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Protein

Kinesin light chain 4

Gene

KLC4

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

Functioni

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).By similarity

GO - Molecular functioni

  1. microtubule motor activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_25201. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin light chain 4
Short name:
KLC 4
Alternative name(s):
Kinesin-like protein 8
Gene namesi
Name:KLC4
Synonyms:KNSL8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:21624. KLC4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. kinesin complex Source: InterPro
  3. microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134934134.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 619618Kinesin light chain 4PRO_0000215097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei460 – 4601Phosphoserine3 Publications
Modified residuei590 – 5901Phosphoserine5 Publications
Modified residuei612 – 6121Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NSK0.
PaxDbiQ9NSK0.
PRIDEiQ9NSK0.

PTM databases

PhosphoSiteiQ9NSK0.

Expressioni

Gene expression databases

BgeeiQ9NSK0.
CleanExiHS_KLC4.
ExpressionAtlasiQ9NSK0. baseline and differential.
GenevestigatoriQ9NSK0.

Organism-specific databases

HPAiHPA030168.
HPA030169.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi124648. 40 interactions.
IntActiQ9NSK0. 4 interactions.
MINTiMINT-4999921.
STRINGi9606.ENSP00000259708.

Structurei

3D structure databases

ProteinModelPortaliQ9NSK0.
SMRiQ9NSK0. Positions 65-90, 192-495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati55 – 8834TPR 1Add
BLAST
Repeati211 – 24434TPR 2Add
BLAST
Repeati253 – 28634TPR 3Add
BLAST
Repeati295 – 32834TPR 4Add
BLAST
Repeati337 – 37034TPR 5Add
BLAST
Repeati379 – 41234TPR 6Add
BLAST
Repeati464 – 49734TPR 7Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili32 – 150119Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the kinesin light chain family.Curated
Contains 7 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, TPR repeat

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00390000006393.
HOGENOMiHOG000261663.
HOVERGENiHBG006217.
InParanoidiQ9NSK0.
KOiK10407.
OMAiMSKSRHR.
OrthoDBiEOG7TXKGD.
PhylomeDBiQ9NSK0.
TreeFamiTF314010.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR015390. Rabaptin_Rab5-bd_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF09311. Rab5-bind. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PRINTSiPR00381. KINESINLIGHT.
SMARTiSM00028. TPR. 4 hits.
[Graphical view]
PROSITEiPS01160. KINESIN_LIGHT. 3 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NSK0-1) [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

        10         20         30         40         50
MSGLVLGQRD EPAGHRLSQE EILGSTRLVS QGLEALRSEH QAVLQSLSQT
60 70 80 90 100
IECLQQGGHE EGLVHEKARQ LRRSMENIEL GLSEAQVMLA LASHLSTVES
110 120 130 140 150
EKQKLRAQVR RLCQENQWLR DELAGTQQRL QRSEQAVAQL EEEKKHLEFL
160 170 180 190 200
GQLRQYDEDG HTSEEKEGDA TKDSLDDLFP NEEEEDPSNG LSRGQGATAA
210 220 230 240 250
QQGGYEIPAR LRTLHNLVIQ YAAQGRYEVA VPLCKQALED LERTSGRGHP
260 270 280 290 300
DVATMLNILA LVYRDQNKYK EAAHLLNDAL SIRESTLGPD HPAVAATLNN
310 320 330 340 350
LAVLYGKRGK YKEAEPLCQR ALEIREKVLG TNHPDVAKQL NNLALLCQNQ
360 370 380 390 400
GKYEAVERYY QRALAIYEGQ LGPDNPNVAR TKNNLASCYL KQGKYAEAET
410 420 430 440 450
LYKEILTRAH VQEFGSVDDD HKPIWMHAEE REEMSKSRHH EGGTPYAEYG
460 470 480 490 500
GWYKACKVSS PTVNTTLRNL GALYRRQGKL EAAETLEECA LRSRRQGTDP
510 520 530 540 550
ISQTKVAELL GESDGRRTSQ EGPGDSVKFE GGEDASVAVE WSGDGSGTLQ
560 570 580 590 600
RSGSLGKIRD VLRRSSELLV RKLQGTEPRP SSSNMKRAAS LNYLNQPSAA
610
PLQVSRGLSA STMDLSSSS
Length:619
Mass (Da):68,640
Last modified:October 17, 2006 - v3
Checksum:i32DFC2A9A91B5574
GO
Isoform 2 (identifier: Q9NSK0-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-131: VMLALASHLS...ELAGTQQRLQ → NLELRGCAHL...AMPGEPVAAG
     132-619: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

Show »
Length:131
Mass (Da):13,682
Checksum:i18DB578896960243
GO
Isoform 3 (identifier: Q9NSK0-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEVTGFGVTRPGKVPQARM

Show »
Length:637
Mass (Da):70,552
Checksum:iCAA62901967C6918
GO
Isoform 4 (identifier: Q9NSK0-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     295-315: AATLNNLAVLYGKRGKYKEAE → SIPCPPHPTPRTPHHCCFGLS
     316-619: Missing.

Note: No experimental confirmation available.

Show »
Length:315
Mass (Da):35,102
Checksum:iB2F27C231C949391
GO
Isoform 5 (identifier: Q9NSK0-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-163: Missing.

Note: No experimental confirmation available.

Show »
Length:542
Mass (Da):59,640
Checksum:i85687792E15F896D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541L → LQTIECL in BAC87179. (PubMed:14702039)Curated
Sequence conflicti286 – 2861T → S in BAG51695. (PubMed:14702039)Curated
Sequence conflicti366 – 3661I → T in BAG51695. (PubMed:14702039)Curated
Sequence conflicti434 – 4341M → L in BAG52815. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721R → H.1 Publication
Corresponds to variant rs11558979 [ dbSNP | Ensembl ].
VAR_049708

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MEVTGFGVTRPGKVPQARM in isoform 3. 1 PublicationVSP_038083
Alternative sequencei87 – 16377Missing in isoform 5. 1 PublicationVSP_057231Add
BLAST
Alternative sequencei87 – 13145VMLAL…QQRLQ → NLELRGCAHLGDAGSSQPPE HSGVGETEAAGSGAAAMPGE PVAAG in isoform 2. 1 PublicationVSP_037875Add
BLAST
Alternative sequencei132 – 619488Missing in isoform 2. 1 PublicationVSP_037876Add
BLAST
Alternative sequencei295 – 31521AATLN…YKEAE → SIPCPPHPTPRTPHHCCFGL S in isoform 4. 1 PublicationVSP_043324Add
BLAST
Alternative sequencei316 – 619304Missing in isoform 4. 1 PublicationVSP_043325Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055293 mRNA. Translation: BAG51496.1.
AK056393 mRNA. Translation: BAG51695.1.
AK094102 mRNA. Translation: BAG52815.1.
AK127018 mRNA. Translation: BAC86788.1. Sequence problems.
AK127894 mRNA. Translation: BAC87179.1.
AK297433 mRNA. Translation: BAG59861.1.
AL162078 mRNA. Translation: CAB82411.1.
AL136304 Genomic DNA. No translation available.
AL355385 Genomic DNA. Translation: CAI13781.1.
CH471081 Genomic DNA. Translation: EAX04149.1.
BC012357 mRNA. Translation: AAH12357.1.
BC080637 mRNA. Translation: AAH80637.1.
BC103727 mRNA. Translation: AAI03728.1.
BX640717 mRNA. Translation: CAE45836.1.
CCDSiCCDS47429.1. [Q9NSK0-4]
CCDS4882.1. [Q9NSK0-3]
CCDS4883.1. [Q9NSK0-1]
PIRiT47147.
RefSeqiNP_001275963.1. NM_001289034.1. [Q9NSK0-1]
NP_001275964.1. NM_001289035.1. [Q9NSK0-5]
NP_612352.1. NM_138343.3. [Q9NSK0-4]
NP_958929.1. NM_201521.2. [Q9NSK0-1]
NP_958930.1. NM_201522.2. [Q9NSK0-1]
NP_958931.1. NM_201523.2. [Q9NSK0-3]
UniGeneiHs.655123.

Genome annotation databases

EnsembliENST00000259708; ENSP00000259708; ENSG00000137171. [Q9NSK0-3]
ENST00000347162; ENSP00000340221; ENSG00000137171. [Q9NSK0-1]
ENST00000394056; ENSP00000377620; ENSG00000137171. [Q9NSK0-1]
ENST00000453940; ENSP00000395806; ENSG00000137171. [Q9NSK0-5]
ENST00000458460; ENSP00000410358; ENSG00000137171. [Q9NSK0-4]
ENST00000467906; ENSP00000418759; ENSG00000137171. [Q9NSK0-2]
ENST00000479388; ENSP00000418031; ENSG00000137171. [Q9NSK0-1]
GeneIDi89953.
KEGGihsa:89953.
UCSCiuc003otu.3. human. [Q9NSK0-4]
uc003otv.1. human. [Q9NSK0-1]
uc003otw.1. human. [Q9NSK0-3]

Polymorphism databases

DMDMi116242607.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055293 mRNA. Translation: BAG51496.1.
AK056393 mRNA. Translation: BAG51695.1.
AK094102 mRNA. Translation: BAG52815.1.
AK127018 mRNA. Translation: BAC86788.1. Sequence problems.
AK127894 mRNA. Translation: BAC87179.1.
AK297433 mRNA. Translation: BAG59861.1.
AL162078 mRNA. Translation: CAB82411.1.
AL136304 Genomic DNA. No translation available.
AL355385 Genomic DNA. Translation: CAI13781.1.
CH471081 Genomic DNA. Translation: EAX04149.1.
BC012357 mRNA. Translation: AAH12357.1.
BC080637 mRNA. Translation: AAH80637.1.
BC103727 mRNA. Translation: AAI03728.1.
BX640717 mRNA. Translation: CAE45836.1.
CCDSiCCDS47429.1. [Q9NSK0-4]
CCDS4882.1. [Q9NSK0-3]
CCDS4883.1. [Q9NSK0-1]
PIRiT47147.
RefSeqiNP_001275963.1. NM_001289034.1. [Q9NSK0-1]
NP_001275964.1. NM_001289035.1. [Q9NSK0-5]
NP_612352.1. NM_138343.3. [Q9NSK0-4]
NP_958929.1. NM_201521.2. [Q9NSK0-1]
NP_958930.1. NM_201522.2. [Q9NSK0-1]
NP_958931.1. NM_201523.2. [Q9NSK0-3]
UniGeneiHs.655123.

3D structure databases

ProteinModelPortaliQ9NSK0.
SMRiQ9NSK0. Positions 65-90, 192-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124648. 40 interactions.
IntActiQ9NSK0. 4 interactions.
MINTiMINT-4999921.
STRINGi9606.ENSP00000259708.

PTM databases

PhosphoSiteiQ9NSK0.

Polymorphism databases

DMDMi116242607.

Proteomic databases

MaxQBiQ9NSK0.
PaxDbiQ9NSK0.
PRIDEiQ9NSK0.

Protocols and materials databases

DNASUi89953.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000259708; ENSP00000259708; ENSG00000137171. [Q9NSK0-3]
ENST00000347162; ENSP00000340221; ENSG00000137171. [Q9NSK0-1]
ENST00000394056; ENSP00000377620; ENSG00000137171. [Q9NSK0-1]
ENST00000453940; ENSP00000395806; ENSG00000137171. [Q9NSK0-5]
ENST00000458460; ENSP00000410358; ENSG00000137171. [Q9NSK0-4]
ENST00000467906; ENSP00000418759; ENSG00000137171. [Q9NSK0-2]
ENST00000479388; ENSP00000418031; ENSG00000137171. [Q9NSK0-1]
GeneIDi89953.
KEGGihsa:89953.
UCSCiuc003otu.3. human. [Q9NSK0-4]
uc003otv.1. human. [Q9NSK0-1]
uc003otw.1. human. [Q9NSK0-3]

Organism-specific databases

CTDi89953.
GeneCardsiGC06P043008.
HGNCiHGNC:21624. KLC4.
HPAiHPA030168.
HPA030169.
neXtProtiNX_Q9NSK0.
PharmGKBiPA134934134.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0457.
GeneTreeiENSGT00390000006393.
HOGENOMiHOG000261663.
HOVERGENiHBG006217.
InParanoidiQ9NSK0.
KOiK10407.
OMAiMSKSRHR.
OrthoDBiEOG7TXKGD.
PhylomeDBiQ9NSK0.
TreeFamiTF314010.

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_25201. Kinesins.

Miscellaneous databases

ChiTaRSiKLC4. human.
GeneWikiiKLC4.
GenomeRNAii89953.
NextBioi35473306.
PROiQ9NSK0.

Gene expression databases

BgeeiQ9NSK0.
CleanExiHS_KLC4.
ExpressionAtlasiQ9NSK0. baseline and differential.
GenevestigatoriQ9NSK0.

Family and domain databases

Gene3Di1.25.40.10. 2 hits.
InterProiIPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR015390. Rabaptin_Rab5-bd_dom.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR013105. TPR_2.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF09311. Rab5-bind. 1 hit.
PF07719. TPR_2. 1 hit.
[Graphical view]
PRINTSiPR00381. KINESINLIGHT.
SMARTiSM00028. TPR. 4 hits.
[Graphical view]
PROSITEiPS01160. KINESIN_LIGHT. 3 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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; 2; 3 AND 5), VARIANT HIS-72.
    Tissue: Adrenal gland, Brain and Small intestine.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Amygdala and Esophageal 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.
    , 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] [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] (ISOFORMS 1 AND 4).
    Tissue: Prostate and Skin.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-590, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-590, 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 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-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "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-590 AND THR-612, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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-460 AND SER-590, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(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].
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiKLC4_HUMAN
AccessioniPrimary (citable) accession number: Q9NSK0
Secondary accession number(s): B3KNY4
, B3KPI3, B3KSQ3, B4DME9, Q66K28, Q96EG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 17, 2006
Last modified: February 4, 2015
This is version 129 of the entry and version 3 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 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.