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DC1I1_HUMAN
ID   DC1I1_HUMAN             Reviewed;         645 AA.
AC   O14576; B4DME3; F5H050; G5E9K1; Q8TBF7; Q9Y2X1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 2.
DT   03-AUG-2022, entry version 192.
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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 chain
RT   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] (ISOFORMS 2 AND 4).
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., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., 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., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   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., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., 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., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
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 the
RT   spindle assembly checkpoint.";
RL   EMBO J. 28:902-914(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [9]
RP   INTERACTION WITH DYNLT1, AND MUTAGENESIS OF LEU-148; GLY-149; VAL-150;
RP   LYS-152; VAL-153; GLN-155; VAL-156; ASP-157 AND PHE-158.
RX   PubMed=27502274; DOI=10.1074/jbc.m116.736884;
RA   Merino-Gracia J., Zamora-Carreras H., Bruix M., Rodriguez-Crespo I.;
RT   "Molecular basis for the protein recognition specificity of the dynein
RT   light chain DYNLT1/Tctex1: characterization of the interaction with activin
RT   receptor IIB.";
RL   J. Biol. Chem. 291:20962-20975(2016).
RN   [10]
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., Davies H.,
RA   Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA   Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA   Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA   Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA   Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA   Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA   Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT   "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT   PBRM1 in renal carcinoma.";
RL   Nature 469:539-542(2011).
CC   -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC       the cytoplasmic dynein 1 complex that are thought to be involved in
CC       linking dynein to cargos and to adapter proteins that regulate dynein
CC       function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC       retrograde motility of vesicles and organelles along microtubules. The
CC       intermediate chains mediate the binding of dynein to dynactin via its
CC       150 kDa component (p150-glued) DCTN1. May play a role in mediating the
CC       interaction of cytoplasmic dynein with membranous organelles and
CC       kinetochores.
CC   -!- SUBUNIT: Homodimer (By similarity). The cytoplasmic dynein 1 complex
CC       consists of two catalytic heavy chains (HCs) and a number of non-
CC       catalytic subunits presented by intermediate chains (ICs), light
CC       intermediate chains (LICs) and light chains (LCs); the composition
CC       seems to vary in respect to the IC, LIC and LC composition. The heavy
CC       chain homodimer serves as a scaffold for the probable homodimeric
CC       assembly of the respective non-catalytic subunits. The ICs and LICs
CC       bind directly to the HC dimer and the LCs assemble on the IC dimer.
CC       Interacts with DYNC1H1. Interacts with DYNLT1 and DYNLT3. Interacts
CC       with DCTN1 (By similarity). {ECO:0000250, ECO:0000269|PubMed:27502274}.
CC   -!- INTERACTION:
CC       O14576; Q8TD16: BICD2; NbExp=2; IntAct=EBI-366267, EBI-2372628;
CC       O14576; Q9CZA6: Nde1; Xeno; NbExp=2; IntAct=EBI-366267, EBI-309934;
CC       O14576-2; P05067: APP; NbExp=3; IntAct=EBI-25840445, EBI-77613;
CC       O14576-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-25840445, EBI-25840379;
CC       O14576-2; Q9GZQ8: MAP1LC3B; NbExp=3; IntAct=EBI-25840445, EBI-373144;
CC       O14576-2; P00491: PNP; NbExp=3; IntAct=EBI-25840445, EBI-712238;
CC       O14576-2; P04271: S100B; NbExp=3; IntAct=EBI-25840445, EBI-458391;
CC       O14576-2; Q13501: SQSTM1; NbExp=3; IntAct=EBI-25840445, EBI-307104;
CC       O14576-2; P43405-2: SYK; NbExp=3; IntAct=EBI-25840445, EBI-25892332;
CC       O14576-2; Q9BVJ6: UTP14A; NbExp=3; IntAct=EBI-25840445, EBI-473284;
CC       O14576-2; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-25840445, EBI-11141397;
CC       O14576-5; P05067: APP; NbExp=3; IntAct=EBI-25936079, EBI-77613;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Chromosome, centromere,
CC       kinetochore {ECO:0000269|PubMed:19229290}. Cytoplasm, cytoskeleton,
CC       spindle pole {ECO:0000269|PubMed:19229290}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
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       Name=4;
CC         IsoId=O14576-4; Sequence=VSP_001332, VSP_001333, VSP_054766;
CC       Name=5;
CC         IsoId=O14576-5; Sequence=VSP_001333;
CC   -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC       {ECO:0000305}.
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DR   EMBL; AF063228; AAC33443.1; -; mRNA.
DR   EMBL; AF123074; AAD26852.1; -; mRNA.
DR   EMBL; AK091339; BAC03639.1; -; mRNA.
DR   EMBL; AK297427; BAG59855.1; -; 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   EMBL; CH471091; EAW76753.1; -; Genomic_DNA.
DR   EMBL; BC022540; AAH22540.1; -; mRNA.
DR   CCDS; CCDS47645.1; -. [O14576-2]
DR   CCDS; CCDS47646.1; -. [O14576-3]
DR   CCDS; CCDS5644.1; -. [O14576-1]
DR   CCDS; CCDS64718.1; -. [O14576-5]
DR   CCDS; CCDS64719.1; -. [O14576-4]
DR   RefSeq; NP_001129028.1; NM_001135556.1. [O14576-2]
DR   RefSeq; NP_001129029.1; NM_001135557.1. [O14576-3]
DR   RefSeq; NP_001265350.1; NM_001278421.1. [O14576-5]
DR   RefSeq; NP_001265351.1; NM_001278422.1. [O14576-4]
DR   RefSeq; NP_004402.1; NM_004411.4. [O14576-1]
DR   RefSeq; XP_011514163.1; XM_011515861.1.
DR   RefSeq; XP_011514164.1; XM_011515862.1.
DR   RefSeq; XP_016867293.1; XM_017011804.1.
DR   RefSeq; XP_016867294.1; XM_017011805.1.
DR   AlphaFoldDB; O14576; -.
DR   SMR; O14576; -.
DR   BioGRID; 108118; 105.
DR   CORUM; O14576; -.
DR   ELM; O14576; -.
DR   IntAct; O14576; 57.
DR   MINT; O14576; -.
DR   STRING; 9606.ENSP00000320130; -.
DR   GlyGen; O14576; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O14576; -.
DR   PhosphoSitePlus; O14576; -.
DR   BioMuta; DYNC1I1; -.
DR   EPD; O14576; -.
DR   jPOST; O14576; -.
DR   MassIVE; O14576; -.
DR   MaxQB; O14576; -.
DR   PaxDb; O14576; -.
DR   PeptideAtlas; O14576; -.
DR   PRIDE; O14576; -.
DR   ProteomicsDB; 25229; -.
DR   ProteomicsDB; 33962; -.
DR   ProteomicsDB; 48091; -. [O14576-1]
DR   ProteomicsDB; 48092; -. [O14576-2]
DR   ProteomicsDB; 48093; -. [O14576-3]
DR   TopDownProteomics; O14576-3; -. [O14576-3]
DR   Antibodypedia; 15905; 160 antibodies from 26 providers.
DR   DNASU; 1780; -.
DR   Ensembl; ENST00000324972.10; ENSP00000320130.6; ENSG00000158560.14. [O14576-1]
DR   Ensembl; ENST00000359388.8; ENSP00000352348.4; ENSG00000158560.14. [O14576-3]
DR   Ensembl; ENST00000437599.5; ENSP00000398118.1; ENSG00000158560.14. [O14576-5]
DR   Ensembl; ENST00000447467.6; ENSP00000392337.2; ENSG00000158560.14. [O14576-2]
DR   Ensembl; ENST00000457059.2; ENSP00000412444.1; ENSG00000158560.14. [O14576-2]
DR   Ensembl; ENST00000630942.2; ENSP00000486363.1; ENSG00000158560.14. [O14576-4]
DR   GeneID; 1780; -.
DR   KEGG; hsa:1780; -.
DR   MANE-Select; ENST00000447467.6; ENSP00000392337.2; NM_001135556.2; NP_001129028.1. [O14576-2]
DR   UCSC; uc003uob.4; human. [O14576-1]
DR   CTD; 1780; -.
DR   DisGeNET; 1780; -.
DR   GeneCards; DYNC1I1; -.
DR   HGNC; HGNC:2963; DYNC1I1.
DR   HPA; ENSG00000158560; Tissue enhanced (brain).
DR   MIM; 603772; gene.
DR   neXtProt; NX_O14576; -.
DR   OpenTargets; ENSG00000158560; -.
DR   PharmGKB; PA27434; -.
DR   VEuPathDB; HostDB:ENSG00000158560; -.
DR   eggNOG; KOG1587; Eukaryota.
DR   GeneTree; ENSGT00940000156032; -.
DR   HOGENOM; CLU_012999_1_1_1; -.
DR   InParanoid; O14576; -.
DR   OMA; YVRDYTI; -.
DR   PhylomeDB; O14576; -.
DR   TreeFam; TF300553; -.
DR   PathwayCommons; O14576; -.
DR   Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   Reactome; R-HSA-68877; Mitotic Prometaphase.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Reactome; R-HSA-9646399; Aggrephagy.
DR   Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   SignaLink; O14576; -.
DR   BioGRID-ORCS; 1780; 7 hits in 1066 CRISPR screens.
DR   ChiTaRS; DYNC1I1; human.
DR   GeneWiki; DYNC1I1; -.
DR   GenomeRNAi; 1780; -.
DR   Pharos; O14576; Tbio.
DR   PRO; PR:O14576; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; O14576; protein.
DR   Bgee; ENSG00000158560; Expressed in endothelial cell and 167 other tissues.
DR   ExpressionAtlas; O14576; baseline and differential.
DR   Genevisible; O14576; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
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:0005634; C:nucleus; IDA:AgBase.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR   GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR   GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR   GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR   GO; GO:0003774; F:cytoskeletal motor activity; TAS:ProtInc.
DR   GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR   GO; GO:0045503; F:dynein light chain binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; ISS:HGNC-UCL.
DR   GO; GO:0003777; F:microtubule motor activity; ISS:HGNC-UCL.
DR   GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR   GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR   GO; GO:0010970; P:transport along microtubule; IBA:GO_Central.
DR   GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR025956; DYNC1I1/DYNC1I2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF11540; Dynein_IC2; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 5.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Centromere; Chromosome; Cytoplasm;
KW   Cytoskeleton; Dynein; Kinetochore; Microtubule; Motor protein;
KW   Phosphoprotein; Reference proteome; Repeat; Transport; WD repeat.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q13409"
FT   CHAIN           2..645
FT                   /note="Cytoplasmic dynein 1 intermediate chain 1"
FT                   /id="PRO_0000114652"
FT   REPEAT          285..334
FT                   /note="WD 1"
FT   REPEAT          338..378
FT                   /note="WD 2"
FT   REPEAT          387..428
FT                   /note="WD 3"
FT   REPEAT          437..477
FT                   /note="WD 4"
FT   REPEAT          482..527
FT                   /note="WD 5"
FT   REPEAT          530..570
FT                   /note="WD 6"
FT   REPEAT          576..615
FT                   /note="WD 7"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2..123
FT                   /note="Interaction with DCTN1"
FT                   /evidence="ECO:0000250"
FT   REGION          95..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..163
FT                   /note="Interaction with DYNLT1"
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   REGION          169..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        192..221
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13409"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88485"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62871"
FT   MOD_RES         105
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13409"
FT   MOD_RES         107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13409"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88485"
FT   MOD_RES         114
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88485"
FT   MOD_RES         176
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:O88485"
FT   MOD_RES         179
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88485"
FT   MOD_RES         197
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O88485"
FT   MOD_RES         635
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   VAR_SEQ         74..90
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT                   /id="VSP_001332"
FT   VAR_SEQ         123..142
FT                   /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT                   /id="VSP_001333"
FT   VAR_SEQ         610..645
FT                   /note="LAVPHNDEWTRFARTLVEIRANRADSEEEGTVELSA -> GLAMLPGWSQNS
FT                   WTQAILLCWPPKVLGLQT (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_054766"
FT   VARIANT         373
FT                   /note="H -> L (found in a renal cell carcinoma case;
FT                   somatic mutation)"
FT                   /evidence="ECO:0000269|PubMed:21248752"
FT                   /id="VAR_064709"
FT   VARIANT         582
FT                   /note="N -> T (in dbSNP:rs35077523)"
FT                   /id="VAR_048905"
FT   MUTAGEN         148
FT                   /note="L->G: Disrupts interaction with DYNLT1."
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   MUTAGEN         149
FT                   /note="G->E: No effect on interaction with DYNLT1."
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   MUTAGEN         150
FT                   /note="V->G: Disrupts interaction with DYNLT1."
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   MUTAGEN         150
FT                   /note="V->W: No effect on interaction with DYNLT1."
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   MUTAGEN         152
FT                   /note="K->A,Y: No effect on interaction with DYNLT1."
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   MUTAGEN         153
FT                   /note="V->G: Decreases interaction with DYNLT1."
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   MUTAGEN         155
FT                   /note="Q->H,R,T,Y: No effect on interaction with DYNLT1."
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   MUTAGEN         156
FT                   /note="V->G: Decreases interaction with DYNLT1."
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   MUTAGEN         157
FT                   /note="D->R: No effect on interaction with DYNLT1."
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   MUTAGEN         158
FT                   /note="F->G: Disrupts interaction with DYNLT1."
FT                   /evidence="ECO:0000269|PubMed:27502274"
FT   CONFLICT        254
FT                   /note="D -> G (in Ref. 3; BAG59855)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        517
FT                   /note="W -> C (in Ref. 6; AAH22540)"
FT                   /evidence="ECO:0000305"
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
 
 
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