DC1I2_HUMAN
ID DC1I2_HUMAN Reviewed; 638 AA.
AC Q13409; B7ZA04; D3DPD4; D3DPD5; D3DPD6; Q32LY9; Q53S84; Q5BJF8; Q7Z4X1;
AC Q96NG7; Q96S87; Q9BXZ5; Q9NT58;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Cytoplasmic dynein 1 intermediate chain 2;
DE AltName: Full=Cytoplasmic dynein intermediate chain 2;
DE AltName: Full=Dynein intermediate chain 2, cytosolic;
DE Short=DH IC-2;
GN Name=DYNC1I2; Synonyms=DNCI2, DNCIC2;
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 2C).
RA Huang J., Yu L., Zhao S.Y.;
RT "Cloning of a new human cDNA homologous to Rattus norvegicus cytoplasmic
RT dynein intermediate chain 2C.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2C AND 2F).
RA Li N., Wan T., Zhang M., Zhang W., Cao X.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2A AND 3).
RC TISSUE=Brain, and Thalamus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C).
RC TISSUE=Endometrium, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C).
RC TISSUE=Kidney, Skin, and Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-448 (ISOFORM 2A).
RX PubMed=8522607; DOI=10.1083/jcb.131.6.1507;
RA Vaughan K.T., Vallee R.B.;
RT "Cytoplasmic dynein binds dynactin through a direct interaction between the
RT intermediate chains and p150Glued.";
RL J. Cell Biol. 131:1507-1516(1995).
RN [10]
RP PROTEIN SEQUENCE OF 236-250, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-73 (ISOFORMS 2B; 2C AND 2F), AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP INTERACTION WITH HUMAN ADENOVIRUS HEXON PROTEIN (MICROBIAL INFECTION).
RX PubMed=20006841; DOI=10.1016/j.chom.2009.11.006;
RA Bremner K.H., Scherer J., Yi J., Vershinin M., Gross S.P., Vallee R.B.;
RT "Adenovirus transport via direct interaction of cytoplasmic dynein with the
RT viral capsid hexon subunit.";
RL Cell Host Microbe 6:523-535(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-81 (ISOFORMS 2B; 2C AND 2F), 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 (ISOFORMS 2B; 2C AND 2F),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; THR-95; SER-97; SER-101
RP AND SER-104, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84 (ISOFORMS 2B; 2C AND 2F),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [24]
RP INVOLVEMENT IN NEDMIBA, VARIANTS NEDMIBA CYS-247 AND 290-GLN--ALA-638 DEL,
RP CHARACTERIZATION OF VARIANTS NEDMIBA CYS-247 AND 290-GLN--ALA-638 DEL,
RP CHARACTERIZATION OF VARIANT ALA-516, AND FUNCTION.
RX PubMed=31079899; DOI=10.1016/j.ajhg.2019.04.002;
RA Ansar M., Ullah F., Paracha S.A., Adams D.J., Lai A., Pais L.,
RA Iwaszkiewicz J., Millan F., Sarwar M.T., Agha Z., Shah S.F., Qaisar A.A.,
RA Falconnet E., Zoete V., Ranza E., Makrythanasis P., Santoni F.A., Ahmed J.,
RA Katsanis N., Walsh C., Davis E.E., Antonarakis S.E.;
RT "Bi-allelic variants in DYNC1I2 cause syndromic microcephaly with
RT intellectual disability, cerebral malformations, and dysmorphic facial
RT features.";
RL Am. J. Hum. Genet. 104:1073-1087(2019).
RN [25]
RP STRUCTURE BY NMR OF 134-154 IN COMPLEX WITH DYNLT1.
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).
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 (PubMed:31079899). Cytoplasmic dynein 1 acts as a motor for
CC the intracellular retrograde motility of vesicles and organelles along
CC microtubules (PubMed:31079899). The intermediate chains mediate the
CC binding of dynein to dynactin via its 150 kDa component (p150-glued)
CC DCTN1 (By similarity). Involved in membrane-transport, such as Golgi
CC apparatus, late endosomes and lysosomes (By similarity).
CC {ECO:0000250|UniProtKB:Q62871, ECO:0000269|PubMed:31079899}.
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 (By
CC similarity). The heavy chain homodimer serves as a scaffold for the
CC probable homodimeric assembly of the respective non-catalytic subunits
CC (By similarity). The ICs and LICs bind directly to the HC dimer and the
CC LCs assemble on the IC dimer (By similarity). Interacts with DYNLT3 (By
CC similarity). Interacts with DYNLT1 (PubMed:27502274). Interacts
CC (dephosphorylated at Ser-90) with DCTN1 (By similarity). Interacts with
CC BICD2. Interacts with SPEF2 (By similarity).
CC {ECO:0000250|UniProtKB:O88487, ECO:0000250|UniProtKB:Q62871,
CC ECO:0000269|PubMed:27502274}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human adenovirus 5 hexon
CC protein; this interaction probably allows virus intracellular
CC transport. {ECO:0000269|PubMed:20006841}.
CC -!- INTERACTION:
CC Q13409; Q9NP97: DYNLRB1; NbExp=5; IntAct=EBI-742998, EBI-372128;
CC Q13409-3; P63172: DYNLT1; NbExp=3; IntAct=EBI-12094038, EBI-1176455;
CC Q13409-3; P51808: DYNLT3; NbExp=3; IntAct=EBI-12094038, EBI-743027;
CC Q13409-3; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-12094038, EBI-10172876;
CC Q13409-3; Q13136: PPFIA1; NbExp=3; IntAct=EBI-12094038, EBI-745426;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O88487}. Cytoplasm
CC {ECO:0000250|UniProtKB:O88487}. Note=Detected in the cytoplasm of
CC pachytene spermatocytes. Localizes to the manchette in elongating
CC spermatids. {ECO:0000250|UniProtKB:O88487}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=2A;
CC IsoId=Q13409-1; Sequence=Displayed;
CC Name=2B;
CC IsoId=Q13409-2; Sequence=VSP_001336;
CC Name=2C;
CC IsoId=Q13409-3; Sequence=VSP_001336, VSP_001337;
CC Name=2E;
CC IsoId=Q13409-5; Sequence=VSP_023011;
CC Name=2F;
CC IsoId=Q13409-6; Sequence=VSP_001336, VSP_001337, VSP_023011;
CC Name=3;
CC IsoId=Q13409-7; Sequence=VSP_054377, VSP_001337;
CC -!- PTM: The phosphorylation status of Ser-90 appears to be involved in
CC dynactin-dependent target binding. {ECO:0000250|UniProtKB:Q62871}.
CC -!- PTM: Pyrophosphorylation by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) promotes interaction with DCTN1. Serine pyrophosphorylation is
CC achieved by Mg(2+)-dependent, but enzyme independent transfer of a
CC beta-phosphate from a inositol pyrophosphate to a pre-phosphorylated
CC serine residue. {ECO:0000250|UniProtKB:O88487}.
CC -!- DISEASE: Neurodevelopmental disorder with microcephaly and structural
CC brain anomalies (NEDMIBA) [MIM:618492]: An autosomal recessive
CC neurodevelopmental disorder characterized by global developmental
CC delay, severe intellectual disability, microcephaly, dysmorphic facial
CC features, and cerebral malformations including simplification of
CC cerebral gyration, agenesis of the corpus callosum, and brainstem and
CC white matter hypoplasia. {ECO:0000269|PubMed:31079899}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the dynein intermediate chain family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA89166.1; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Several sequence problems.; Evidence={ECO:0000305};
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DR EMBL; AF134477; AAP97254.1; -; mRNA.
DR EMBL; AF250307; AAK37426.1; -; mRNA.
DR EMBL; AY037160; AAK67638.1; -; mRNA.
DR EMBL; BT007130; AAP35794.1; -; mRNA.
DR EMBL; AK055491; BAB70932.1; -; mRNA.
DR EMBL; AK316119; BAH14490.1; -; mRNA.
DR EMBL; AL137519; CAB70785.1; -; mRNA.
DR EMBL; BX537412; CAD97654.1; -; mRNA.
DR EMBL; AC064826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068039; AAY24133.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11202.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11204.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11206.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11207.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11208.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11209.1; -; Genomic_DNA.
DR EMBL; BC091498; AAH91498.1; -; mRNA.
DR EMBL; BC109375; AAI09376.1; -; mRNA.
DR EMBL; BC015038; AAH15038.1; -; mRNA.
DR EMBL; U39575; AAA89166.1; ALT_SEQ; mRNA.
DR CCDS; CCDS46450.1; -. [Q13409-1]
DR CCDS; CCDS63054.1; -. [Q13409-7]
DR CCDS; CCDS63056.1; -. [Q13409-3]
DR CCDS; CCDS63057.1; -. [Q13409-6]
DR CCDS; CCDS82533.1; -. [Q13409-2]
DR PIR; T46365; T46365.
DR RefSeq; NP_001258714.1; NM_001271785.1. [Q13409-1]
DR RefSeq; NP_001258715.1; NM_001271786.1. [Q13409-7]
DR RefSeq; NP_001258716.1; NM_001271787.1. [Q13409-7]
DR RefSeq; NP_001258717.1; NM_001271788.1. [Q13409-3]
DR RefSeq; NP_001258718.1; NM_001271789.1. [Q13409-3]
DR RefSeq; NP_001258719.1; NM_001271790.1. [Q13409-6]
DR RefSeq; NP_001307811.1; NM_001320882.1. [Q13409-2]
DR RefSeq; NP_001307812.1; NM_001320883.1. [Q13409-2]
DR RefSeq; NP_001307813.1; NM_001320884.1. [Q13409-6]
DR RefSeq; NP_001369.1; NM_001378.2. [Q13409-1]
DR PDB; 5JPW; NMR; -; A/B=134-154.
DR PDB; 6F1T; EM; 3.50 A; g/h/o/p=1-638.
DR PDB; 6F1U; EM; 3.40 A; h=1-638.
DR PDB; 6F1Z; EM; 3.40 A; o/p=1-638.
DR PDB; 6F38; EM; 6.70 A; g/h/o/p=1-638.
DR PDB; 6F3A; EM; 8.20 A; g/h=1-638.
DR PDBsum; 5JPW; -.
DR PDBsum; 6F1T; -.
DR PDBsum; 6F1U; -.
DR PDBsum; 6F1Z; -.
DR PDBsum; 6F38; -.
DR PDBsum; 6F3A; -.
DR AlphaFoldDB; Q13409; -.
DR SMR; Q13409; -.
DR BioGRID; 108119; 227.
DR ComplexPortal; CPX-5025; Cytoplasmic dynein complex, variant 1.
DR ELM; Q13409; -.
DR IntAct; Q13409; 42.
DR MINT; Q13409; -.
DR STRING; 9606.ENSP00000380308; -.
DR ChEMBL; CHEMBL4295815; -.
DR GlyGen; Q13409; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13409; -.
DR PhosphoSitePlus; Q13409; -.
DR SwissPalm; Q13409; -.
DR BioMuta; DYNC1I2; -.
DR DMDM; 23503058; -.
DR REPRODUCTION-2DPAGE; IPI00827813; -.
DR EPD; Q13409; -.
DR jPOST; Q13409; -.
DR MassIVE; Q13409; -.
DR MaxQB; Q13409; -.
DR PaxDb; Q13409; -.
DR PeptideAtlas; Q13409; -.
DR PRIDE; Q13409; -.
DR ProteomicsDB; 59388; -. [Q13409-1]
DR ProteomicsDB; 59389; -. [Q13409-2]
DR ProteomicsDB; 59390; -. [Q13409-3]
DR ProteomicsDB; 59391; -. [Q13409-5]
DR ProteomicsDB; 59392; -. [Q13409-6]
DR ProteomicsDB; 7048; -.
DR Antibodypedia; 33847; 150 antibodies from 30 providers.
DR DNASU; 1781; -.
DR Ensembl; ENST00000340296.8; ENSP00000339430.4; ENSG00000077380.16. [Q13409-3]
DR Ensembl; ENST00000397119.8; ENSP00000380308.3; ENSG00000077380.16. [Q13409-1]
DR Ensembl; ENST00000409197.5; ENSP00000386397.1; ENSG00000077380.16. [Q13409-3]
DR Ensembl; ENST00000409317.5; ENSP00000386591.1; ENSG00000077380.16. [Q13409-2]
DR Ensembl; ENST00000409453.5; ENSP00000386886.1; ENSG00000077380.16. [Q13409-5]
DR Ensembl; ENST00000409773.5; ENSP00000386415.1; ENSG00000077380.16. [Q13409-1]
DR Ensembl; ENST00000410079.7; ENSP00000386522.3; ENSG00000077380.16. [Q13409-7]
DR Ensembl; ENST00000508530.5; ENSP00000423339.1; ENSG00000077380.16. [Q13409-6]
DR GeneID; 1781; -.
DR KEGG; hsa:1781; -.
DR MANE-Select; ENST00000397119.8; ENSP00000380308.3; NM_001378.3; NP_001369.1.
DR UCSC; uc002uha.3; human. [Q13409-1]
DR CTD; 1781; -.
DR DisGeNET; 1781; -.
DR GeneCards; DYNC1I2; -.
DR HGNC; HGNC:2964; DYNC1I2.
DR HPA; ENSG00000077380; Low tissue specificity.
DR MalaCards; DYNC1I2; -.
DR MIM; 603331; gene.
DR MIM; 618492; phenotype.
DR neXtProt; NX_Q13409; -.
DR OpenTargets; ENSG00000077380; -.
DR PharmGKB; PA27435; -.
DR VEuPathDB; HostDB:ENSG00000077380; -.
DR eggNOG; KOG1587; Eukaryota.
DR GeneTree; ENSGT00940000155442; -.
DR HOGENOM; CLU_012999_1_1_1; -.
DR InParanoid; Q13409; -.
DR OMA; EEGSIYP; -.
DR PhylomeDB; Q13409; -.
DR TreeFam; TF300553; -.
DR PathwayCommons; Q13409; -.
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-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
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-8854518; AURKA Activation by TPX2.
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; Q13409; -.
DR SIGNOR; Q13409; -.
DR BioGRID-ORCS; 1781; 764 hits in 1083 CRISPR screens.
DR ChiTaRS; DYNC1I2; human.
DR GeneWiki; DYNC1I2; -.
DR GenomeRNAi; 1781; -.
DR Pharos; Q13409; Tbio.
DR PRO; PR:Q13409; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q13409; protein.
DR Bgee; ENSG00000077380; Expressed in calcaneal tendon and 163 other tissues.
DR ExpressionAtlas; Q13409; baseline and differential.
DR Genevisible; Q13409; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030286; C:dynein complex; IPI:ComplexPortal.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
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:0003777; F:microtubule motor activity; NAS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0010970; P:transport along microtubule; IBA:GO_Central.
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 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Disease variant; Dynein; Host-virus interaction;
KW Intellectual disability; Microtubule; Motor protein; Phosphoprotein;
KW Reference proteome; Repeat; Transport; WD repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..638
FT /note="Cytoplasmic dynein 1 intermediate chain 2"
FT /id="PRO_0000114655"
FT REPEAT 277..326
FT /note="WD 1"
FT REPEAT 330..370
FT /note="WD 2"
FT REPEAT 379..420
FT /note="WD 3"
FT REPEAT 429..469
FT /note="WD 4"
FT REPEAT 474..519
FT /note="WD 5"
FT REPEAT 522..562
FT /note="WD 6"
FT REPEAT 568..607
FT /note="WD 7"
FT REGION 1..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 51
FT /note="Diphosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88487"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62871"
FT MOD_RES 95
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 76..81
FT /note="VFSEYW -> AEQPLRVVTADTCLFHYL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054377"
FT VAR_SEQ 77..82
FT /note="Missing (in isoform 2B, isoform 2C and isoform 2F)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_001336"
FT VAR_SEQ 113..132
FT /note="Missing (in isoform 2C, isoform 2F and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.1, ECO:0000303|Ref.2, ECO:0000303|Ref.3"
FT /id="VSP_001337"
FT VAR_SEQ 602
FT /note="Missing (in isoform 2E and isoform 2F)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_023011"
FT VARIANT 247
FT /note="Y -> C (in NEDMIBA; loss-of-function variant; does
FT not rescue neurodevelopmental defects in zebrafish
FT morphants)"
FT /evidence="ECO:0000269|PubMed:31079899"
FT /id="VAR_082947"
FT VARIANT 290..638
FT /note="Missing (in NEDMIBA; loss-of-function variant; does
FT not rescue neurodevelopmental defects in zebrafish
FT morphants)"
FT /evidence="ECO:0000269|PubMed:31079899"
FT /id="VAR_082948"
FT VARIANT 516
FT /note="P -> A (likely benign variant; can rescue
FT neurodevelopmental defects in zebrafish morphants;
FT dbSNP:rs767705533)"
FT /evidence="ECO:0000269|PubMed:31079899"
FT /id="VAR_082949"
FT CONFLICT 510
FT /note="T -> S (in Ref. 1; AAP97254)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="D -> G (in Ref. 1; AAP97254)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="A -> G (in Ref. 8; AAI09376)"
FT /evidence="ECO:0000305"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:5JPW"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:6F1Z"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:6F1Z"
FT HELIX 222..235
FT /evidence="ECO:0007829|PDB:6F1Z"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 289..293
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 295..301
FT /evidence="ECO:0007829|PDB:6F1T"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:6F1T"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:6F1U"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 358..361
FT /evidence="ECO:0007829|PDB:6F1U"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:6F1T"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:6F1U"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 419..423
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 467..472
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 477..483
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 497..506
FT /evidence="ECO:0007829|PDB:6F1U"
FT TURN 511..513
FT /evidence="ECO:0007829|PDB:6F1T"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:6F1T"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 545..552
FT /evidence="ECO:0007829|PDB:6F1U"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 568..570
FT /evidence="ECO:0007829|PDB:6F1T"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 585..588
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 594..597
FT /evidence="ECO:0007829|PDB:6F1U"
FT STRAND 600..602
FT /evidence="ECO:0007829|PDB:6F1T"
FT HELIX 610..619
FT /evidence="ECO:0007829|PDB:6F1U"
FT MOD_RES Q13409-2:73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q13409-2:81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q13409-2:84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q13409-3:73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q13409-3:81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q13409-3:84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q13409-6:73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q13409-6:81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES Q13409-6:84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 638 AA; 71457 MW; 2F868EC9556C47F2 CRC64;
MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA
EALLQSMGLT PESPIVFSEY WVPPPMSPSS KSVSTPSEAG SQDSGDGAVG SRTLHWDTDP
SVLQLHSDSD LGRGPIKLGM AKITQVDFPP REIVTYTKET QTPVMAQPKE DEEEDDDVVA
PKPPIEPEEE KTLKKDEEND SKAPPHELTE EEKQQILHSE EFLSFFDHST RIVERALSEQ
INIFFDYSGR DLEDKEGEIQ AGAKLSLNRQ FFDERWSKHR VVSCLDWSSQ YPELLVASYN
NNEDAPHEPD GVALVWNMKY KKTTPEYVFH CQSAVMSATF AKFHPNLVVG GTYSGQIVLW
DNRSNKRTPV QRTPLSAAAH THPVYCVNVV GTQNAHNLIS ISTDGKICSW SLDMLSHPQD
SMELVHKQSK AVAVTSMSFP VGDVNNFVVG SEEGSVYTAC RHGSKAGISE MFEGHQGPIT
GIHCHAAVGA VDFSHLFVTS SFDWTVKLWT TKNNKPLYSF EDNADYVYDV MWSPTHPALF
ACVDGMGRLD LWNLNNDTEV PTASISVEGN PALNRVRWTH SGREIAVGDS EGQIVIYDVG
EQIAVPRNDE WARFGRTLAE INANRADAEE EAATRIPA
