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Q13409 (DC1I2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length638 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. The intermediate chains mediate the binding of dynein to dynactin via its 150 kDa component (p150-glued) DCNT1. 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.14

Subcellular location

Cytoplasmcytoskeleton By similarity.

Post-translational modification

The phosphorylation status of Ser-90 appears to be involved in dynactin-dependent target binding By similarity.

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 processHost-virus interaction
Transport
   Cellular componentCytoplasm
Cytoskeleton
Dynein
Microtubule
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   Molecular functionMotor protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

metabolic process

Non-traceable author statement Ref.9. Source: GOC

microtubule-based movement

Non-traceable author statement Ref.9. Source: UniProtKB

mitotic cell cycle

Traceable author statement. Source: Reactome

transport

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

cytoplasm

Non-traceable author statement Ref.9. Source: UniProtKB

cytoplasmic dynein complex

Inferred from electronic annotation. Source: InterPro

cytosol

Traceable author statement. Source: Reactome

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

vesicle

Inferred from direct assay PubMed 20682791. Source: UniProtKB

   Molecular_functionmicrotubule motor activity

Non-traceable author statement Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 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.
Note: Contains a phosphoserine at position 73. Contains a phosphoserine at position 81.
Isoform 2C (identifier: Q13409-3)

The sequence of this isoform differs from the canonical sequence as follows:
     77-82: Missing.
     113-132: Missing.
Note: Contains a phosphoserine at position 73. Contains a phosphoserine at position 81.
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.
Note: Contains a phosphoserine at position 73. Contains a phosphoserine at position 81.
Isoform 3 (identifier: Q13409-7)

The sequence of this isoform differs from the canonical sequence as follows:
     76-81: VFSEYW → AEQPLRVVTADTCLFHYL
     113-132: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 638637Cytoplasmic dynein 1 intermediate chain 2
PRO_0000114655

Regions

Repeat277 – 32650WD 1
Repeat330 – 37041WD 2
Repeat379 – 42042WD 3
Repeat429 – 46941WD 4
Repeat474 – 51946WD 5
Repeat522 – 56241WD 6
Repeat568 – 60740WD 7

Amino acid modifications

Modified residue21N-acetylserine Ref.19
Modified residue901Phosphoserine By similarity
Modified residue971Phosphoserine Ref.12
Modified residue1011Phosphoserine Ref.18
Modified residue1041Phosphoserine Ref.15

Natural variations

Alternative sequence76 – 816VFSEYW → AEQPLRVVTADTCLFHYL in isoform 3.
VSP_054377
Alternative sequence77 – 826Missing in isoform 2B, isoform 2C and isoform 2F.
VSP_001336
Alternative sequence113 – 13220Missing in isoform 2C, isoform 2F and isoform 3.
VSP_001337
Alternative sequence6021Missing in isoform 2E and isoform 2F.
VSP_023011

Experimental info

Sequence conflict5101T → S in AAP97254. Ref.1
Sequence conflict5251D → G in AAP97254. Ref.1
Sequence conflict5721A → G in AAI09376. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 2A [UniParc].

Last modified September 19, 2002. Version 3.
Checksum: 2F868EC9556C47F2

FASTA63871,457
        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 

« Hide

Isoform 2B [UniParc].

Checksum: 5E643B54A2979294
Show »

FASTA63270,645
Isoform 2C [UniParc].

Checksum: 518E1D765A2CBB15
Show »

FASTA61268,426
Isoform 2E [UniParc].

Checksum: 0526BC20523DF804
Show »

FASTA63771,328
Isoform 2F [UniParc].

Checksum: 9DB5032F12C11F5B
Show »

FASTA61168,298
Isoform 3 [UniParc].

Checksum: 5C3022F6F62D9C67
Show »

FASTA63070,485

References

« Hide '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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2A AND 3).
Tissue: Brain and Thalamus.
[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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[11]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 (ISOFORMS 2B; 2C AND 2F), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS HEXON PROTEIN.
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81 (ISOFORMS 2B; 2C AND 2F), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 (ISOFORMS 2B; 2C AND 2F), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [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.
AK316119 mRNA. Translation: BAH14490.1.
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.
CCDSCCDS46450.1. [Q13409-1]
CCDS63056.1. [Q13409-3]
CCDS63057.1. [Q13409-6]
PIRT46365.
RefSeqNP_001258714.1. NM_001271785.1. [Q13409-1]
NP_001258715.1. NM_001271786.1. [Q13409-7]
NP_001258716.1. NM_001271787.1. [Q13409-7]
NP_001258717.1. NM_001271788.1. [Q13409-3]
NP_001258718.1. NM_001271789.1. [Q13409-3]
NP_001258719.1. NM_001271790.1. [Q13409-6]
NP_001369.1. NM_001378.2. [Q13409-1]
XP_005246423.1. XM_005246366.1. [Q13409-2]
XP_005246424.1. XM_005246367.1. [Q13409-2]
XP_005246426.1. XM_005246369.2. [Q13409-6]
UniGeneHs.546250.

3D structure databases

ProteinModelPortalQ13409.
SMRQ13409. Positions 136-164, 333-583.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108119. 35 interactions.
IntActQ13409. 6 interactions.
MINTMINT-5004520.

PTM databases

PhosphoSiteQ13409.

Polymorphism databases

DMDM23503058.

2D gel databases

REPRODUCTION-2DPAGEIPI00827813.

Proteomic databases

MaxQBQ13409.
PaxDbQ13409.
PRIDEQ13409.

Protocols and materials databases

DNASU1781.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263811; ENSP00000263811; ENSG00000077380. [Q13409-2]
ENST00000340296; ENSP00000339430; ENSG00000077380. [Q13409-3]
ENST00000358002; ENSP00000350692; ENSG00000077380.
ENST00000397119; ENSP00000380308; ENSG00000077380. [Q13409-1]
ENST00000409197; ENSP00000386397; ENSG00000077380. [Q13409-3]
ENST00000409317; ENSP00000386591; ENSG00000077380. [Q13409-2]
ENST00000409453; ENSP00000386886; ENSG00000077380. [Q13409-5]
ENST00000409773; ENSP00000386415; ENSG00000077380. [Q13409-1]
ENST00000508530; ENSP00000423339; ENSG00000077380. [Q13409-6]
GeneID1781.
KEGGhsa:1781.
UCSCuc002uha.2. human. [Q13409-1]
uc002uhb.2. human. [Q13409-3]
uc002uhc.4. human. [Q13409-6]
uc002uhd.2. human. [Q13409-2]

Organism-specific databases

CTD1781.
GeneCardsGC02P172543.
HGNCHGNC:2964. DYNC1I2.
HPACAB033836.
MIM603331. gene.
neXtProtNX_Q13409.
PharmGKBPA27435.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG308180.
HOVERGENHBG004083.
KOK10415.
OrthoDBEOG7FR7FX.
PhylomeDBQ13409.
TreeFamTF300553.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_6900. Immune System.
SignaLinkQ13409.

Gene expression databases

ArrayExpressQ13409.
BgeeQ13409.
GenevestigatorQ13409.

Family and domain databases

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

Other

ChiTaRSDYNC1I2. human.
GeneWikiDYNC1I2.
GenomeRNAi1781.
NextBio35480817.
PROQ13409.
SOURCESearch...

Entry information

Entry nameDC1I2_HUMAN
AccessionPrimary (citable) accession number: Q13409
Secondary accession number(s): B7ZA04 expand/collapse secondary AC list , 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: July 9, 2014
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM