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O43237

- DC1L2_HUMAN

UniProt

O43237 - DC1L2_HUMAN

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Protein

Cytoplasmic dynein 1 light intermediate chain 2

Gene
DYNC1LI2, DNCLI2, LIC2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. May play a role in binding dynein to membranous organelles or chromosomes.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 688ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. microtubule motor activity Source: InterPro

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. centrosome localization Source: Ensembl
  3. microtubule-based movement Source: InterPro
  4. microtubule cytoskeleton organization Source: Ensembl
  5. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic dynein 1 light intermediate chain 2
Alternative name(s):
Dynein light intermediate chain 2, cytosolic
Short name:
LIC-2
LIC53/55
Gene namesi
Synonyms:DNCLI2, LIC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:2966. DYNC1LI2.

Subcellular locationi

Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasmic dynein complex Source: ProtInc
  3. cytosol Source: Reactome
  4. microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27438.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Cytoplasmic dynein 1 light intermediate chain 2PRO_0000114670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941Phosphoserine5 Publications
Modified residuei383 – 3831Phosphoserine1 Publication
Modified residuei391 – 3911Phosphoserine1 Publication
Modified residuei441 – 4411Phosphothreonine1 Publication
Modified residuei443 – 4431Phosphoserine2 Publications
Modified residuei446 – 4461Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43237.
PaxDbiO43237.
PeptideAtlasiO43237.
PRIDEiO43237.

PTM databases

PhosphoSiteiO43237.

Expressioni

Gene expression databases

ArrayExpressiO43237.
BgeeiO43237.
CleanExiHS_DYNC1LI2.
GenevestigatoriO43237.

Interactioni

Subunit structurei

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. Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1 By similarity.

Protein-protein interaction databases

BioGridi108120. 26 interactions.
IntActiO43237. 9 interactions.
MINTiMINT-2999261.
STRINGi9606.ENSP00000258198.

Structurei

3D structure databases

ProteinModelPortaliO43237.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG265404.
HOGENOMiHOG000236263.
HOVERGENiHBG005546.
InParanoidiO43237.
KOiK10416.
OMAiNIHDEDR.
OrthoDBiEOG7V7668.
PhylomeDBiO43237.
TreeFamiTF352602.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR008467. Dynein1_light_intermed_chain.
IPR022780. Dynein_light_int_chain.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR12688. PTHR12688. 1 hit.
PfamiPF05783. DLIC. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O43237-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRARSK    50
LPSGKNILVF GEDGSGKTTL MTKLQGAEHG KKGRGLEYLY LSVHDEDRDD 100
HTRCNVWILD GDLYHKGLLK FAVSAESLPE TLVIFVADMS RPWTVMESLQ 150
KWASVLREHI DKMKIPPEKM RELERKFVKD FQDYMEPEEG CQGSPQRRGP 200
LTSGSDEENV ALPLGDNVLT HNLGIPVLVV CTKCDAVSVL EKEHDYRDEH 250
LDFIQSHLRR FCLQYGAALI YTSVKEEKNL DLLYKYIVHK TYGFHFTTPA 300
LVVEKDAVFI PAGWDNEKKI AILHENFTTV KPEDAYEDFI VKPPVRKLVH 350
DKELAAEDEQ VFLMKQQSLL AKQPATPTRA SESPARGPSG SPRTQGRGGP 400
ASVPSSSPGT SVKKPDPNIK NNAASEGVLA SFFNSLLSKK TGSPGSPGAG 450
GVQSTAKKSG QKTVLSNVQE ELDRMTRKPD SMVTNSSTEN EA 492
Length:492
Mass (Da):54,099
Last modified:June 1, 1998 - v1
Checksum:iAF7B4E49E3983DCC
GO
Isoform 2 (identifier: O43237-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     100-177: DHTRCNVWIL...EKMRELERKF → V

Note: No experimental confirmation available.

Show »
Length:415
Mass (Da):45,005
Checksum:i758F32BAD4482709
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei100 – 17778DHTRC…LERKF → V in isoform 2. VSP_054663Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti458 – 4581K → N in AAH25959. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF035812 mRNA. Translation: AAB88513.1.
AK291766 mRNA. Translation: BAF84455.1.
AK303031 mRNA. Translation: BAG64156.1.
AC018557 Genomic DNA. No translation available.
AC044802 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83039.1.
BC025959 mRNA. Translation: AAH25959.1.
CCDSiCCDS10818.1. [O43237-1]
CCDS67049.1. [O43237-2]
RefSeqiNP_001273086.1. NM_001286157.1. [O43237-2]
NP_006132.1. NM_006141.2. [O43237-1]
UniGeneiHs.369068.

Genome annotation databases

EnsembliENST00000258198; ENSP00000258198; ENSG00000135720.
ENST00000443351; ENSP00000394289; ENSG00000135720.
GeneIDi1783.
KEGGihsa:1783.
UCSCiuc002eqb.1. human. [O43237-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF035812 mRNA. Translation: AAB88513.1 .
AK291766 mRNA. Translation: BAF84455.1 .
AK303031 mRNA. Translation: BAG64156.1 .
AC018557 Genomic DNA. No translation available.
AC044802 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83039.1 .
BC025959 mRNA. Translation: AAH25959.1 .
CCDSi CCDS10818.1. [O43237-1 ]
CCDS67049.1. [O43237-2 ]
RefSeqi NP_001273086.1. NM_001286157.1. [O43237-2 ]
NP_006132.1. NM_006141.2. [O43237-1 ]
UniGenei Hs.369068.

3D structure databases

ProteinModelPortali O43237.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108120. 26 interactions.
IntActi O43237. 9 interactions.
MINTi MINT-2999261.
STRINGi 9606.ENSP00000258198.

PTM databases

PhosphoSitei O43237.

Proteomic databases

MaxQBi O43237.
PaxDbi O43237.
PeptideAtlasi O43237.
PRIDEi O43237.

Protocols and materials databases

DNASUi 1783.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258198 ; ENSP00000258198 ; ENSG00000135720 .
ENST00000443351 ; ENSP00000394289 ; ENSG00000135720 .
GeneIDi 1783.
KEGGi hsa:1783.
UCSCi uc002eqb.1. human. [O43237-1 ]

Organism-specific databases

CTDi 1783.
GeneCardsi GC16M066754.
HGNCi HGNC:2966. DYNC1LI2.
MIMi 611406. gene.
neXtProti NX_O43237.
PharmGKBi PA27438.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG265404.
HOGENOMi HOG000236263.
HOVERGENi HBG005546.
InParanoidi O43237.
KOi K10416.
OMAi NIHDEDR.
OrthoDBi EOG7V7668.
PhylomeDBi O43237.
TreeFami TF352602.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.

Miscellaneous databases

ChiTaRSi DYNC1LI2. human.
GeneWikii DYNC1LI2.
GenomeRNAii 1783.
NextBioi 35476533.
PROi O43237.
SOURCEi Search...

Gene expression databases

ArrayExpressi O43237.
Bgeei O43237.
CleanExi HS_DYNC1LI2.
Genevestigatori O43237.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR008467. Dynein1_light_intermed_chain.
IPR022780. Dynein_light_int_chain.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR12688. PTHR12688. 1 hit.
Pfami PF05783. DLIC. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Zha D., Hu G.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Placenta and Testis.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1).
    Tissue: Uterus.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-383; SER-443 AND SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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-194; SER-391; THR-441; SER-443 AND SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDC1L2_HUMAN
AccessioniPrimary (citable) accession number: O43237
Secondary accession number(s): A8K6V1, B4DZP4, Q8TAT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 1, 1998
Last modified: September 3, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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