Q13409 (DC1I2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytoplasmic dynein 1 intermediate chain 2

Alternative name(s):
Cytoplasmic dynein intermediate chain 2
Dynein intermediate chain 2, cytosolic
Short name=DH IC-2

Gene names

Name:	DYNC1I2
Synonyms:	DNCI2, DNCIC2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	638 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Involved in membrane-transport, such as Golgi apparatus, late endosomes and lysosomes.
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 DYNLT1 and DYNLT3. Interacts with DCNT1 By similarity. Interacts with human adenovirus 5 hexon protein; this interaction probably allows virus intracellular transport. Ref.17
Subcellular location	Cytoplasm › cytoskeleton By similarity.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. The phosphorylation status of Ser-90 appears to be involved in dynactin-dependent target binding By similarity. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Sequence similarities	Belongs to the dynein intermediate chain family. Contains 7 WD repeats.
Sequence caution	The sequence AAA89166.1 differs from that shown. Reason: Unlikely isoform. Several sequence problems.

Ontologies

Keywords
Biological process	Host-virus interaction Transport
Cellular component	Cytoplasm Cytoskeleton Dynein Microtubule
Coding sequence diversity	Alternative splicing
Domain	Repeat WD repeat
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	G2/M transition of mitotic cell cycle Traceable author statement. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW microtubule-based movement Non-traceable author statement Ref.9. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	centrosome Inferred from direct assay. Source: UniProtKB cytosol Traceable author statement. Source: Reactome dynein complex Inferred from electronic annotation. Source: UniProtKB-KW microtubule Inferred from electronic annotation. Source: UniProtKB-KW vesicle Inferred from direct assay. Source: UniProtKB
Molecular function	microtubule motor activity Non-traceable author statement Ref.9. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2A (identifier: Q13409-1)

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 2B (identifier: Q13409-2)

The sequence of this isoform differs from the canonical sequence as follows:
     77-82: Missing.

Isoform 2C (identifier: Q13409-3)

The sequence of this isoform differs from the canonical sequence as follows:
     77-82: Missing.
     113-132: Missing.

Isoform 2E (identifier: Q13409-5)

The sequence of this isoform differs from the canonical sequence as follows:
     602-602: Missing.

Isoform 2F (identifier: Q13409-6)

The sequence of this isoform differs from the canonical sequence as follows:
     77-82: Missing.
     113-132: Missing.
     602-602: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 638	638	Cytoplasmic dynein 1 intermediate chain 2		PRO_0000114655
Regions
	Repeat	277 – 326	50	WD 1
	Repeat	330 – 370	41	WD 2
	Repeat	379 – 420	42	WD 3
	Repeat	429 – 469	41	WD 4
	Repeat	474 – 519	46	WD 5
	Repeat	522 – 562	41	WD 6
	Repeat	568 – 607	40	WD 7
Amino acid modifications
	Modified residue	87	1	Phosphoserine Ref.11 Ref.16
	Modified residue	90	1	Phosphoserine By similarity
	Modified residue	92	1	Phosphoserine Ref.15
	Modified residue	94	1	Phosphoserine Ref.12 Ref.14 Ref.15
	Modified residue	95	1	Phosphothreonine Ref.15
	Modified residue	97	1	Phosphoserine Ref.13 Ref.14
	Modified residue	101	1	Phosphoserine Ref.13 Ref.15
	Modified residue	104	1	Phosphoserine Ref.15 Ref.16
	Modified residue	162	1	Phosphothreonine Ref.15
Natural variations
	Alternative sequence	77 – 82	6	Missing in isoform 2B, isoform 2C and isoform 2F.		VSP_001336
	Alternative sequence	113 – 132	20	Missing in isoform 2C and isoform 2F.		VSP_001337
	Alternative sequence	602	1	Missing in isoform 2E and isoform 2F.		VSP_023011
Experimental info
	Sequence conflict	510	1	T → S in AAP97254. Ref.1
	Sequence conflict	525	1	D → G in AAP97254. Ref.1
	Sequence conflict	572	1	A → G in AAI09376. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2A [UniParc]. Last modified September 19, 2002. Version 3. Checksum: 2F868EC9556C47F2	FASTA	638	71,457
	10 20 30 40 50 60 MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA 70 80 90 100 110 120 EALLQSMGLT PESPIVFSEY WVPPPMSPSS KSVSTPSEAG SQDSGDGAVG SRTLHWDTDP 130 140 150 160 170 180 SVLQLHSDSD LGRGPIKLGM AKITQVDFPP REIVTYTKET QTPVMAQPKE DEEEDDDVVA 190 200 210 220 230 240 PKPPIEPEEE KTLKKDEEND SKAPPHELTE EEKQQILHSE EFLSFFDHST RIVERALSEQ 250 260 270 280 290 300 INIFFDYSGR DLEDKEGEIQ AGAKLSLNRQ FFDERWSKHR VVSCLDWSSQ YPELLVASYN 310 320 330 340 350 360 NNEDAPHEPD GVALVWNMKY KKTTPEYVFH CQSAVMSATF AKFHPNLVVG GTYSGQIVLW 370 380 390 400 410 420 DNRSNKRTPV QRTPLSAAAH THPVYCVNVV GTQNAHNLIS ISTDGKICSW SLDMLSHPQD 430 440 450 460 470 480 SMELVHKQSK AVAVTSMSFP VGDVNNFVVG SEEGSVYTAC RHGSKAGISE MFEGHQGPIT 490 500 510 520 530 540 GIHCHAAVGA VDFSHLFVTS SFDWTVKLWT TKNNKPLYSF EDNADYVYDV MWSPTHPALF 550 560 570 580 590 600 ACVDGMGRLD LWNLNNDTEV PTASISVEGN PALNRVRWTH SGREIAVGDS EGQIVIYDVG 610 620 630 EQIAVPRNDE WARFGRTLAE INANRADAEE EAATRIPA
	Isoform 2B [UniParc]. Checksum: 5E643B54A2979294	FASTA	632	70,645
	10 20 30 40 50 60 MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA 70 80 90 100 110 120 EALLQSMGLT PESPIVPPPM SPSSKSVSTP SEAGSQDSGD GAVGSRTLHW DTDPSVLQLH 130 140 150 160 170 180 SDSDLGRGPI KLGMAKITQV DFPPREIVTY TKETQTPVMA QPKEDEEEDD DVVAPKPPIE 190 200 210 220 230 240 PEEEKTLKKD EENDSKAPPH ELTEEEKQQI LHSEEFLSFF DHSTRIVERA LSEQINIFFD 250 260 270 280 290 300 YSGRDLEDKE GEIQAGAKLS LNRQFFDERW SKHRVVSCLD WSSQYPELLV ASYNNNEDAP 310 320 330 340 350 360 HEPDGVALVW NMKYKKTTPE YVFHCQSAVM SATFAKFHPN LVVGGTYSGQ IVLWDNRSNK 370 380 390 400 410 420 RTPVQRTPLS AAAHTHPVYC VNVVGTQNAH NLISISTDGK ICSWSLDMLS HPQDSMELVH 430 440 450 460 470 480 KQSKAVAVTS MSFPVGDVNN FVVGSEEGSV YTACRHGSKA GISEMFEGHQ GPITGIHCHA 490 500 510 520 530 540 AVGAVDFSHL FVTSSFDWTV KLWTTKNNKP LYSFEDNADY VYDVMWSPTH PALFACVDGM 550 560 570 580 590 600 GRLDLWNLNN DTEVPTASIS VEGNPALNRV RWTHSGREIA VGDSEGQIVI YDVGEQIAVP 610 620 630 RNDEWARFGR TLAEINANRA DAEEEAATRI PA
	Isoform 2C [UniParc]. Checksum: 518E1D765A2CBB15	FASTA	612	68,426
	10 20 30 40 50 60 MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA 70 80 90 100 110 120 EALLQSMGLT PESPIVPPPM SPSSKSVSTP SEAGSQDSGD GAVGSRRGPI KLGMAKITQV 130 140 150 160 170 180 DFPPREIVTY TKETQTPVMA QPKEDEEEDD DVVAPKPPIE PEEEKTLKKD EENDSKAPPH 190 200 210 220 230 240 ELTEEEKQQI LHSEEFLSFF DHSTRIVERA LSEQINIFFD YSGRDLEDKE GEIQAGAKLS 250 260 270 280 290 300 LNRQFFDERW SKHRVVSCLD WSSQYPELLV ASYNNNEDAP HEPDGVALVW NMKYKKTTPE 310 320 330 340 350 360 YVFHCQSAVM SATFAKFHPN LVVGGTYSGQ IVLWDNRSNK RTPVQRTPLS AAAHTHPVYC 370 380 390 400 410 420 VNVVGTQNAH NLISISTDGK ICSWSLDMLS HPQDSMELVH KQSKAVAVTS MSFPVGDVNN 430 440 450 460 470 480 FVVGSEEGSV YTACRHGSKA GISEMFEGHQ GPITGIHCHA AVGAVDFSHL FVTSSFDWTV 490 500 510 520 530 540 KLWTTKNNKP LYSFEDNADY VYDVMWSPTH PALFACVDGM GRLDLWNLNN DTEVPTASIS 550 560 570 580 590 600 VEGNPALNRV RWTHSGREIA VGDSEGQIVI YDVGEQIAVP RNDEWARFGR TLAEINANRA 610 DAEEEAATRI PA
	Isoform 2E [UniParc]. Checksum: 0526BC20523DF804	FASTA	637	71,328
	10 20 30 40 50 60 MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA 70 80 90 100 110 120 EALLQSMGLT PESPIVFSEY WVPPPMSPSS KSVSTPSEAG SQDSGDGAVG SRTLHWDTDP 130 140 150 160 170 180 SVLQLHSDSD LGRGPIKLGM AKITQVDFPP REIVTYTKET QTPVMAQPKE DEEEDDDVVA 190 200 210 220 230 240 PKPPIEPEEE KTLKKDEEND SKAPPHELTE EEKQQILHSE EFLSFFDHST RIVERALSEQ 250 260 270 280 290 300 INIFFDYSGR DLEDKEGEIQ AGAKLSLNRQ FFDERWSKHR VVSCLDWSSQ YPELLVASYN 310 320 330 340 350 360 NNEDAPHEPD GVALVWNMKY KKTTPEYVFH CQSAVMSATF AKFHPNLVVG GTYSGQIVLW 370 380 390 400 410 420 DNRSNKRTPV QRTPLSAAAH THPVYCVNVV GTQNAHNLIS ISTDGKICSW SLDMLSHPQD 430 440 450 460 470 480 SMELVHKQSK AVAVTSMSFP VGDVNNFVVG SEEGSVYTAC RHGSKAGISE MFEGHQGPIT 490 500 510 520 530 540 GIHCHAAVGA VDFSHLFVTS SFDWTVKLWT TKNNKPLYSF EDNADYVYDV MWSPTHPALF 550 560 570 580 590 600 ACVDGMGRLD LWNLNNDTEV PTASISVEGN PALNRVRWTH SGREIAVGDS EGQIVIYDVG 610 620 630 EIAVPRNDEW ARFGRTLAEI NANRADAEEE AATRIPA
	Isoform 2F [UniParc]. Checksum: 9DB5032F12C11F5B	FASTA	611	68,298
	10 20 30 40 50 60 MSDKSELKAE LERKKQRLAQ IREEKKRKEE ERKKKETDQK KEAVAPVQEE SDLEKKRREA 70 80 90 100 110 120 EALLQSMGLT PESPIVPPPM SPSSKSVSTP SEAGSQDSGD GAVGSRRGPI KLGMAKITQV 130 140 150 160 170 180 DFPPREIVTY TKETQTPVMA QPKEDEEEDD DVVAPKPPIE PEEEKTLKKD EENDSKAPPH 190 200 210 220 230 240 ELTEEEKQQI LHSEEFLSFF DHSTRIVERA LSEQINIFFD YSGRDLEDKE GEIQAGAKLS 250 260 270 280 290 300 LNRQFFDERW SKHRVVSCLD WSSQYPELLV ASYNNNEDAP HEPDGVALVW NMKYKKTTPE 310 320 330 340 350 360 YVFHCQSAVM SATFAKFHPN LVVGGTYSGQ IVLWDNRSNK RTPVQRTPLS AAAHTHPVYC 370 380 390 400 410 420 VNVVGTQNAH NLISISTDGK ICSWSLDMLS HPQDSMELVH KQSKAVAVTS MSFPVGDVNN 430 440 450 460 470 480 FVVGSEEGSV YTACRHGSKA GISEMFEGHQ GPITGIHCHA AVGAVDFSHL FVTSSFDWTV 490 500 510 520 530 540 KLWTTKNNKP LYSFEDNADY VYDVMWSPTH PALFACVDGM GRLDLWNLNN DTEVPTASIS 550 560 570 580 590 600 VEGNPALNRV RWTHSGREIA VGDSEGQIVI YDVGEIAVPR NDEWARFGRT LAEINANRAD 610 AEEEAATRIP A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a new human cDNA homologous to Rattus norvegicus cytoplasmic dynein intermediate chain 2C." Huang J., Yu L., Zhao S.Y. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2C).
[2]	Li N., Wan T., Zhang M., Zhang W., Cao X. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2C AND 2F).
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C).
[4]	"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. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2A). Tissue: Brain.
[5]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C). Tissue: Endometrium and Testis.
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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. , 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].
[8]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2C). Tissue: Kidney, Skin and Testis.
[9]	"Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued." Vaughan K.T., Vallee R.B. J. Cell Biol. 131:1507-1516(1995) [PubMed: 8522607] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 82-448 (ISOFORM 2A).
[10]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 236-250, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[11]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-101, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-97, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-94; THR-95; SER-101; SER-104 AND THR-162, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[16]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87 AND SER-104, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Adenovirus transport via direct interaction of cytoplasmic dynein with the viral capsid hexon subunit." Bremner K.H., Scherer J., Yi J., Vershinin M., Gross S.P., Vallee R.B. Cell Host Microbe 6:523-535(2009) [PubMed: 20006841] [Abstract] Cited for: INTERACTION WITH HUMAN ADENOVIRUS HEXON PROTEIN.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF134477 mRNA. Translation: AAP97254.1. AF250307 mRNA. Translation: AAK37426.1. AY037160 mRNA. Translation: AAK67638.1. BT007130 mRNA. Translation: AAP35794.1. AK055491 mRNA. Translation: BAB70932.1. AL137519 mRNA. Translation: CAB70785.1. BX537412 mRNA. Translation: CAD97654.1. AC064826 Genomic DNA. No translation available. AC068039 Genomic DNA. Translation: AAY24133.1. CH471058 Genomic DNA. Translation: EAX11202.1. CH471058 Genomic DNA. Translation: EAX11204.1. CH471058 Genomic DNA. Translation: EAX11206.1. CH471058 Genomic DNA. Translation: EAX11207.1. CH471058 Genomic DNA. Translation: EAX11208.1. CH471058 Genomic DNA. Translation: EAX11209.1. BC091498 mRNA. Translation: AAH91498.1. BC109375 mRNA. Translation: AAI09376.1. BC015038 mRNA. Translation: AAH15038.1. U39575 mRNA. Translation: AAA89166.1. Sequence problems.
IPI	IPI00216348. IPI00302712. IPI00744015. IPI00827813. IPI00827859.
PIR	T46365.
RefSeq	NP_001369.1. NM_001378.1.
UniGene	Hs.546250.
3D structure databases
ProteinModelPortal	Q13409.
SMR	Q13409. Positions 136-164, 208-245, 468-602.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13409. 4 interactions.
MINT	MINT-5004520.
STRING	Q13409.
PTM databases
PhosphoSite	Q13409.
Polymorphism databases
DMDM	23503058.
2D gel databases
REPRODUCTION-2DPAGE	IPI00827813.
Proteomic databases
PRIDE	Q13409.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000397119; ENSP00000380308; ENSG00000077380. ENST00000409773; ENSP00000386415; ENSG00000077380.
GeneID	1781.
KEGG	hsa:1781.
UCSC	uc002uha.1. human. uc002uhc.2. human.
Organism-specific databases
CTD	1781.
GeneCards	GC02P172543.
H-InvDB	HIX0002589.
HGNC	HGNC:2964. DYNC1I2.
HPA	CAB033836.
MIM	603331. gene.
neXtProt	NX_Q13409.
PharmGKB	PA27435.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09255.
HOVERGEN	HBG004083.
OMA	IVFSEYW.
OrthoDB	EOG4RBQJ5.
PhylomeDB	Q13409.
Enzyme and pathway databases
Reactome	REACT_152. Cell Cycle, Mitotic.
Gene expression databases
ArrayExpress	Q13409.
Bgee	Q13409.
Genevestigator	Q13409.
GermOnline	ENSG00000077380. Homo sapiens.
Family and domain databases
InterPro	IPR015943. WD40/YVTN_repeat-like_dom. IPR001680. WD40_repeat. IPR011046. WD40_repeat-like_dom. IPR017986. WD40_repeat_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
KO	K10415.
Pfam	PF00400. WD40. 2 hits. [Graphical view]
SMART	SM00320. WD40. 5 hits. [Graphical view]
SUPFAM	SSF50978. WD40_like. 1 hit.
PROSITE	PS00678. WD_REPEATS_1. False negative. PS50082. WD_REPEATS_2. False negative. PS50294. WD_REPEATS_REGION. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	7247.
SOURCE	Search...

Entry information

Entry name

DC1I2_HUMAN

Accession

Primary (citable) accession number: Q13409
Secondary accession number(s): D3DPD4 , D3DPD5, D3DPD6, Q32LY9, Q53S84, Q5BJF8, Q7Z4X1, Q96NG7, Q96S87, Q9BXZ5, Q9NT58

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	September 19, 2002
Last modified:	January 25, 2012
This is version 123 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.