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O14576 (DC1I1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Cytoplasmic dynein 1 intermediate chain 1
Alternative name(s):
Cytoplasmic dynein intermediate chain 1
Dynein intermediate chain 1, cytosolic
Short name=DH IC-1
Gene names
Name:DYNC1I1
Synonyms:DNCI1, DNCIC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCNT1. May play a role in mediating the interaction of cytoplasmic dynein with membranous organelles and kinetochores.

Subunit structure

Homodimer By similarity. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with DYNC1H1. Interacts with DYNLT1 and DYNLT3. Interacts with DCNT1 By similarity.

Subcellular location

Cytoplasm By similarity. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle pole Ref.7.

Sequence similarities

Belongs to the dynein intermediate chain family.

Contains 7 WD repeats.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Dynein
Kinetochore
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
WD repeat
   Molecular functionMotor protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

metabolic process

Inferred from sequence or structural similarity. Source: GOC

vesicle transport along microtubule

Inferred from sequence or structural similarity. Source: HGNC

   Cellular_componentcondensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic dynein complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

kinetochore

Inferred from direct assay Ref.7. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: HGNC

spindle pole

Inferred from direct assay Ref.7. Source: UniProtKB

vesicle

Inferred from direct assay PubMed 20682791. Source: UniProtKB

   Molecular_functionmicrotubule binding

Inferred from sequence or structural similarity. Source: HGNC

microtubule motor activity

Inferred from sequence or structural similarity. Source: HGNC

motor activity

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 19927128. Source: IntAct

spectrin binding

Inferred from direct assay PubMed 23704327. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Nde1Q9CZA62EBI-366267,EBI-309934From a different organism.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14576-1)

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: O14576-2)

The sequence of this isoform differs from the canonical sequence as follows:
     74-90: Missing.
Isoform 3 (identifier: O14576-3)

The sequence of this isoform differs from the canonical sequence as follows:
     74-90: Missing.
     123-142: Missing.
Isoform 4 (identifier: O14576-4)

The sequence of this isoform differs from the canonical sequence as follows:
     74-90: Missing.
     123-142: Missing.
     610-645: LAVPHNDEWTRFARTLVEIRANRADSEEEGTVELSA → GLAMLPGWSQNSWTQAILLCWPPKVLGLQT
Note: No experimental confirmation available.
Isoform 5 (identifier: O14576-5)

The sequence of this isoform differs from the canonical sequence as follows:
     123-142: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 645645Cytoplasmic dynein 1 intermediate chain 1
PRO_0000114652

Regions

Repeat285 – 33450WD 1
Repeat338 – 37841WD 2
Repeat387 – 42842WD 3
Repeat437 – 47741WD 4
Repeat482 – 52746WD 5
Repeat530 – 57041WD 6
Repeat576 – 61540WD 7
Region1 – 123123Interaction with DCTN1 By similarity

Amino acid modifications

Modified residue6351Phosphoserine Ref.8

Natural variations

Alternative sequence74 – 9017Missing in isoform 2, isoform 3 and isoform 4.
VSP_001332
Alternative sequence123 – 14220Missing in isoform 3, isoform 4 and isoform 5.
VSP_001333
Alternative sequence610 – 64536LAVPH…VELSA → GLAMLPGWSQNSWTQAILLC WPPKVLGLQT in isoform 4.
VSP_054766
Natural variant3731H → L Found in a renal cell carcinoma case; somatic mutation. Ref.9
VAR_064709
Natural variant5821N → T.
Corresponds to variant rs35077523 [ dbSNP | Ensembl ].
VAR_048905

Experimental info

Sequence conflict2541D → G in BAG59855. Ref.3
Sequence conflict5171W → C in AAH22540. Ref.6

Sequences

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

Last modified May 1, 1999. Version 2.
Checksum: 55A6FF971E632DA0

FASTA64572,955
        10         20         30         40         50         60 
MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKEADMQ QKKEPVQDDS DLDRKRRETE 

        70         80         90        100        110        120 
ALLQSIGISP EPPLVQPLHF LTWDTCYFHY LVPTPMSPSS KSVSTPSEAG SQDSGDLGPL 

       130        140        150        160        170        180 
TRTLQWDTDP SVLQLQSDSE LGRRLHKLGV SKVTQVDFLP REVVSYSKET QTPLATHQSE 

       190        200        210        220        230        240 
EDEEDEEMVE SKVGQDSELE NQDKKQEVKE APPRELTEEE KQQILHSEEF LIFFDRTIRV 

       250        260        270        280        290        300 
IERALAEDSD IFFDYSGREL EEKDGDVQAG ANLSFNRQFY DEHWSKHRVV TCMDWSLQYP 

       310        320        330        340        350        360 
ELMVASYNNN EDAPHEPDGV ALVWNMKFKK TTPEYVFHCQ SSVMSVCFAR FHPNLVVGGT 

       370        380        390        400        410        420 
YSGQIVLWDN RSHRRTPVQR TPLSAAAHTH PVYCVNVVGT QNAHNLITVS TDGKMCSWSL 

       430        440        450        460        470        480 
DMLSTPQESM ELVYNKSKPV AVTGMAFPTG DVNNFVVGSE EGTVYTACRH GSKAGIGEVF 

       490        500        510        520        530        540 
EGHQGPVTGI NCHMAVGPID FSHLFVTSSF DWTVKLWTTK HNKPLYSFED NADYVYDVMW 

       550        560        570        580        590        600 
SPVHPALFAC VDGMGRLDLW NLNNDTEVPT ASVAIEGASA LNRVRWAQAG KEVAVGDSEG 

       610        620        630        640 
RIWVYDVGEL AVPHNDEWTR FARTLVEIRA NRADSEEEGT VELSA 

« Hide

Isoform 2 [UniParc].

Checksum: 0360B15D5295971F
Show »

FASTA62870,790
Isoform 3 [UniParc].

Checksum: D88D3EB3D1FC82B2
Show »

FASTA60868,575
Isoform 4 [UniParc].

Checksum: C72E232C21BED944
Show »

FASTA60267,802
Isoform 5 [UniParc].

Checksum: E9675FAE856C56F1
Show »

FASTA62570,741

References

« Hide 'large scale' references
[1]"Cloning and characterization of two cytoplasmic dynein intermediate chain genes in mouse and human."
Crackower M.A., Sinasac D.S., Xia J., Motoyama J., Prochazka M., Rommens J.M., Scherer S.W., Tsui L.-C.
Genomics 55:257-267(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular cloning of a cytoplasmic dynein gene."
Li G., Jin J., Hu S., Li W., Yuan J., Qiang B.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
Tissue: Brain.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Brain.
[7]"Dynein light intermediate chain 1 is required for progress through the spindle assembly checkpoint."
Sivaram M.V., Wadzinski T.L., Redick S.D., Manna T., Doxsey S.J.
EMBO J. 28:902-914(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"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-635, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[9]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LEU-373.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF063228 mRNA. Translation: AAC33443.1.
AF123074 mRNA. Translation: AAD26852.1.
AK091339 mRNA. Translation: BAC03639.1.
AK297427 mRNA. Translation: BAG59855.1.
AC022261 Genomic DNA. No translation available.
AC091779 Genomic DNA. No translation available.
AC002452 Genomic DNA. Translation: AAB67047.2.
AC002540 Genomic DNA. Translation: AAB70113.1.
CH471091 Genomic DNA. Translation: EAW76753.1.
BC022540 mRNA. Translation: AAH22540.1.
CCDSCCDS47645.1. [O14576-2]
CCDS47646.1. [O14576-3]
CCDS5644.1. [O14576-1]
RefSeqNP_001129028.1. NM_001135556.1. [O14576-2]
NP_001129029.1. NM_001135557.1. [O14576-3]
NP_001265350.1. NM_001278421.1. [O14576-5]
NP_001265351.1. NM_001278422.1. [O14576-4]
NP_004402.1. NM_004411.4. [O14576-1]
UniGeneHs.440364.

3D structure databases

DisProtDP00360.
ProteinModelPortalO14576.
SMRO14576. Positions 147-174, 341-566.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108118. 38 interactions.
IntActO14576. 34 interactions.
MINTMINT-156403.
STRING9606.ENSP00000320130.

PTM databases

PhosphoSiteO14576.

Proteomic databases

MaxQBO14576.
PaxDbO14576.
PRIDEO14576.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324972; ENSP00000320130; ENSG00000158560. [O14576-1]
ENST00000359388; ENSP00000352348; ENSG00000158560. [O14576-3]
ENST00000437599; ENSP00000398118; ENSG00000158560.
ENST00000447467; ENSP00000392337; ENSG00000158560. [O14576-2]
ENST00000457059; ENSP00000412444; ENSG00000158560. [O14576-2]
ENST00000537881; ENSP00000438377; ENSG00000158560.
GeneID1780.
KEGGhsa:1780.
UCSCuc003uob.3. human. [O14576-3]
uc003uoc.4. human. [O14576-1]
uc003uod.4. human. [O14576-2]

Organism-specific databases

CTD1780.
GeneCardsGC07P095401.
HGNCHGNC:2963. DYNC1I1.
HPAHPA021315.
MIM603772. gene.
neXtProtNX_O14576.
PharmGKBPA27434.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG308180.
HOGENOMHOG000116383.
HOVERGENHBG004083.
InParanoidO14576.
KOK10415.
OMAKVGHDSE.
OrthoDBEOG7FR7FX.
PhylomeDBO14576.
TreeFamTF300553.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkO14576.

Gene expression databases

ArrayExpressO14576.
BgeeO14576.
CleanExHS_DYNC1I1.
GenevestigatorO14576.

Family and domain databases

Gene3D2.130.10.10. 1 hit.
InterProIPR025956. Dynein_IC_1/2.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamPF11540. Dynein_IC2. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTSM00320. WD40. 5 hits.
[Graphical view]
SUPFAMSSF50978. SSF50978. 1 hit.
PROSITEPS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDYNC1I1.
GenomeRNAi1780.
NextBio35473300.
PROO14576.
SOURCESearch...

Entry information

Entry nameDC1I1_HUMAN
AccessionPrimary (citable) accession number: O14576
Secondary accession number(s): B4DME3 expand/collapse secondary AC list , F5H050, G5E9K1, Q8TBF7, Q9Y2X1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 130 of the entry and version 2 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM