K.T., Vallee R.B. J. Cell Biol. 132:617-633(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION.
[2]	"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] (ISOFORM 2).
[3]	"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].
[4]	"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: Placenta, Skin and Uterus.
[5]	"Human 50 kD dynactin subunit, p50 dynamitin, isolated from HeLa cells." Aumais J.P., Yu-Lee L.-Y. Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-385 (ISOFORM 3).
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14. Tissue: Platelet.
[7]	Bienvenut W.V., Ramsay A., Leung H.Y. Submitted (FEB-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 6-14; 79-96; 106-119; 157-185; 231-282 AND 366-395, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[9]	"The APC-associated protein EB1 associates with components of the dynactin complex and cytoplasmic dynein intermediate chain." Berrueta L., Tirnauer J.S., Schuyler S.C., Pellman D., Bierer B.E. Curr. Biol. 9:425-428(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAPRE1.
[10]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"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.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components." Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M. J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ECM29.
[14]	"A novel human dynactin-associated protein, dynAP, promotes activation of Akt, and ergosterol-related compounds induce dynAP-dependent apoptosis of human cancer cells." Kunoh T., Noda T., Koseki K., Sekigawa M., Takagi M., Shin-ya K., Goshima N., Iemura S., Natsume T., Wada S., Mukai Y., Ohta S., Sasaki R., Mizukami T. Mol. Cancer Ther. 9:2934-2942(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DYNAP.
[15]	"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.
[16]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U50733 mRNA. Translation: AAC50423.1. AK314705 mRNA. Translation: BAG37252.1. AC022366 Genomic DNA. No translation available. AC022506 Genomic DNA. No translation available. BC000718 mRNA. Translation: AAH00718.1. BC009468 mRNA. Translation: AAH09468.1. BC014083 mRNA. Translation: AAH14083.1. AY189155 mRNA. Translation: AAO34395.1. Frameshift.
IPI	IPI00220503. IPI00973457. IPI00973500.
RefSeq	NP_001248341.1. NM_001261412.1. NP_001248342.1. NM_001261413.1. NP_006391.1. NM_006400.4.
UniGene	Hs.289123.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13561. 10 interactions.
MINT	MINT-206219.
STRING	9606.ENSP00000408910.
PTM databases
PhosphoSite	Q13561.
Polymorphism databases
DMDM	22096346.
2D gel databases
REPRODUCTION-2DPAGE	IPI00220503.
Proteomic databases
PaxDb	Q13561.
PRIDE	Q13561.
Protocols and materials databases
DNASU	10540.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000434715; ENSP00000408910; ENSG00000175203. ENST00000548249; ENSP00000447824; ENSG00000175203.
GeneID	10540.
KEGG	hsa:10540.
UCSC	uc001som.1. human. uc009zpv.1. human.
Organism-specific databases
CTD	10540.
GeneCards	GC12M057924.
H-InvDB	HIX0010763.
HGNC	HGNC:2712. DCTN2.
HPA	HPA039715. HPA040040.
MIM	607376. gene.
neXtProt	NX_Q13561.
PharmGKB	PA27181.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG39555.
HOVERGEN	HBG051323.
InParanoid	Q13561.
KO	K10424.
OMA	SGEYEML.
OrthoDB	EOG4CC41M.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_6900. Immune System.
SignaLink	Q13561.
Gene expression databases
ArrayExpress	Q13561.
Bgee	Q13561.
CleanEx	HS_DCTN2.
Genevestigator	Q13561.
GermOnline	ENSG00000175203. Homo sapiens.
Family and domain databases
InterPro	IPR006996. Dynamitin_2su. [Graphical view]
PANTHER	PTHR15346:SF0. PTHR15346:SF0. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	DCTN2. human.
GenomeRNAi	10540.
NextBio	39989.
PMAP-CutDB	Q13561.
SOURCE	Search...

Entry information

Entry name

DCTN2_HUMAN

Accession

Primary (citable) accession number: Q13561
Secondary accession number(s): B2RBK5, Q86YN2, Q9BW17

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 130 of the entry and version 4 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.