Q9H0B6 (KLC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kinesin light chain 2
Short name=KLC 2

Gene names

Name:

KLC2

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	622 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Subcellular location	Cytoplasm › cytoskeleton Probable.
Sequence similarities	Belongs to the kinesin light chain family. Contains 6 TPR repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat TPR repeat
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Traceable author statement. Source: Reactome
Cellular component	cytosol Inferred from sequence or structural similarity. Source: HGNC kinesin I complex Non-traceable author statement. Source: BHF-UCL microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	kinesin binding Inferred from sequence or structural similarity. Source: BHF-UCL microtubule motor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 622

622

Kinesin light chain 2

PRO_0000215095

Regions

Repeat

198 – 231

34

TPR 1

Repeat

240 – 273

34

TPR 2

Repeat

282 – 315

34

TPR 3

Repeat

324 – 357

34

TPR 4

Repeat

366 – 399

34

TPR 5

Repeat

449 – 482

34

TPR 6

Coiled coil

78 – 143

66

Potential

Amino acid modifications

Modified residue

445

1

Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9

Modified residue

507

1

Phosphoserine Ref.5

Modified residue

508

1

Phosphoserine Ref.5

Modified residue

582

1

Phosphoserine Ref.4 Ref.5 Ref.8 Ref.9 Ref.10

Modified residue

589

1

Phosphoserine Ref.8 Ref.9

Modified residue

610

1

Phosphoserine Ref.10

Natural variations

Natural variant

517

1

P → S.
Corresponds to variant rs2276036 [ dbSNP | Ensembl ].

VAR_020379

Experimental info

Sequence conflict

6

1

F → Y in BAB14302. Ref.2

Sequence conflict

306

1

K → R in BAB14039. Ref.2

Secondary structure

1

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622

Helix Strand Turn

Details...

Helix

217 – 231

15

Helix

237 – 252

16

Helix

256 – 273

18

Helix

279 – 291

13

Helix

298 – 315

18

Helix

321 – 335

15

Helix

340 – 357

18

Helix

363 – 378

16

Helix

382 – 400

19

Helix

411 – 420

10

Helix

446 – 454

9

Helix

458 – 461

4

Helix

465 – 476

12

Sequences

	Sequence		Length	Mass (Da)
	Q9H0B6 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 5B57ABE4DF6E396E	FASTA	622	68,935
	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

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. , 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. , 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: Cervix carcinoma.
[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: Cervix carcinoma.
[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: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[9]	"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. Tissue: Embryonic kidney.
[10]	"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: Leukemic T-cell.
[11]	"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

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.

IPI

IPI00021634.

RefSeq

NP_001128246.1. NM_001134774.1.
NP_001128247.1. NM_001134775.1.
NP_001128248.1. NM_001134776.1.
NP_073733.1. NM_022822.2.

UniGene

Hs.280792.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CEQ	X-ray	2.75	A/B	217-480	[»]
3EDT	X-ray	2.70	B/D/F/H	217-480	[»]

ProteinModelPortal

Q9H0B6.

SMR

Q9H0B6. Positions 179-607.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9H0B6. 5 interactions.

MINT

MINT-1401363.

STRING

Q9H0B6.

PTM databases

PhosphoSite

Q9H0B6.

Polymorphism databases

DMDM

13878553.

Proteomic databases

PRIDE

Q9H0B6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000316924; ENSP00000314837; ENSG00000174996.
ENST00000394067; ENSP00000377631; ENSG00000174996.
ENST00000414181; ENSP00000391680; ENSG00000174996.
ENST00000417856; ENSP00000399403; ENSG00000174996.

GeneID

64837.

KEGG

hsa:64837.

UCSC

uc001ohb.1. human.

Organism-specific databases

CTD

64837.

GeneCards

GC11P066026.

H-InvDB

HIX0201607.

HGNC

HGNC:20716. KLC2.

HPA

HPA040416.
HPA040434.

MIM

611729. gene.

neXtProt

NX_Q9H0B6.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12029.

GeneTree

ENSGT00390000006393.

HOGENOM

HBG447230.

HOVERGEN

HBG006217.

InParanoid

Q9H0B6.

OMA

AAEWSGD.

OrthoDB

EOG45MN52.

PhylomeDB

Q9H0B6.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

Q9H0B6.

Bgee

Q9H0B6.

CleanEx

HS_KLC2.

Genevestigator

Q9H0B6.

GermOnline

ENSG00000174996. Homo sapiens.

Family and domain databases

InterPro

IPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR015390. Rabaptin_Rab5-bd.
IPR001440. TPR-1.
IPR013026. TPR-contain.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]

Gene3D

G3DSA:1.25.40.10. TPR-like_helical. 2 hits.

KO

K10407.

Pfam

PF09311. Rab5-bind. 1 hit.
PF00515. TPR_1. 2 hits.
[Graphical view]

PRINTS

PR00381. KINESINLIGHT.

SMART

SM00028. TPR. 4 hits.
[Graphical view]

PROSITE

PS01160. KINESIN_LIGHT. 2 hits.
PS50005. TPR. 5 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

66920.

SOURCE

Search...

Entry information

Entry name

KLC2_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 108 of the entry and version 1 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.