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Protein

Kinesin light chain 1

Gene

KLC1

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.

GO - Molecular functioni

  • microtubule motor activity Source: InterPro
  • motor activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-2132295. MHC class II antigen presentation.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-983189. Kinesins.
SIGNORiQ07866.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin light chain 1
Short name:
KLC 1
Gene namesi
Name:KLC1
Synonyms:KLC, KNS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:6387. KLC1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic, membrane-bounded vesicle Source: UniProtKB-SubCell
  • cytosol Source: HGNC
  • growth cone Source: UniProtKB
  • kinesin complex Source: HGNC
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi521 – 5211S → A or D: No effect on motor function; when associated with A/D-524. 1 Publication
Mutagenesisi524 – 5241S → A or D: No effect on motor function; when associated with A/D-521. 1 Publication

Organism-specific databases

PharmGKBiPA162393424.

Polymorphism and mutation databases

BioMutaiKLC1.
DMDMi223590110.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 573573Kinesin light chain 1PRO_0000215092Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei449 – 4491PhosphotyrosineBy similarity
Modified residuei460 – 4601PhosphoserineBy similarity
Modified residuei521 – 5211Phosphoserine; by AMPK1 Publication
Modified residuei524 – 5241Phosphoserine; by AMPK1 Publication
Isoform P (identifier: Q07866-7)
Modified residuei547 – 5471PhosphoserineCombined sources
Modified residuei578 – 5781PhosphoserineCombined sources
Isoform N (identifier: Q07866-6)
Modified residuei591 – 5911PhosphoserineCombined sourcesCurated
Modified residuei622 – 6221PhosphoserineCombined sourcesCurated
Isoform J (identifier: Q07866-4)
Modified residuei600 – 6001PhosphoserineCombined sourcesCurated
Modified residuei631 – 6311PhosphoserineCombined sourcesCurated
Isoform I (identifier: Q07866-9)
Modified residuei600 – 6001PhosphoserineCombined sources

Post-translational modificationi

Isoform I is phosphorylated on Ser-600. Isoform J is phosphorylated on Ser-631.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ07866.
MaxQBiQ07866.
PaxDbiQ07866.
PeptideAtlasiQ07866.
PRIDEiQ07866.

2D gel databases

UCD-2DPAGEQ07866.

PTM databases

iPTMnetiQ07866.
PhosphoSiteiQ07866.
SwissPalmiQ07866.

Expressioni

Tissue specificityi

Found in a variety of tissues. Mostly abundant in brain and spine.1 Publication

Gene expression databases

BgeeiQ07866.
ExpressionAtlasiQ07866. baseline and differential.
GenevisibleiQ07866. HS.

Organism-specific databases

HPAiCAB009798.
HPA044617.
HPA052450.

Interactioni

Subunit structurei

Oligomeric complex composed of two heavy chains and two light chains. Interacts with SPAG9. Interacts with ATCAY; may link mitochondria to KLC1 and regulate mitochondria localization into neuron projections. Interacts (via TPR repeats) with TOR1A; the interaction associates TOR1A with the kinesin oligomeric complex. Interacts with adenovirus hexon-interlacing protein; this interaction leads to capsid disruption at the nuclear pore complex during virus entry into host cell.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BNIP2Q129823EBI-721019,EBI-752094
CCDC114Q96M633EBI-721019,EBI-10173858
KRT31Q153233EBI-721019,EBI-948001

Protein-protein interaction databases

BioGridi110029. 74 interactions.
DIPiDIP-40371N.
IntActiQ07866. 30 interactions.
MINTiMINT-1417975.
STRINGi9606.ENSP00000414982.

Structurei

Secondary structure

1
573
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi203 – 2053Combined sources
Helixi211 – 22515Combined sources
Helixi229 – 24719Combined sources
Beta strandi249 – 2513Combined sources
Helixi252 – 26716Combined sources
Helixi271 – 28919Combined sources
Helixi294 – 30815Combined sources
Turni309 – 3113Combined sources
Helixi313 – 33119Combined sources
Helixi336 – 35015Combined sources
Turni351 – 3533Combined sources
Helixi355 – 37117Combined sources
Helixi378 – 39417Combined sources
Helixi397 – 41620Combined sources
Helixi426 – 43510Combined sources
Helixi461 – 47717Combined sources
Helixi480 – 49415Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NF1X-ray2.80A203-497[»]
ProteinModelPortaliQ07866.
SMRiQ07866. Positions 203-495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati213 – 24634TPR 1Add
BLAST
Repeati255 – 28834TPR 2Add
BLAST
Repeati297 – 33034TPR 3Add
BLAST
Repeati339 – 37234TPR 4Add
BLAST
Repeati381 – 41434TPR 5Add
BLAST
Repeati464 – 49734TPR 6Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili27 – 156130Add
BLAST

Sequence similaritiesi

Belongs to the kinesin light chain family.Curated
Contains 6 TPR repeats.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, TPR repeat

Phylogenomic databases

eggNOGiKOG1840. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00390000006393.
HOGENOMiHOG000261663.
HOVERGENiHBG006217.
InParanoidiQ07866.
KOiK10407.
OMAiEREEHKY.
OrthoDBiEOG7TXKGD.
PhylomeDBiQ07866.
TreeFamiTF314010.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13374. TPR_10. 2 hits.
[Graphical view]
PRINTSiPR00381. KINESINLIGHT.
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS01160. KINESIN_LIGHT. 4 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]

Sequences (10)i

Sequence statusi: Complete.

This entry describes 10 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist. Has the potential to produce 285'919 splice forms.

Isoform A (identifier: Q07866-1) [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
MYDNMSTMVY IKEDKLEKLT QDEIISKTKQ VIQGLEALKN EHNSILQSLL
60 70 80 90 100
ETLKCLKKDD ESNLVEEKSN MIRKSLEMLE LGLSEAQVMM ALSNHLNAVE
110 120 130 140 150
SEKQKLRAQV RRLCQENQWL RDELANTQQK LQKSEQSVAQ LEEEKKHLEF
160 170 180 190 200
MNQLKKYDDD ISPSEDKDTD STKEPLDDLF PNDEDDPGQG IQQQHSSAAA
210 220 230 240 250
AAQQGGYEIP ARLRTLHNLV IQYASQGRYE VAVPLCKQAL EDLEKTSGHD
260 270 280 290 300
HPDVATMLNI LALVYRDQNK YKDAANLLND ALAIREKTLG KDHPAVAATL
310 320 330 340 350
NNLAVLYGKR GKYKEAEPLC KRALEIREKV LGKDHPDVAK QLNNLALLCQ
360 370 380 390 400
NQGKYEEVEY YYQRALEIYQ TKLGPDDPNV AKTKNNLASC YLKQGKFKQA
410 420 430 440 450
ETLYKEILTR AHEREFGSVD DENKPIWMHA EEREECKGKQ KDGTSFGEYG
460 470 480 490 500
GWYKACKVDS PTVTTTLKNL GALYRRQGKF EAAETLEEAA MRSRKQGLDN
510 520 530 540 550
VHKQRVAEVL NDPENMEKRR SRESLNVDVV KYESGPDGGE EVSMSVEWNG
560 570
GVSGRASFCG KRQQQQWPGR RHR
Length:573
Mass (Da):65,310
Last modified:February 10, 2009 - v2
Checksum:iA66E3915C57C2764
GO
Isoform C (identifier: Q07866-2) [UniParc]FASTAAdd to basket

Also known as: KLC1C, R, KLC1R

The sequence of this isoform differs from the canonical sequence as follows:
     551-573: GVSGRASFCGKRQQQQWPGRRHR → MRKMKLGLVN

Show »
Length:560
Mass (Da):63,816
Checksum:iFF62962AF112575C
GO
Isoform G (identifier: Q07866-3) [UniParc]FASTAAdd to basket

Also known as: KLC1G

The sequence of this isoform differs from the canonical sequence as follows:
     542-550: Missing.

Show »
Length:564
Mass (Da):64,319
Checksum:i6576A4BCFC138FA6
GO
Isoform J (identifier: Q07866-4) [UniParc]FASTAAdd to basket

Also known as: KLC1J

The sequence of this isoform differs from the canonical sequence as follows:
     551-551: G → DGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSRESEPKNPG
     552-573: VSGRASFCGKRQQQQWPGRRHR → MKRASSLNVLNVGGKAAEDRFQERNNCLADSRALSASHTDLAH

Show »
Length:637
Mass (Da):71,996
Checksum:iDCCD9D3E561F7A23
GO
Isoform K (identifier: Q07866-5) [UniParc]FASTAAdd to basket

Also known as: KLC1K

The sequence of this isoform differs from the canonical sequence as follows:
     551-551: G → DGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSRESEPKNPG

Show »
Length:616
Mass (Da):69,967
Checksum:i40C895F6BAC6EC56
GO
Isoform N (identifier: Q07866-6) [UniParc]FASTAAdd to basket

Also known as: KLC1N

The sequence of this isoform differs from the canonical sequence as follows:
     542-550: Missing.
     551-551: G → DGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSRESEPKNPG
     552-573: VSGRASFCGKRQQQQWPGRRHR → MKRASSLNVLNVGGKAAEDRFQERNNCLADSRALSASHTDLAH

Show »
Length:628
Mass (Da):71,006
Checksum:iDA665C9E7DCC89D9
GO
Isoform P (identifier: Q07866-7) [UniParc]FASTAAdd to basket

Also known as: KLC1P

The sequence of this isoform differs from the canonical sequence as follows:
     542-573: VSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR → MKRASSLNVLNVGGKAAEDRFQERNNCLADSRALSASHTDLAH

Show »
Length:584
Mass (Da):66,292
Checksum:i7E92734C1FB43CDA
GO
Isoform S (identifier: Q07866-8) [UniParc]FASTAAdd to basket

Also known as: KLC1S, Q, KLC1Q

The sequence of this isoform differs from the canonical sequence as follows:
     542-550: Missing.
     551-573: GVSGRASFCGKRQQQQWPGRRHR → MRKMKLGLVN

Show »
Length:551
Mass (Da):62,826
Checksum:i8754DC7FBB75E8C3
GO
Isoform I (identifier: Q07866-9) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     550-550: G → GDGTGSLKRSGSFSKLRASIRRSSEKLVRKLKGGSSRESEPKNPGMKRASSLNVLNVGGKAAEDRFQ

Show »
Length:639
Mass (Da):72,398
Checksum:i5EA25AF4C9ECDFFC
GO
Isoform D (identifier: Q07866-10) [UniParc]FASTAAdd to basket

Also known as: KLC1D

The sequence of this isoform differs from the canonical sequence as follows:
     551-573: GVSGRASFCGKRQQQQWPGRRHR → DGTGSLKRSG...SSGLEDATAN

Show »
Length:618
Mass (Da):69,765
Checksum:i18C502E6C345E222
GO

Sequence cautioni

The sequence AAA16576.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAF72543.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAO62549.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence DAA01265.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence DAA01266.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence DAA01268.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence DAA01289.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence DAA01291.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence DAA01292.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence DAA01295.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence DAA01296.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence DAA01297.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41N → T in AAA16576 (PubMed:8274221).Curated
Sequence conflicti4 – 41N → T in AAO62548 (PubMed:12839500).Curated
Sequence conflicti4 – 41N → T in AAO62549 (PubMed:12839500).Curated
Sequence conflicti4 – 41N → T in AAO62550 (PubMed:12839500).Curated
Sequence conflicti4 – 41N → T in AAO62551 (PubMed:12839500).Curated
Sequence conflicti4 – 41N → T in AAO62553 (PubMed:12839500).Curated
Sequence conflicti4 – 41N → T in AAO62552 (PubMed:12839500).Curated
Sequence conflicti4 – 41N → T in AAO62554 (PubMed:12839500).Curated
Sequence conflicti4 – 41N → T in AAO62555 (PubMed:12839500).Curated
Sequence conflicti4 – 41N → T in AAO64641 (PubMed:12839500).Curated
Sequence conflicti4 – 41N → T in AAF72543 (Ref. 3) Curated
Isoform N (identifier: Q07866-6)
Sequence conflicti622 – 6221S → T in AAO62551 (PubMed:12839500).Combined sourcesCurated
Isoform J (identifier: Q07866-4)
Sequence conflicti631 – 6311S → T in AAO62555 (PubMed:12839500).Combined sourcesCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei542 – 57332VSMSV…GRRHR → MKRASSLNVLNVGGKAAEDR FQERNNCLADSRALSASHTD LAH in isoform P. 1 PublicationVSP_008021Add
BLAST
Alternative sequencei542 – 5509Missing in isoform G, isoform N and isoform S. 1 PublicationVSP_008017
Alternative sequencei550 – 5501G → GDGTGSLKRSGSFSKLRASI RRSSEKLVRKLKGGSSRESE PKNPGMKRASSLNVLNVGGK AAEDRFQ in isoform I. 1 PublicationVSP_023323
Alternative sequencei551 – 57323GVSGR…GRRHR → MRKMKLGLVN in isoform C and isoform S. 2 PublicationsVSP_008018Add
BLAST
Alternative sequencei551 – 57323GVSGR…GRRHR → DGTGSLKRSGSFSKLRASIR RSSEKLVRKLKGGSSRESEP KNPGASLAEPLFVENDSSSS GLEDATAN in isoform D. 1 PublicationVSP_046424Add
BLAST
Alternative sequencei551 – 5511G → DGTGSLKRSGSFSKLRASIR RSSEKLVRKLKGGSSRESEP KNPG in isoform J, isoform K and isoform N. 1 PublicationVSP_008019
Alternative sequencei552 – 57322VSGRA…GRRHR → MKRASSLNVLNVGGKAAEDR FQERNNCLADSRALSASHTD LAH in isoform J and isoform N. 1 PublicationVSP_008020Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04733 mRNA. Translation: AAA16576.1. Different initiation.
AY180163 mRNA. Translation: AAO62548.1.
AY180164 mRNA. Translation: AAO62549.1. Different initiation.
AY180165 mRNA. Translation: AAO62550.1.
AY180166 mRNA. Translation: AAO62551.1.
AY180168 mRNA. Translation: AAO62553.1.
AY180167 mRNA. Translation: AAO62552.1.
AY180169 mRNA. Translation: AAO62554.1.
AY180170 mRNA. Translation: AAO62555.1.
AY244715 mRNA. Translation: AAO64641.1.
AF267530
, AF267518, AF267519, AF267520, AF267521, AF267522, AF267523, AF267524, AF267525, AF267526, AF267527, AF267528, AF267529 Genomic DNA. Translation: AAF72543.1. Different initiation.
AL049840 Genomic DNA. No translation available.
AL139300 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81834.1.
BC008881 mRNA. Translation: AAH08881.1.
BK000681 mRNA. Translation: DAA01265.1. Different initiation.
BK000682 mRNA. Translation: DAA01266.1. Different initiation.
BK000684 mRNA. Translation: DAA01268.1. Different initiation.
BK001163 mRNA. Translation: DAA01289.1. Different initiation.
BK001165 mRNA. Translation: DAA01291.1. Different initiation.
BK001166 mRNA. Translation: DAA01292.1. Different initiation.
BK001169 mRNA. Translation: DAA01295.1. Different initiation.
BK001170 mRNA. Translation: DAA01296.1. Different initiation.
BK001171 mRNA. Translation: DAA01297.1. Different initiation.
CCDSiCCDS32165.1. [Q07866-2]
CCDS41996.1. [Q07866-1]
CCDS45168.1. [Q07866-10]
PIRiI53013.
RefSeqiNP_001123579.1. NM_001130107.1. [Q07866-10]
NP_005543.2. NM_005552.4. [Q07866-2]
NP_891553.2. NM_182923.3. [Q07866-1]
UniGeneiHs.20107.
Hs.657678.

Genome annotation databases

EnsembliENST00000246489; ENSP00000246489; ENSG00000126214. [Q07866-4]
ENST00000334553; ENSP00000334523; ENSG00000126214. [Q07866-9]
ENST00000347839; ENSP00000334618; ENSG00000126214. [Q07866-6]
ENST00000348520; ENSP00000341154; ENSG00000126214. [Q07866-1]
ENST00000389744; ENSP00000374394; ENSG00000126214. [Q07866-2]
ENST00000452929; ENSP00000414982; ENSG00000126214. [Q07866-10]
ENST00000553286; ENSP00000452487; ENSG00000126214. [Q07866-2]
ENST00000554228; ENSP00000450616; ENSG00000126214. [Q07866-2]
ENST00000557450; ENSP00000450648; ENSG00000126214. [Q07866-3]
ENST00000634686; ENSP00000488938; ENSG00000126214. [Q07866-7]
GeneIDi3831.
KEGGihsa:3831.
UCSCiuc001ynm.2. human. [Q07866-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04733 mRNA. Translation: AAA16576.1. Different initiation.
AY180163 mRNA. Translation: AAO62548.1.
AY180164 mRNA. Translation: AAO62549.1. Different initiation.
AY180165 mRNA. Translation: AAO62550.1.
AY180166 mRNA. Translation: AAO62551.1.
AY180168 mRNA. Translation: AAO62553.1.
AY180167 mRNA. Translation: AAO62552.1.
AY180169 mRNA. Translation: AAO62554.1.
AY180170 mRNA. Translation: AAO62555.1.
AY244715 mRNA. Translation: AAO64641.1.
AF267530
, AF267518, AF267519, AF267520, AF267521, AF267522, AF267523, AF267524, AF267525, AF267526, AF267527, AF267528, AF267529 Genomic DNA. Translation: AAF72543.1. Different initiation.
AL049840 Genomic DNA. No translation available.
AL139300 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81834.1.
BC008881 mRNA. Translation: AAH08881.1.
BK000681 mRNA. Translation: DAA01265.1. Different initiation.
BK000682 mRNA. Translation: DAA01266.1. Different initiation.
BK000684 mRNA. Translation: DAA01268.1. Different initiation.
BK001163 mRNA. Translation: DAA01289.1. Different initiation.
BK001165 mRNA. Translation: DAA01291.1. Different initiation.
BK001166 mRNA. Translation: DAA01292.1. Different initiation.
BK001169 mRNA. Translation: DAA01295.1. Different initiation.
BK001170 mRNA. Translation: DAA01296.1. Different initiation.
BK001171 mRNA. Translation: DAA01297.1. Different initiation.
CCDSiCCDS32165.1. [Q07866-2]
CCDS41996.1. [Q07866-1]
CCDS45168.1. [Q07866-10]
PIRiI53013.
RefSeqiNP_001123579.1. NM_001130107.1. [Q07866-10]
NP_005543.2. NM_005552.4. [Q07866-2]
NP_891553.2. NM_182923.3. [Q07866-1]
UniGeneiHs.20107.
Hs.657678.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NF1X-ray2.80A203-497[»]
ProteinModelPortaliQ07866.
SMRiQ07866. Positions 203-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110029. 74 interactions.
DIPiDIP-40371N.
IntActiQ07866. 30 interactions.
MINTiMINT-1417975.
STRINGi9606.ENSP00000414982.

PTM databases

iPTMnetiQ07866.
PhosphoSiteiQ07866.
SwissPalmiQ07866.

Polymorphism and mutation databases

BioMutaiKLC1.
DMDMi223590110.

2D gel databases

UCD-2DPAGEQ07866.

Proteomic databases

EPDiQ07866.
MaxQBiQ07866.
PaxDbiQ07866.
PeptideAtlasiQ07866.
PRIDEiQ07866.

Protocols and materials databases

DNASUi3831.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000246489; ENSP00000246489; ENSG00000126214. [Q07866-4]
ENST00000334553; ENSP00000334523; ENSG00000126214. [Q07866-9]
ENST00000347839; ENSP00000334618; ENSG00000126214. [Q07866-6]
ENST00000348520; ENSP00000341154; ENSG00000126214. [Q07866-1]
ENST00000389744; ENSP00000374394; ENSG00000126214. [Q07866-2]
ENST00000452929; ENSP00000414982; ENSG00000126214. [Q07866-10]
ENST00000553286; ENSP00000452487; ENSG00000126214. [Q07866-2]
ENST00000554228; ENSP00000450616; ENSG00000126214. [Q07866-2]
ENST00000557450; ENSP00000450648; ENSG00000126214. [Q07866-3]
ENST00000634686; ENSP00000488938; ENSG00000126214. [Q07866-7]
GeneIDi3831.
KEGGihsa:3831.
UCSCiuc001ynm.2. human. [Q07866-1]

Organism-specific databases

CTDi3831.
GeneCardsiKLC1.
HGNCiHGNC:6387. KLC1.
HPAiCAB009798.
HPA044617.
HPA052450.
MIMi600025. gene.
neXtProtiNX_Q07866.
PharmGKBiPA162393424.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1840. Eukaryota.
COG0457. LUCA.
GeneTreeiENSGT00390000006393.
HOGENOMiHOG000261663.
HOVERGENiHBG006217.
InParanoidiQ07866.
KOiK10407.
OMAiEREEHKY.
OrthoDBiEOG7TXKGD.
PhylomeDBiQ07866.
TreeFamiTF314010.

Enzyme and pathway databases

ReactomeiR-HSA-2132295. MHC class II antigen presentation.
R-HSA-5625970. RHO GTPases activate KTN1.
R-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-983189. Kinesins.
SIGNORiQ07866.

Miscellaneous databases

ChiTaRSiKLC1. human.
GeneWikiiKLC1.
GenomeRNAii3831.
PROiQ07866.
SOURCEiSearch...

Gene expression databases

BgeeiQ07866.
ExpressionAtlasiQ07866. baseline and differential.
GenevisibleiQ07866. HS.

Family and domain databases

Gene3Di1.25.40.10. 1 hit.
InterProiIPR002151. Kinesin_light.
IPR015792. Kinesin_light_repeat.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical_dom.
IPR019734. TPR_repeat.
[Graphical view]
PfamiPF13374. TPR_10. 2 hits.
[Graphical view]
PRINTSiPR00381. KINESINLIGHT.
SMARTiSM00028. TPR. 5 hits.
[Graphical view]
SUPFAMiSSF48452. SSF48452. 3 hits.
PROSITEiPS01160. KINESIN_LIGHT. 4 hits.
PS50005. TPR. 6 hits.
PS50293. TPR_REGION. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and genetic characterization of the human kinesin light-chain (KLC) gene."
    Cabeza-Arvelaiz Y., Shih L.-C.N., Hardman N., Asselbergs F., Bilbe G., Schmitz A., White B., Siciliano M.J., Lachman L.B.
    DNA Cell Biol. 12:881-892(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  2. "Alternatively spliced products of the human kinesin light chain 1 (KNS2) gene."
    McCart A.E., Mahony D., Rothnagel J.A.
    Traffic 4:576-580(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; C; D; G; I; P AND S), NUCLEOTIDE SEQUENCE [MRNA] OF 444-573 (ISOFORMS J; K AND N).
    Tissue: Brain, Foreskin and Liver.
  3. Gerber S., Rozet J.-M., Perrault I., Ducroq D., Souied E., Munnich A., Kaplan J.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 C).
    Tissue: Uterus.
  7. "The early onset dystonia protein torsinA interacts with kinesin light chain 1."
    Kamm C., Boston H., Hewett J., Wilbur J., Corey D.P., Hanson P.I., Ramesh V., Breakefield X.O.
    J. Biol. Chem. 279:19882-19892(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH TOR1A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "Cell-wide analysis of secretory granule dynamics in three dimensions in living pancreatic beta-cells: evidence against a role for AMPK-dependent phosphorylation of KLC1 at Ser517/Ser520 in glucose-stimulated insulin granule movement."
    McDonald A., Fogarty S., Leclerc I., Hill E.V., Hardie D.G., Rutter G.A.
    Biochem. Soc. Trans. 38:205-208(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-521 AND SER-524, MUTAGENESIS OF SER-521 AND SER-524.
  14. "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-600 (ISOFORMS I AND J), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 (ISOFORM J), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591 AND SER-622 (ISOFORM N), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-578 (ISOFORM P), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Kinesin-1-mediated capsid disassembly and disruption of the nuclear pore complex promote virus infection."
    Strunze S., Engelke M.F., Wang I.H., Puntener D., Boucke K., Schleich S., Way M., Schoenenberger P., Burckhardt C.J., Greber U.F.
    Cell Host Microbe 10:210-223(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ADENOVIRUS HEXON-INTERLACING PROTEIN.
  16. "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-600 (ISOFORMS I AND J), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631 (ISOFORM J), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591 AND SER-622 (ISOFORM N), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 AND SER-578 (ISOFORM P), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 (ISOFORMS I AND J), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-591 (ISOFORM N), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547 (ISOFORM P), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Crystal structure of the TPR domain of kinesin light chain 1."
    Structural genomics consortium (SGC)
    Submitted (MAY-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 205-497.

Entry informationi

Entry nameiKLC1_HUMAN
AccessioniPrimary (citable) accession number: Q07866
Secondary accession number(s): A6NF62
, F8VTM4, Q7RTM2, Q7RTM3, Q7RTM5, Q7RTP9, Q7RTQ3, Q7RTQ5, Q7RTQ6, Q86SF5, Q86TF5, Q86V74, Q86V75, Q86V76, Q86V77, Q86V78, Q86V79, Q96H62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: February 10, 2009
Last modified: July 6, 2016
This is version 165 of the entry and version 2 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

Caution

It is uncertain whether Met-1 or Met-5 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.