Full text data of DYNC1I1
DYNC1I1
(DNCI1, DNCIC1)
[Confidence: low (only semi-automatic identification from reviews)]
Cytoplasmic dynein 1 intermediate chain 1 (Cytoplasmic dynein intermediate chain 1; Dynein intermediate chain 1, cytosolic; DH IC-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Cytoplasmic dynein 1 intermediate chain 1 (Cytoplasmic dynein intermediate chain 1; Dynein intermediate chain 1, cytosolic; DH IC-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O14576
ID DC1I1_HUMAN Reviewed; 645 AA.
AC O14576; Q9Y2X1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 2.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 1;
DE AltName: Full=Cytoplasmic dynein intermediate chain 1;
DE AltName: Full=Dynein intermediate chain 1, cytosolic;
DE Short=DH IC-1;
GN Name=DYNC1I1; Synonyms=DNCI1, DNCIC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10049579; DOI=10.1006/geno.1998.5665;
RA Crackower M.A., Sinasac D.S., Xia J., Motoyama J., Prochazka M.,
RA Rommens J.M., Scherer S.W., Tsui L.-C.;
RT "Cloning and characterization of two cytoplasmic dynein intermediate
RT chain genes in mouse and human.";
RL Genomics 55:257-267(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Li G., Jin J., Hu S., Li W., Yuan J., Qiang B.;
RT "Molecular cloning of a cytoplasmic dynein gene.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=19229290; DOI=10.1038/emboj.2009.38;
RA Sivaram M.V., Wadzinski T.L., Redick S.D., Manna T., Doxsey S.J.;
RT "Dynein light intermediate chain 1 is required for progress through
RT the spindle assembly checkpoint.";
RL EMBO J. 28:902-914(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP VARIANT LEU-373.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
RA Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT gene PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory
CC components of the cytoplasmic dynein 1 complex that are thought to
CC be involved in linking dynein to cargos and to adapter proteins
CC that regulate dynein function. Cytoplasmic dynein 1 acts as a
CC motor for the intracellular retrograde motility of vesicles and
CC organelles along microtubules. The intermediate chains mediate the
CC binding of dynein to dynactin via its 150 kDa component (p150-
CC glued) DCNT1. May play a role in mediating the interaction of
CC cytoplasmic dynein with membranous organelles and kinetochores.
CC -!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1
CC complex consists of two catalytic heavy chains (HCs) and a number
CC of non-catalytic subunits presented by intermediate chains (ICs),
CC light intermediate chains (LICs) and light chains (LCs); the
CC composition seems to vary in respect to the IC, LIC and LC
CC composition. The heavy chain homodimer serves as a scaffold for
CC the probable homodimeric assembly of the respective non-catalytic
CC subunits. The ICs and LICs bind directly to the HC dimer and the
CC LCs assemble on the IC dimer. Interacts with DYNC1H1. Interacts
CC with DYNLT1 and DYNLT3. Interacts with DCNT1 (By similarity).
CC -!- INTERACTION:
CC Q9CZA6:Nde1 (xeno); NbExp=2; IntAct=EBI-366267, EBI-309934;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Chromosome,
CC centromere, kinetochore. Cytoplasm, cytoskeleton, spindle pole.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O14576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14576-2; Sequence=VSP_001332;
CC Name=3;
CC IsoId=O14576-3; Sequence=VSP_001332, VSP_001333;
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC -!- SIMILARITY: Contains 7 WD repeats.
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DR EMBL; AF063228; AAC33443.1; -; mRNA.
DR EMBL; AF123074; AAD26852.1; -; mRNA.
DR EMBL; AK091339; BAC03639.1; -; mRNA.
DR EMBL; AC022261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002452; AAB67047.2; -; Genomic_DNA.
DR EMBL; AC002540; AAB70113.1; -; Genomic_DNA.
DR RefSeq; NP_001129028.1; NM_001135556.1.
DR RefSeq; NP_001129029.1; NM_001135557.1.
DR RefSeq; NP_004402.1; NM_004411.4.
DR UniGene; Hs.440364; -.
DR DisProt; DP00360; -.
DR ProteinModelPortal; O14576; -.
DR SMR; O14576; 147-173, 341-566.
DR IntAct; O14576; 34.
DR MINT; MINT-156403; -.
DR STRING; 9606.ENSP00000320130; -.
DR PhosphoSite; O14576; -.
DR PaxDb; O14576; -.
DR PRIDE; O14576; -.
DR Ensembl; ENST00000324972; ENSP00000320130; ENSG00000158560.
DR Ensembl; ENST00000359388; ENSP00000352348; ENSG00000158560.
DR Ensembl; ENST00000447467; ENSP00000392337; ENSG00000158560.
DR Ensembl; ENST00000457059; ENSP00000412444; ENSG00000158560.
DR GeneID; 1780; -.
DR KEGG; hsa:1780; -.
DR UCSC; uc003uoc.4; human.
DR CTD; 1780; -.
DR GeneCards; GC07P095401; -.
DR HGNC; HGNC:2963; DYNC1I1.
DR HPA; HPA021315; -.
DR MIM; 603772; gene.
DR neXtProt; NX_O14576; -.
DR PharmGKB; PA27434; -.
DR eggNOG; NOG308180; -.
DR HOGENOM; HOG000116383; -.
DR HOVERGEN; HBG004083; -.
DR InParanoid; O14576; -.
DR KO; K10415; -.
DR OMA; KVGHDSE; -.
DR PhylomeDB; O14576; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; O14576; -.
DR GeneWiki; DYNC1I1; -.
DR GenomeRNAi; 1780; -.
DR NextBio; 7243; -.
DR PRO; PR:O14576; -.
DR ArrayExpress; O14576; -.
DR Bgee; O14576; -.
DR CleanEx; HS_DYNC1I1; -.
DR Genevestigator; O14576; -.
DR GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:HGNC.
DR GO; GO:0003777; F:microtubule motor activity; ISS:HGNC.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:HGNC.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR025956; Dynein_IC_1/2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF11540; Dynein_IC2; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Centromere; Chromosome; Complete proteome;
KW Cytoplasm; Cytoskeleton; Dynein; Kinetochore; Microtubule;
KW Motor protein; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat; Transport; WD repeat.
FT CHAIN 1 645 Cytoplasmic dynein 1 intermediate chain
FT 1.
FT /FTId=PRO_0000114652.
FT REPEAT 285 334 WD 1.
FT REPEAT 338 378 WD 2.
FT REPEAT 387 428 WD 3.
FT REPEAT 437 477 WD 4.
FT REPEAT 482 527 WD 5.
FT REPEAT 530 570 WD 6.
FT REPEAT 576 615 WD 7.
FT REGION 1 123 Interaction with DCTN1 (By similarity).
FT MOD_RES 635 635 Phosphoserine.
FT VAR_SEQ 74 90 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_001332.
FT VAR_SEQ 123 142 Missing (in isoform 3).
FT /FTId=VSP_001333.
FT VARIANT 373 373 H -> L (found in a renal cell carcinoma
FT case; somatic mutation).
FT /FTId=VAR_064709.
FT VARIANT 582 582 N -> T (in dbSNP:rs35077523).
FT /FTId=VAR_048905.
SQ SEQUENCE 645 AA; 72955 MW; 55A6FF971E632DA0 CRC64;
MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKEADMQ QKKEPVQDDS DLDRKRRETE
ALLQSIGISP EPPLVQPLHF LTWDTCYFHY LVPTPMSPSS KSVSTPSEAG SQDSGDLGPL
TRTLQWDTDP SVLQLQSDSE LGRRLHKLGV SKVTQVDFLP REVVSYSKET QTPLATHQSE
EDEEDEEMVE SKVGQDSELE NQDKKQEVKE APPRELTEEE KQQILHSEEF LIFFDRTIRV
IERALAEDSD IFFDYSGREL EEKDGDVQAG ANLSFNRQFY DEHWSKHRVV TCMDWSLQYP
ELMVASYNNN EDAPHEPDGV ALVWNMKFKK TTPEYVFHCQ SSVMSVCFAR FHPNLVVGGT
YSGQIVLWDN RSHRRTPVQR TPLSAAAHTH PVYCVNVVGT QNAHNLITVS TDGKMCSWSL
DMLSTPQESM ELVYNKSKPV AVTGMAFPTG DVNNFVVGSE EGTVYTACRH GSKAGIGEVF
EGHQGPVTGI NCHMAVGPID FSHLFVTSSF DWTVKLWTTK HNKPLYSFED NADYVYDVMW
SPVHPALFAC VDGMGRLDLW NLNNDTEVPT ASVAIEGASA LNRVRWAQAG KEVAVGDSEG
RIWVYDVGEL AVPHNDEWTR FARTLVEIRA NRADSEEEGT VELSA
//
ID DC1I1_HUMAN Reviewed; 645 AA.
AC O14576; Q9Y2X1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-MAY-1999, sequence version 2.
DT 22-JAN-2014, entry version 124.
DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 1;
DE AltName: Full=Cytoplasmic dynein intermediate chain 1;
DE AltName: Full=Dynein intermediate chain 1, cytosolic;
DE Short=DH IC-1;
GN Name=DYNC1I1; Synonyms=DNCI1, DNCIC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10049579; DOI=10.1006/geno.1998.5665;
RA Crackower M.A., Sinasac D.S., Xia J., Motoyama J., Prochazka M.,
RA Rommens J.M., Scherer S.W., Tsui L.-C.;
RT "Cloning and characterization of two cytoplasmic dynein intermediate
RT chain genes in mouse and human.";
RL Genomics 55:257-267(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Li G., Jin J., Hu S., Li W., Yuan J., Qiang B.;
RT "Molecular cloning of a cytoplasmic dynein gene.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=19229290; DOI=10.1038/emboj.2009.38;
RA Sivaram M.V., Wadzinski T.L., Redick S.D., Manna T., Doxsey S.J.;
RT "Dynein light intermediate chain 1 is required for progress through
RT the spindle assembly checkpoint.";
RL EMBO J. 28:902-914(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP VARIANT LEU-373.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
RA Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
RA Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
RA Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
RA Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
RA Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
RA Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
RA Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
RA Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex
RT gene PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory
CC components of the cytoplasmic dynein 1 complex that are thought to
CC be involved in linking dynein to cargos and to adapter proteins
CC that regulate dynein function. Cytoplasmic dynein 1 acts as a
CC motor for the intracellular retrograde motility of vesicles and
CC organelles along microtubules. The intermediate chains mediate the
CC binding of dynein to dynactin via its 150 kDa component (p150-
CC glued) DCNT1. May play a role in mediating the interaction of
CC cytoplasmic dynein with membranous organelles and kinetochores.
CC -!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1
CC complex consists of two catalytic heavy chains (HCs) and a number
CC of non-catalytic subunits presented by intermediate chains (ICs),
CC light intermediate chains (LICs) and light chains (LCs); the
CC composition seems to vary in respect to the IC, LIC and LC
CC composition. The heavy chain homodimer serves as a scaffold for
CC the probable homodimeric assembly of the respective non-catalytic
CC subunits. The ICs and LICs bind directly to the HC dimer and the
CC LCs assemble on the IC dimer. Interacts with DYNC1H1. Interacts
CC with DYNLT1 and DYNLT3. Interacts with DCNT1 (By similarity).
CC -!- INTERACTION:
CC Q9CZA6:Nde1 (xeno); NbExp=2; IntAct=EBI-366267, EBI-309934;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Chromosome,
CC centromere, kinetochore. Cytoplasm, cytoskeleton, spindle pole.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O14576-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O14576-2; Sequence=VSP_001332;
CC Name=3;
CC IsoId=O14576-3; Sequence=VSP_001332, VSP_001333;
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC -!- SIMILARITY: Contains 7 WD repeats.
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DR EMBL; AF063228; AAC33443.1; -; mRNA.
DR EMBL; AF123074; AAD26852.1; -; mRNA.
DR EMBL; AK091339; BAC03639.1; -; mRNA.
DR EMBL; AC022261; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002452; AAB67047.2; -; Genomic_DNA.
DR EMBL; AC002540; AAB70113.1; -; Genomic_DNA.
DR RefSeq; NP_001129028.1; NM_001135556.1.
DR RefSeq; NP_001129029.1; NM_001135557.1.
DR RefSeq; NP_004402.1; NM_004411.4.
DR UniGene; Hs.440364; -.
DR DisProt; DP00360; -.
DR ProteinModelPortal; O14576; -.
DR SMR; O14576; 147-173, 341-566.
DR IntAct; O14576; 34.
DR MINT; MINT-156403; -.
DR STRING; 9606.ENSP00000320130; -.
DR PhosphoSite; O14576; -.
DR PaxDb; O14576; -.
DR PRIDE; O14576; -.
DR Ensembl; ENST00000324972; ENSP00000320130; ENSG00000158560.
DR Ensembl; ENST00000359388; ENSP00000352348; ENSG00000158560.
DR Ensembl; ENST00000447467; ENSP00000392337; ENSG00000158560.
DR Ensembl; ENST00000457059; ENSP00000412444; ENSG00000158560.
DR GeneID; 1780; -.
DR KEGG; hsa:1780; -.
DR UCSC; uc003uoc.4; human.
DR CTD; 1780; -.
DR GeneCards; GC07P095401; -.
DR HGNC; HGNC:2963; DYNC1I1.
DR HPA; HPA021315; -.
DR MIM; 603772; gene.
DR neXtProt; NX_O14576; -.
DR PharmGKB; PA27434; -.
DR eggNOG; NOG308180; -.
DR HOGENOM; HOG000116383; -.
DR HOVERGEN; HBG004083; -.
DR InParanoid; O14576; -.
DR KO; K10415; -.
DR OMA; KVGHDSE; -.
DR PhylomeDB; O14576; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; O14576; -.
DR GeneWiki; DYNC1I1; -.
DR GenomeRNAi; 1780; -.
DR NextBio; 7243; -.
DR PRO; PR:O14576; -.
DR ArrayExpress; O14576; -.
DR Bgee; O14576; -.
DR CleanEx; HS_DYNC1I1; -.
DR Genevestigator; O14576; -.
DR GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:HGNC.
DR GO; GO:0003777; F:microtubule motor activity; ISS:HGNC.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0047496; P:vesicle transport along microtubule; ISS:HGNC.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR025956; Dynein_IC_1/2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR017986; WD40_repeat_dom.
DR Pfam; PF11540; Dynein_IC2; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 5.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; FALSE_NEG.
DR PROSITE; PS50082; WD_REPEATS_2; FALSE_NEG.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Centromere; Chromosome; Complete proteome;
KW Cytoplasm; Cytoskeleton; Dynein; Kinetochore; Microtubule;
KW Motor protein; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat; Transport; WD repeat.
FT CHAIN 1 645 Cytoplasmic dynein 1 intermediate chain
FT 1.
FT /FTId=PRO_0000114652.
FT REPEAT 285 334 WD 1.
FT REPEAT 338 378 WD 2.
FT REPEAT 387 428 WD 3.
FT REPEAT 437 477 WD 4.
FT REPEAT 482 527 WD 5.
FT REPEAT 530 570 WD 6.
FT REPEAT 576 615 WD 7.
FT REGION 1 123 Interaction with DCTN1 (By similarity).
FT MOD_RES 635 635 Phosphoserine.
FT VAR_SEQ 74 90 Missing (in isoform 2 and isoform 3).
FT /FTId=VSP_001332.
FT VAR_SEQ 123 142 Missing (in isoform 3).
FT /FTId=VSP_001333.
FT VARIANT 373 373 H -> L (found in a renal cell carcinoma
FT case; somatic mutation).
FT /FTId=VAR_064709.
FT VARIANT 582 582 N -> T (in dbSNP:rs35077523).
FT /FTId=VAR_048905.
SQ SEQUENCE 645 AA; 72955 MW; 55A6FF971E632DA0 CRC64;
MSDKSDLKAE LERKKQRLAQ IREEKKRKEE ERKKKEADMQ QKKEPVQDDS DLDRKRRETE
ALLQSIGISP EPPLVQPLHF LTWDTCYFHY LVPTPMSPSS KSVSTPSEAG SQDSGDLGPL
TRTLQWDTDP SVLQLQSDSE LGRRLHKLGV SKVTQVDFLP REVVSYSKET QTPLATHQSE
EDEEDEEMVE SKVGQDSELE NQDKKQEVKE APPRELTEEE KQQILHSEEF LIFFDRTIRV
IERALAEDSD IFFDYSGREL EEKDGDVQAG ANLSFNRQFY DEHWSKHRVV TCMDWSLQYP
ELMVASYNNN EDAPHEPDGV ALVWNMKFKK TTPEYVFHCQ SSVMSVCFAR FHPNLVVGGT
YSGQIVLWDN RSHRRTPVQR TPLSAAAHTH PVYCVNVVGT QNAHNLITVS TDGKMCSWSL
DMLSTPQESM ELVYNKSKPV AVTGMAFPTG DVNNFVVGSE EGTVYTACRH GSKAGIGEVF
EGHQGPVTGI NCHMAVGPID FSHLFVTSSF DWTVKLWTTK HNKPLYSFED NADYVYDVMW
SPVHPALFAC VDGMGRLDLW NLNNDTEVPT ASVAIEGASA LNRVRWAQAG KEVAVGDSEG
RIWVYDVGEL AVPHNDEWTR FARTLVEIRA NRADSEEEGT VELSA
//
MIM
603772
*RECORD*
*FIELD* NO
603772
*FIELD* TI
*603772 DYNEIN, CYTOPLASMIC 1, INTERMEDIATE CHAIN 1; DYNC1I1
;;DNCI1;;
IC74
*FIELD* TX
read moreCytoplasmic dynein is large multisubunit microtubule-based motor protein
composed of heavy, intermediate, light-intermediate, and light chains.
See 603297. By searching for genes within the candidate region for
split-hand/foot deformity, type I (183600) on chromosome 7q21.3-q22.1,
Crackower et al. (1999) identified DNCI1, a gene encoding a cytoplasmic
dynein intermediate chain. The DNCI1 gene contains 17 exons and spans
approximately 160 kb. These authors also cloned cDNAs encoding mouse
Dnci2 (603331) and several alternatively spliced isoforms of human and
mouse Dnci1. The longest human isoform, DNCI1A, is a predicted 645-amino
acid protein that is 97% and 98% identical to mouse and rat Dnci1,
respectively. Northern blot analysis and in situ hybridization detected
Dnci1 expression primarily in the developing mouse forebrain as well as
in the peripheral nervous system. Crackower et al. (1999) noted that
mouse Dnci1 had been mapped to mouse chromosome 6.
*FIELD* RF
1. Crackower, M. A.; Sinasac, D. S.; Xia, J.; Motoyama, J.; Prochazka,
M.; Rommens, J. M.; Scherer, S. W.; Tsui, L.-C.: Cloning and characterization
of two cytoplasmic dynein intermediate chain genes in mouse and human. Genomics 55:
257-267, 1999.
*FIELD* CD
Rebekah S. Rasooly: 4/26/1999
*FIELD* ED
mgross: 02/10/2012
mgross: 4/19/2006
alopez: 4/26/1999
*RECORD*
*FIELD* NO
603772
*FIELD* TI
*603772 DYNEIN, CYTOPLASMIC 1, INTERMEDIATE CHAIN 1; DYNC1I1
;;DNCI1;;
IC74
*FIELD* TX
read moreCytoplasmic dynein is large multisubunit microtubule-based motor protein
composed of heavy, intermediate, light-intermediate, and light chains.
See 603297. By searching for genes within the candidate region for
split-hand/foot deformity, type I (183600) on chromosome 7q21.3-q22.1,
Crackower et al. (1999) identified DNCI1, a gene encoding a cytoplasmic
dynein intermediate chain. The DNCI1 gene contains 17 exons and spans
approximately 160 kb. These authors also cloned cDNAs encoding mouse
Dnci2 (603331) and several alternatively spliced isoforms of human and
mouse Dnci1. The longest human isoform, DNCI1A, is a predicted 645-amino
acid protein that is 97% and 98% identical to mouse and rat Dnci1,
respectively. Northern blot analysis and in situ hybridization detected
Dnci1 expression primarily in the developing mouse forebrain as well as
in the peripheral nervous system. Crackower et al. (1999) noted that
mouse Dnci1 had been mapped to mouse chromosome 6.
*FIELD* RF
1. Crackower, M. A.; Sinasac, D. S.; Xia, J.; Motoyama, J.; Prochazka,
M.; Rommens, J. M.; Scherer, S. W.; Tsui, L.-C.: Cloning and characterization
of two cytoplasmic dynein intermediate chain genes in mouse and human. Genomics 55:
257-267, 1999.
*FIELD* CD
Rebekah S. Rasooly: 4/26/1999
*FIELD* ED
mgross: 02/10/2012
mgross: 4/19/2006
alopez: 4/26/1999