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Reviewed, UniProtKB/Swiss-Prot Q9NSK0 (KLC4_HUMAN)

Last modified July 7, 2009. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kinesin light chain 4
      Short name=KLC 4
Alternative name(s):
    Kinesin-like protein 8
Gene names
Name: KLC4
Synonyms: KNSL8
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 7 TPR repeats.

Ontologies

Keywords
   Cellular componentMicrotubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
TPR repeat
   Molecular functionMotor protein
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Cellular componentkinesin complex

Inferred from electronic annotation. Source: InterPro

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NSK0-1)

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 2 (identifier: Q9NSK0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-87: Missing.
     419-422: DDHK → EPAP
     423-619: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 619619Kinesin light chain 4
PRO_0000215097

Regions

Repeat55 – 8834TPR 1
Repeat211 – 24434TPR 2
Repeat253 – 28634TPR 3
Repeat295 – 32834TPR 4
Repeat337 – 37034TPR 5
Repeat379 – 41234TPR 6
Repeat464 – 49734TPR 7
Coiled coil32 – 150119 Potential

Amino acid modifications

Modified residue741Phosphoserine Ref.6
Modified residue831Phosphoserine Ref.6
Modified residue931Phosphoserine Ref.6
Modified residue1001Phosphoserine Ref.6
Modified residue1741Phosphoserine By similarity
Modified residue4601Phosphoserine Ref.5 Ref.8 Ref.9
Modified residue5661Phosphoserine By similarity
Modified residue5901Phosphoserine Ref.9 Ref.7

Natural variations

Alternative sequence1 – 8787Missing in isoform 2.
VSP_021012
Alternative sequence419 – 4224DDHK → EPAP in isoform 2.
VSP_021013
Alternative sequence423 – 619197Missing in isoform 2.
VSP_021014
Natural variant721R → H: dbSNP rs11558979. Ref.1
VAR_049708

Experimental info

Sequence conflict541L → LQTIECL in BAC87179. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: 32DFC2A9A91B5574

FASTA61968,640
        10         20         30         40         50         60 
MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLEALRSEH QAVLQSLSQT IECLQQGGHE 

        70         80         90        100        110        120 
EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES EKQKLRAQVR RLCQENQWLR 

       130        140        150        160        170        180 
DELAGTQQRL QRSEQAVAQL EEEKKHLEFL GQLRQYDEDG HTSEEKEGDA TKDSLDDLFP 

       190        200        210        220        230        240 
NEEEEDPSNG LSRGQGATAA QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED 

       250        260        270        280        290        300 
LERTSGRGHP DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGPD HPAVAATLNN 

       310        320        330        340        350        360 
LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TNHPDVAKQL NNLALLCQNQ GKYEAVERYY 

       370        380        390        400        410        420 
QRALAIYEGQ LGPDNPNVAR TKNNLASCYL KQGKYAEAET LYKEILTRAH VQEFGSVDDD 

       430        440        450        460        470        480 
HKPIWMHAEE REEMSKSRHH EGGTPYAEYG GWYKACKVSS PTVNTTLRNL GALYRRQGKL 

       490        500        510        520        530        540 
EAAETLEECA LRSRRQGTDP ISQTKVAELL GESDGRRTSQ EGPGDSVKFE GGEDASVAVE 

       550        560        570        580        590        600 
WSGDGSGTLQ RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSNMKRAAS LNYLNQPSAA 

       610 
PLQVSRGLSA STMDLSSSS 

« Hide

Isoform 2.

Checksum: D2CA951E060DD9E7
Show »

FASTA33537,604

References

[1]"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] (ISOFORMS 1 AND 2), VARIANT HIS-72.
Tissue: Brain and Small intestine.
[2]"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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Amygdala and Oesophageal carcinoma.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 1).
Tissue: Prostate and Skin.
[5]"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-460, MASS SPECTROMETRY.
Tissue: Epithelium.
[6]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-83; SER-93 AND SER-100, MASS SPECTROMETRY.
[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-590, MASS SPECTROMETRY.
[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: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, MASS SPECTROMETRY.
[9]"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-460 AND SER-590, MASS SPECTROMETRY.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases

AK055293 mRNA. Translation: BAG51496.1.
AK127018 mRNA. Translation: BAC86788.1.
AK127894 mRNA. Translation: BAC87179.1.
AL162078 mRNA. Translation: CAB82411.1.
AL355385 Genomic DNA. Translation: CAI13781.1.
BC080637 mRNA. Translation: AAH80637.1.
BC103727 mRNA. Translation: AAI03728.1.
BX640717 mRNA. Translation: CAE45836.1.
IPIIPI00398812.
IPI00788630.
PIRT47147.
RefSeqNP_958929.1.
NP_958930.1.
UniGeneHs.655123

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9NSK0. 6 interactions.

PTM databases

PhosphoSiteQ9NSK0.

Proteomic databases

PRIDEQ9NSK0.

Genome annotation databases

EnsemblENSG00000137171. Homo sapiens. [Contig view]
GeneID89953.
UCSCuc003otv.1. human.

Organism-specific databases

GeneCardsGC06P043136.
HGNCHGNC:21624. KLC4.
PharmGKBPA134934134.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9NSK0.
HOVERGENQ9NSK0.

Gene expression databases

ArrayExpressQ9NSK0.
BgeeQ9NSK0.
CleanExHS_KLC4.
GermOnlineENSG00000137171. Homo sapiens.

Family and domain databases

InterProIPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR015390. Rabaptin_Rab5-bd.
IPR001440. TPR-1.
IPR011990. TPR-like_helical.
IPR013026. TPR_region.
IPR019734. TPR_repeat.
[Graphical view]
Gene3DG3DSA:1.25.40.10. TPR-like_helical. 1 hit.
PfamPF09311. Rab5-bind. 1 hit.
PF00515. TPR_1. 4 hits.
[Graphical view]
PRINTSPR00381. KINESINLIGHT.
SMARTSM00028. TPR. 4 hits.
[Graphical view]
PROSITEPS01160. KINESIN_LIGHT. 3 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio76452.

Entry information

Entry nameKLC4_HUMAN
AccessionPrimary (citable) accession number: Q9NSK0
Secondary accession number(s): B3KNY4, Q66K28
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 17, 2006
Last modified: July 7, 2009
This is version 73 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

SIMILARITY comments

Index of protein domains and families

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