Reviewed, UniProtKB/Swiss-Prot Q13561 (DCTN2_HUMAN)

Names and origin

Protein names

Recommended name:
    Dynactin subunit 2
Alternative name(s):
    Dynactin complex 50 kDa subunit
      Short name=DCTN-50
    50 kDa dynein-associated polypeptide
    p50 dynamitin

Gene names

Name:	DCTN2
Synonyms:	DCTN50

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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. May play a role in synapse formation during brain development.
Subunit structure	Subunit of dynactin, a multiprotein complex associated with dynein. Interacts with BICD2 By similarity. Interacts with MAPRE1.
Subcellular location	Cytoplasm › cytoskeleton. Membrane; Peripheral membrane protein.
Sequence similarities	Belongs to the dynactin subunit 2 family.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Dynein Membrane Microtubule
Domain	Coiled coil
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell proliferation Ref.1 Inferred from mutant phenotype. Source: UniProtKB microtubule-based process Inferred from electronic annotation. Source: InterPro mitosis Ref.1 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	centrosome Ref.1 Inferred from direct assay. Source: UniProtKB dynactin complex Ref.1 Inferred from direct assay. Source: UniProtKB dynein complex Inferred from electronic annotation. Source: UniProtKB-KW kinetochore Ref.1 Inferred from direct assay. Source: UniProtKB membrane Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	motor activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.7 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DISC1	Q9NRI5	2	EBI-715074,EBI-529989

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4 Ref.5
	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.5
	Modified residue	83	1	Phosphoserine By similarity
	Modified residue	86	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	35	1	A → AFAQEL in AAC50423. Ref.1
	Sequence conflict	36	1	E → ELE Ref.3
	Sequence conflict	382 – 385	4	LATV → PGHS Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q13561-1 [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

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: 8647893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta, Skin and Uterus.
[3]	"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.
[4]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14. Tissue: Platelet.
[5]	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.
[6]	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.
[7]	"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: 10226031] [Abstract] Cited for: INTERACTION WITH MAPRE1.
[8]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U50733 mRNA. Translation: AAC50423.1. BC000718 mRNA. Translation: AAH00718.1. BC009468 mRNA. Translation: AAH09468.1. BC014083 mRNA. Translation: AAH14083.1. AY189155 mRNA. Translation: AAO34395.1.
IPI	IPI00220503.
RefSeq	NP_006391.1.
UniGene	Hs.151219 Hs.289123
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13561. 5 interactions.
PTM databases
PhosphoSite	Q13561.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00220503.
Proteomic databases
PRIDE	Q13561.
Genome annotation databases
Ensembl	ENSG00000175203. Homo sapiens. [Contig view]
GeneID	10540.
KEGG	hsa:10540.
UCSC	uc001som.1. human.
Organism-specific databases
GeneCards	GC12M056210.
HGNC	HGNC:2712. DCTN2.
MIM	607376. gene.
PharmGKB	PA27181.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q13561.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic.
Gene expression databases
Bgee	Q13561.
CleanEx	HS_DCTN2.
GermOnline	ENSG00000175203. Homo sapiens.
Family and domain databases
InterPro	IPR006996. Dynamitin. [Graphical view]
Pfam	PF04912. Dynamitin. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	39989.
PMAP-CutDB	Q13561.
SOURCE	Search...

Entry information

Entry name

DCTN2_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	July 7, 2009
This is version 86 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)