Skip Header

Contribute Send feedback
Read comments (?) or add your own

O75935 (DCTN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dynactin subunit 3
Alternative name(s):
Dynactin complex subunit 22 kDa subunit
Short name=p22
Gene names
Name:DCTN3
Synonyms:DCTN22
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length186 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Together with dynein may be involved in spindle assembly and cytokinesis. Ref.1

Subunit structure

Subunit of dynactin, a multiprotein complex associated with dynein.

Subcellular location

Cytoplasm. Cytoplasmcytoskeletoncentrosome. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle. Cleavage furrow. Midbody. Note: Localizes to punctate cytoplasmic structures and to the centrosome during interphase, and to kinetochores and to spindle poles throughout mitosis. Colocalizes with dynein to the cleavage furrow and to midbody of dividing cells. Ref.1

Tissue specificity

Ubiquitously expressed. Highly expressed in muscle and pancreas and detected at lower levels in brain. Ref.1

Sequence similarities

Belongs to the dynactin subunit 3 family.

Sequence caution

The sequence CAI13144.1 differs from that shown. Reason: Erroneous initiation.

The sequence CAI14178.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI14180.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PBX2P404251EBI-347442,EBI-348489

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: O75935-1)

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 Ref.4 (identifier: O75935-2)

The sequence of this isoform differs from the canonical sequence as follows:
     138-186: DQCVEITEES...AATQVKPAEE → APWGVGVRDE...GPTGPVCGNH
Note: No experimental confirmation available.
Isoform 3 (identifier: O75935-3)

The sequence of this isoform differs from the canonical sequence as follows:
     90-117: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 186185Dynactin subunit 3
PRO_0000225603

Regions

Coiled coil135 – 15723 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.7

Natural variations

Alternative sequence90 – 11728Missing in isoform 3.
VSP_051961
Alternative sequence138 – 18649DQCVE…KPAEE → APWGVGVRDEAGSLVEDVGF AQFLSVLHFGPTGPVCGNH in isoform 2. Ref.4
VSP_051964

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 70A0B26E24603A77

FASTA18621,119
        10         20         30         40         50         60 
MAGLTDLQRL QARVEELERW VYGPGGARGS RKVADGLVKV QVALGNISSK RERVKILYKK 

        70         80         90        100        110        120 
IEDLIKYLDP EYIDRIAIPD ASKLQFILAE EQFILSQVAL LEQVNALVPM LDSAHIKAVP 

       130        140        150        160        170        180 
EHAARLQRLA QIHIQQQDQC VEITEESKAL LEEYNKTTML LSKQFVQWDE LLCQLEAATQ 


VKPAEE 

« Hide

Isoform 2 [UniParc].

Checksum: FE50412C172E1922
Show »

FASTA17619,469
Isoform 3 [UniParc].

Checksum: 218ABF3564911AB1
Show »

FASTA15818,001

References

« Hide 'large scale' references
[1]"Characterization of the p22 subunit of dynactin reveals the localization of cytoplasmic dynein and dynactin to the midbody of dividing cells."
Karki S., LaMonte B., Holzbaur E.L.F.
J. Cell Biol. 142:1023-1034(1998) [PubMed: 9722614] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 20-28 AND 67-75, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Neuron.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , 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] (ISOFORM 1).
Tissue: Brain.
[4]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed: 15164053] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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. expand/collapse author list , 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].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Lung.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[8]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF082513 mRNA. Translation: AAC61280.1.
CR541889 mRNA. Translation: CAG46687.1.
AK314730 mRNA. Translation: BAG37272.1.
AL160270, AL450283 Genomic DNA. Translation: CAI13143.1.
AL160270, AL450283 Genomic DNA. Translation: CAI13144.1. Different initiation.
AL160270, AL450283 Genomic DNA. Translation: CAI13145.1.
AL450283 Genomic DNA. Translation: CAI14178.1. Sequence problems.
AL450283, AL160270 Genomic DNA. Translation: CAI14180.1. Different initiation.
AL450283, AL160270 Genomic DNA. Translation: CAI14181.1.
AL450283, AL160270 Genomic DNA. Translation: CAI14182.1.
CH471071 Genomic DNA. Translation: EAW58440.1.
CH471071 Genomic DNA. Translation: EAW58441.1.
BC000319 mRNA. Translation: AAH00319.1.
BC003004 mRNA. Translation: AAH03004.1.
BC107697 mRNA. Translation: AAI07698.1.
IPIIPI00013654.
IPI00027014.
IPI00514971.
RefSeqNP_009165.1. NM_007234.3.
NP_077324.1. NM_024348.2.
UniGeneHs.511768.

3D structure databases

ProteinModelPortalO75935.
ModBaseSearch...

Protein-protein interaction databases

IntActO75935. 8 interactions.
MINTMINT-1033946.
STRINGO75935.

PTM databases

PhosphoSiteO75935.

Proteomic databases

PRIDEO75935.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259632; ENSP00000259632; ENSG00000137100.
GeneID11258.
KEGGhsa:11258.
UCSCuc003zuw.1. human.
uc003zux.1. human.

Organism-specific databases

CTD11258.
GeneCardsGC09M034569.
H-InvDBHIX0007999.
HGNCHGNC:2713. DCTN3.
HPAHPA044905.
MIM607387. gene.
neXtProtNX_O75935.
PharmGKBPA27182.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18454.
GeneTreeENSGT00390000016210.
HOGENOMHBG716675.
HOVERGENHBG053181.
InParanoidO75935.
OMAQCMEITE.
OrthoDBEOG4J9N11.
PhylomeDBO75935.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.

Gene expression databases

ArrayExpressO75935.
BgeeO75935.
CleanExHS_DCTN3.
GenevestigatorO75935.
GermOnlineENSG00000137100. Homo sapiens.

Family and domain databases

InterProIPR009991. Dynactin_p22.
[Graphical view]
KOK10425.
PfamPF07426. Dynactin_p22. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio42838.
SOURCESearch...

Entry information

Entry nameDCTN3_HUMAN
AccessionPrimary (citable) accession number: O75935
Secondary accession number(s): A6NII7 expand/collapse secondary AC list , B2RBM5, Q5T1I5, Q5T1I7, Q5T8G3, Q9BPU8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: November 1, 1998
Last modified: January 25, 2012
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families