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Reviewed, UniProtKB/Swiss-Prot Q9H0B6 (KLC2_HUMAN)

Last modified February 9, 2010. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kinesin light chain 2
      Short name=KLC 2
Gene names
Name: KLC2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity By similarity.

Subunit structure

Oligomeric complex composed of two heavy chains and two light chains By similarity.

Sequence similarities

Belongs to the kinesin light chain family.

Contains 6 TPR repeats.

Ontologies

Keywords
   Cellular componentMicrotubule
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Repeat
TPR repeat
   Molecular functionMotor protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Cellular componentcytosol

Inferred from sequence or structural similarity. Source: HGNC

kinesin complex

Inferred from sequence or structural similarity. Source: HGNC

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmicrotubule motor activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YWHAGP619811EBI-726994,EBI-359832
YWHAQP273481EBI-726994,EBI-359854

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Kinesin light chain 2
PRO_0000215095

Regions

Repeat198 – 23134TPR 1
Repeat240 – 27334TPR 2
Repeat282 – 31534TPR 3
Repeat324 – 35734TPR 4
Repeat366 – 39934TPR 5
Repeat449 – 48234TPR 6
Coiled coil78 – 14366 Potential

Amino acid modifications

Modified residue4451Phosphoserine Ref.6 Ref.7 Ref.8 Ref.10
Modified residue5071Phosphoserine Ref.5
Modified residue5081Phosphoserine Ref.5
Modified residue5821Phosphoserine Ref.8 Ref.10 Ref.5 Ref.4 Ref.11
Modified residue5891Phosphoserine Ref.8 Ref.10
Modified residue6101Phosphoserine Ref.11

Natural variations

Natural variant5171P → S: dbSNP rs2276036.
VAR_020379

Experimental info

Sequence conflict61F → Y in BAB14302. Ref.2
Sequence conflict3061K → R in BAB14039. Ref.2

Secondary structure

........................... 622
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9H0B6-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 5B57ABE4DF6E396E

FASTA62268,935
        10         20         30         40         50         60 
MAMMVFPREE KLSQDEIVLG TKAVIQGLET LRGEHRALLA PLVAPEAGEA EPGSQERCIL 

        70         80         90        100        110        120 
LRRSLEAIEL GLGEAQVILA LSSHLGAVES EKQKLRAQVR RLVQENQWLR EELAGTQQKL 

       130        140        150        160        170        180 
QRSEQAVAQL EEEKQHLLFM SQIRKLDEDA SPNEEKGDVP KDTLDDLFPN EDEQSPAPSP 

       190        200        210        220        230        240 
GGGDVSGQHG GYEIPARLRT LHNLVIQYAS QGRYEVAVPL CKQALEDLEK TSGHDHPDVA 

       250        260        270        280        290        300 
TMLNILALVY RDQNKYKEAA HLLNDALAIR EKTLGKDHPA VAATLNNLAV LYGKRGKYKE 

       310        320        330        340        350        360 
AEPLCKRALE IREKVLGKFH PDVAKQLSNL ALLCQNQGKA EEVEYYYRRA LEIYATRLGP 

       370        380        390        400        410        420 
DDPNVAKTKN NLASCYLKQG KYQDAETLYK EILTRAHEKE FGSVNGDNKP IWMHAEEREE 

       430        440        450        460        470        480 
SKDKRRDSAP YGEYGSWYKA CKVDSPTVNT TLRSLGALYR RQGKLEAAHT LEDCASRNRK 

       490        500        510        520        530        540 
QGLDPASQTK VVELLKDGSG RRGDRRSSRD MAGGAGPRSE SDLEDVGPTA EWNGDGSGSL 

       550        560        570        580        590        600 
RRSGSFGKLR DALRRSSEML VKKLQGGTPQ EPPNPRMKRA SSLNFLNKSV EEPTQPGGTG 

       610        620 
LSDSRTLSSS SMDLSRRSSL VG 

« Hide

References

[1]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[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. 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary gland and Testis.
[3]"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].
Tissue: Lymph.
[4]"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-582, MASS SPECTROMETRY.
Tissue: Epithelium.
[5]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-507; SER-508 AND SER-582, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, MASS SPECTROMETRY.
[8]"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-445; SER-582 AND SER-589, MASS SPECTROMETRY.
[9]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-582 AND SER-589, MASS SPECTROMETRY.
[11]"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-582 AND SER-610, MASS SPECTROMETRY.
Tissue: T-cell.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL136864 mRNA. Translation: CAB66798.1.
AK022449 mRNA. Translation: BAB14039.1.
AK022907 mRNA. Translation: BAB14302.1.
AK315725 mRNA. Translation: BAG38081.1.
BC034373 mRNA. Translation: AAH34373.1.
IPIIPI00021634.
RefSeqNP_001128246.1.
NP_001128247.1.
NP_001128248.1.
NP_073733.1.
UniGeneHs.280792

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CEQX-ray2.75A/B217-480[»]
3EDTX-ray2.70B/D/F/H217-480[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9H0B6. 5 interactions.
STRINGQ9H0B6.

PTM databases

PhosphoSiteQ9H0B6.

Proteomic databases

PRIDEQ9H0B6.

Genome annotation databases

EnsemblENST00000316924; ENSP00000314837; ENSG00000174996; Homo sapiens. [Genome view]
ENST00000394067; ENSP00000377631; ENSG00000174996; Homo sapiens. [Genome view]
ENST00000414181; ENSP00000391680; ENSG00000174996; Homo sapiens. [Genome view]
ENST00000417856; ENSP00000399403; ENSG00000174996; Homo sapiens. [Genome view]
GeneID64837.
KEGGhsa:64837.
UCSCuc001ohb.1. human.

Organism-specific databases

CTD64837.
GeneCardsGC11P065781.
GC11P065782.
H-InvDBHIX0009825.
HGNCHGNC:20716. KLC2.
MIM611729. gene.
PharmGKBPA142671587.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12029.
HOGENOMHBG447230.
HOVERGENQ9H0B6.
InParanoidQ9H0B6.
OMAPAAEWSG.
OrthoDBEOG9J6VBF.
PhylomeDBQ9H0B6.

Gene expression databases

ArrayExpressQ9H0B6.
BgeeQ9H0B6.
CleanExHS_KLC2.
GenevestigatorQ9H0B6.
GermOnlineENSG00000174996. Homo sapiens.

Family and domain databases

InterProIPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR015390. Rabaptin_Rab5-bd.
IPR013026. TPR-contain.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PfamPF09311. Rab5-bind. 1 hit.
[Graphical view]
PRINTSPR00381. KINESINLIGHT.
SMARTSM00028. TPR. 4 hits.
[Graphical view]
PROSITEPS01160. KINESIN_LIGHT. 2 hits.
PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio66920.
SOURCESearch...

Entry information

Entry nameKLC2_HUMAN
AccessionPrimary (citable) accession number: Q9H0B6
Secondary accession number(s): B2RDY4, Q9H9C8, Q9HA20
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: March 1, 2001
Last modified: February 9, 2010
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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List of human entries with polymorphisms or disease mutations

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Index of human polymorphisms and disease mutations

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents