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Protein

Kinesin-like protein KIF13B

Gene

KIF13B

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

Functioni

Involved in reorganization of the cortical cytoskeleton. Regulates axon formation by promoting the formation of extra axons. May be functionally important for the intracellular trafficking of MAGUKs and associated protein complexes.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi103 – 110ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • ATPase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • microtubule motor activity Source: UniProtKB
  • protein kinase binding Source: UniProtKB

GO - Biological processi

  • cytoskeleton-dependent intracellular transport Source: GO_Central
  • microtubule-based movement Source: UniProtKB
  • protein targeting Source: UniProtKB
  • regulation of axonogenesis Source: UniProtKB
  • signal transduction Source: UniProtKB
  • T cell activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:G66-31795-MONOMER.
ReactomeiR-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-983189. Kinesins.

Names & Taxonomyi

Protein namesi
Recommended name:
Kinesin-like protein KIF13B
Alternative name(s):
Kinesin-like protein GAKIN
Gene namesi
Name:KIF13B
Synonyms:GAKIN, KIAA0639
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:14405. KIF13B.

Subcellular locationi

  • Cytoplasmcytoskeleton 1 Publication
  • Cell projectionaxon 1 Publication

  • Note: accumulates at the distal part of the microtubules in the tips of axons, but not of dendrites.

GO - Cellular componenti

  • axon Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Ensembl
  • kinesin complex Source: GO_Central
  • microtubule Source: UniProtKB-KW
  • microvillus Source: Ensembl
  • paranode region of axon Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1381S → A: Abolishes phosphorylation by MARK2; when associated with A-1410. 1 Publication1
Mutagenesisi1410S → A: Abolishes phosphorylation by MARK2; when associated with A-1389. 1 Publication1

Organism-specific databases

DisGeNETi23303.
OpenTargetsiENSG00000197892.
PharmGKBiPA30099.

Polymorphism and mutation databases

BioMutaiKIF13B.
DMDMi519668668.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001254481 – 1826Kinesin-like protein KIF13BAdd BLAST1826

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei661PhosphoserineCombined sources1
Modified residuei1379PhosphoserineCombined sources1
Modified residuei1381Phosphoserine; by MARK2Combined sources1 Publication1
Modified residuei1382PhosphoserineCombined sources1
Modified residuei1391PhosphoserineCombined sources1
Modified residuei1410Phosphoserine; by MARK2Combined sources1 Publication1
Modified residuei1432PhosphoserineCombined sources1
Modified residuei1438PhosphoserineCombined sources1
Modified residuei1537PhosphoserineCombined sources1
Modified residuei1545PhosphothreonineCombined sources1
Modified residuei1559PhosphoserineCombined sources1
Modified residuei1644PhosphoserineCombined sources1
Modified residuei1797PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated at Ser-1381 and Ser-1410 by MARK2, promoting interaction with 14-3-3 and inhibiting microtubule-dependent accumulation and formation of axons.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NQT8.
MaxQBiQ9NQT8.
PaxDbiQ9NQT8.
PeptideAtlasiQ9NQT8.
PRIDEiQ9NQT8.

PTM databases

iPTMnetiQ9NQT8.
PhosphoSitePlusiQ9NQT8.
SwissPalmiQ9NQT8.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000197892.
CleanExiHS_KIF13B.
ExpressionAtlasiQ9NQT8. baseline and differential.
GenevisibleiQ9NQT8. HS.

Organism-specific databases

HPAiHPA025023.
HPA049655.

Interactioni

Subunit structurei

Binds to DLG1 and DLG4. Interacts (when phosphorylated at Ser-1381 and Ser-1410) with 14-3-3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DLG1Q12959-23EBI-766408,EBI-357500

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116895. 12 interactors.
DIPiDIP-34586N.
IntActiQ9NQT8. 6 interactors.
STRINGi9606.ENSP00000427900.

Structurei

Secondary structure

11826
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 12Combined sources7
Helixi17 – 22Combined sources6
Beta strandi28 – 31Combined sources4
Beta strandi34 – 37Combined sources4
Beta strandi54 – 57Combined sources4
Beta strandi59 – 63Combined sources5
Turni70 – 72Combined sources3
Helixi76 – 92Combined sources17
Beta strandi97 – 103Combined sources7
Helixi109 – 113Combined sources5
Beta strandi117 – 120Combined sources4
Helixi122 – 137Combined sources16
Beta strandi142 – 154Combined sources13
Beta strandi157 – 160Combined sources4
Beta strandi189 – 191Combined sources3
Helixi194 – 206Combined sources13
Beta strandi222 – 235Combined sources14
Beta strandi241 – 253Combined sources13
Helixi272 – 292Combined sources21
Helixi305 – 307Combined sources3
Helixi309 – 313Combined sources5
Helixi315 – 318Combined sources4
Beta strandi323 – 330Combined sources8
Helixi334 – 336Combined sources3
Helixi337 – 350Combined sources14
Beta strandi449 – 452Combined sources4
Turni457 – 460Combined sources4
Beta strandi464 – 466Combined sources3
Beta strandi469 – 476Combined sources8
Beta strandi480 – 482Combined sources3
Beta strandi493 – 497Combined sources5
Beta strandi503 – 507Combined sources5
Beta strandi513 – 515Combined sources3
Beta strandi524 – 526Combined sources3
Beta strandi531 – 534Combined sources4
Turni535 – 537Combined sources3
Beta strandi538 – 543Combined sources6
Beta strandi1706 – 1708Combined sources3
Beta strandi1710 – 1712Combined sources3
Beta strandi1714 – 1721Combined sources8
Beta strandi1724 – 1728Combined sources5
Beta strandi1730 – 1734Combined sources5
Beta strandi1736 – 1738Combined sources3
Beta strandi1743 – 1746Combined sources4
Beta strandi1760 – 1762Combined sources3
Helixi1764 – 1766Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2COWNMR-A1685-1771[»]
3FM8X-ray2.30A/B440-545[»]
3GBJX-ray2.10A/B/C4-352[»]
3MDBX-ray2.95A/B440-545[»]
ProteinModelPortaliQ9NQT8.
SMRiQ9NQT8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NQT8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 353Kinesin motorPROSITE-ProRule annotationAdd BLAST349
Domaini471 – 535FHAAdd BLAST65
Domaini1721 – 1763CAP-GlyPROSITE-ProRule annotationAdd BLAST43

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili364 – 439Sequence analysisAdd BLAST76
Coiled coili607 – 710Sequence analysisAdd BLAST104
Coiled coili752 – 772Sequence analysisAdd BLAST21
Coiled coili1096 – 1143Sequence analysisAdd BLAST48

Sequence similaritiesi

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation
Contains 1 CAP-Gly domain.PROSITE-ProRule annotation
Contains 1 FHA domain.Curated
Contains 1 kinesin motor domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG0245. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00840000129680.
HOGENOMiHOG000230729.
HOVERGENiHBG052244.
InParanoidiQ9NQT8.
KOiK17914.
OMAiSNDPMQS.
OrthoDBiEOG091G0091.
PhylomeDBiQ9NQT8.
TreeFamiTF105221.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR000253. FHA_dom.
IPR022164. Kinesin-like.
IPR027640. Kinesin-like_fam.
IPR022140. Kinesin-like_KIF1-typ.
IPR032405. Kinesin_assoc.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 2 hits.
PfamiPF01302. CAP_GLY. 1 hit.
PF12473. DUF3694. 1 hit.
PF00498. FHA. 1 hit.
PF12423. KIF1B. 1 hit.
PF00225. Kinesin. 1 hit.
PF16183. Kinesin_assoc. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM01052. CAP_GLY. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NQT8-1) [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
MGDSKVKVAV RIRPMNRRET DLHTKCVVDV DANKVILNPV NTNLSKGDAR
60 70 80 90 100
GQPKVFAYDH CFWSMDESVK EKYAGQDIVF KCLGENILQN AFDGYNACIF
110 120 130 140 150
AYGQTGSGKS YTMMGTADQP GLIPRLCSGL FERTQKEENE EQSFKVEVSY
160 170 180 190 200
MEIYNEKVRD LLDPKGSRQT LKVREHSVLG PYVDGLSKLA VTSYKDIESL
210 220 230 240 250
MSEGNKSRTV AATNMNEESS RSHAVFKITL THTLYDVKSG TSGEKVGKLS
260 270 280 290 300
LVDLAGSERA TKTGAAGDRL KEGSNINKSL TTLGLVISAL ADQSAGKNKN
310 320 330 340 350
KFVPYRDSVL TWLLKDSLGG NSKTAMVATV SPAADNYDET LSTLRYADRA
360 370 380 390 400
KHIVNHAVVN EDPNARIIRD LREEVEKLRE QLTKAEAMKS PELKDRLEES
410 420 430 440 450
EKLIQEMTVT WEEKLRKTEE IAQERQKQLE SLGISLQSSG IKVGDDKCFL
460 470 480 490 500
VNLNADPALN ELLVYYLKEH TLIGSANSQD IQLCGMGILP EHCIIDITSE
510 520 530 540 550
GQVMLTPQKN TRTFVNGSSV SSPIQLHHGD RILWGNNHFF RLNLPKKKKK
560 570 580 590 600
AEREDEDQDP SMKNENSSEQ LDVDGDSSSE VSSEVNFNYE YAQMEVTMKA
610 620 630 640 650
LGSNDPMQSI LNSLEQQHEE EKRSALERQR LMYEHELEQL RRRLSPEKQN
660 670 680 690 700
CRSMDRFSFH SPSAQQRLRQ WAEEREATLN NSLMRLREQI VKANLLVREA
710 720 730 740 750
NYIAEELDKR TEYKVTLQIP ASSLDANRKR GSLLSEPAIQ VRRKGKGKQI
760 770 780 790 800
WSLEKLDNRL LDMRDLYQEW KECEEDNPVI RSYFKRADPF YDEQENHSLI
810 820 830 840 850
GVANVFLESL FYDVKLQYAV PIINQKGEVA GRLHVEVMRL SGDVGERIAG
860 870 880 890 900
GDEVAEVSFE KETQENKLVC MVKILQATGL PQHLSHFVFC KYSFWDQQEP
910 920 930 940 950
VIVAPEVDTS SSSVSKEPHC MVVFDHCNEF SVNITEDFIE HLSEGALAIE
960 970 980 990 1000
VYGHKINDPR KNPALWDLGI IQAKTRSLRD RWSEVTRKLE FWVQILEQNE
1010 1020 1030 1040 1050
NGEYCPVEVI SAKDVPTGGI FQLRQGQSRR VQVEVKSVQE SGTLPLMEEC
1060 1070 1080 1090 1100
ILSVGIGCVK VRPLRAPRTH ETFHEEEEDM DSYQDRDLER LRRKWLNALT
1110 1120 1130 1140 1150
KRQEYLDQQL QKLVSKRDKT EDDADREAQL LEMRLTLTEE RNAVMVPSAG
1160 1170 1180 1190 1200
SGIPGAPAEW TPVPGMETHI PVIFLDLNAD DFSSQDNLDD PEAGGWDATL
1210 1220 1230 1240 1250
TGEEEEEFFE LQIVKQHDGE VKAEASWDSA VHGCPQLSRG TPVDERLFLI
1260 1270 1280 1290 1300
VRVTVQLSHP ADMQLVLRKR ICVNVHGRQG FAQSLLKKMS HRSSIPGCGV
1310 1320 1330 1340 1350
TFEIVSNIPE DAQGVEEREA LARMAANVEN PASADSEAYI EKYLRSVLAV
1360 1370 1380 1390 1400
ENLLTLDRLR QEVAVKEQLT GKGKLSRRSI SSPNVNRLSG SRQDLIPSYS
1410 1420 1430 1440 1450
LGSNKGRWES QQDVSQTTVS RGIAPAPALS VSPQNNHSPD PGLSNLAASY
1460 1470 1480 1490 1500
LNPVKSFVPQ MPKLLKSLFP VRDEKRGKRP SPLAHQPVPR IMVQSASPDI
1510 1520 1530 1540 1550
RVTRMEEAQP EMGPDVLVQT MGAPALKICD KPAKVPSPPP VIAVTAVTPA
1560 1570 1580 1590 1600
PEAQDGPPSP LSEASSGYFS HSVSTATLSD ALGPGLDAAA PPGSMPTAPE
1610 1620 1630 1640 1650
AEPEAPISHP PPPTAVPAEE PPGPQQLVSP GRERPDLEAP APGSPFRVRR
1660 1670 1680 1690 1700
VRASELRSFS RMLAGDPGCS PGAEGNAPAP GAGGQALASD SEEADEVPEW
1710 1720 1730 1740 1750
LREGEFVTVG AHKTGVVRYV GPADFQEGTW VGVELDLPSG KNDGSIGGKQ
1760 1770 1780 1790 1800
YFRCNPGYGL LVRPSRVRRA TGPVRRRSTG LRLGAPEARR SATLSGSATN
1810 1820
LASLTAALAK ADRSHKNPEN RKSWAS
Length:1,826
Mass (Da):202,789
Last modified:June 26, 2013 - v2
Checksum:i7A336B3C5BDA21E6
GO
Isoform 2 (identifier: Q9NQT8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1460: Missing.
     1487-1507: Missing.

Note: No experimental confirmation available.
Show »
Length:345
Mass (Da):35,860
Checksum:i54A705E9CBB2F535
GO

Sequence cautioni

The sequence BAA31614 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti55V → C in AAF81263 (PubMed:10859302).Curated1
Sequence conflicti191V → A in AAF81263 (PubMed:10859302).Curated1
Sequence conflicti226F → L in AAF81263 (PubMed:10859302).Curated1
Sequence conflicti237V → A in AAF81263 (PubMed:10859302).Curated1
Sequence conflicti278K → E in AAF81263 (PubMed:10859302).Curated1
Sequence conflicti356H → N in AAF81263 (PubMed:10859302).Curated1
Sequence conflicti797H → L in AAF81263 (PubMed:10859302).Curated1
Sequence conflicti858S → P in AAF81263 (PubMed:10859302).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0559821471V → I.Corresponds to variant rs17526980dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0563601 – 1460Missing in isoform 2. 1 PublicationAdd BLAST1460
Alternative sequenceiVSP_0563611487 – 1507Missing in isoform 2. 1 PublicationAdd BLAST21

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279865 mRNA. Translation: AAF81263.1.
AB014539 mRNA. Translation: BAA31614.3. Different initiation.
AK294837 mRNA. Translation: BAG57946.1.
AC084262 Genomic DNA. No translation available.
AC103830 Genomic DNA. No translation available.
AC108449 Genomic DNA. No translation available.
AL583912 mRNA. Translation: CAC29496.1.
CCDSiCCDS55217.1. [Q9NQT8-1]
RefSeqiNP_056069.2. NM_015254.3. [Q9NQT8-1]
UniGeneiHs.444767.

Genome annotation databases

EnsembliENST00000524189; ENSP00000427900; ENSG00000197892. [Q9NQT8-1]
GeneIDi23303.
KEGGihsa:23303.
UCSCiuc003xhh.5. human. [Q9NQT8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF279865 mRNA. Translation: AAF81263.1.
AB014539 mRNA. Translation: BAA31614.3. Different initiation.
AK294837 mRNA. Translation: BAG57946.1.
AC084262 Genomic DNA. No translation available.
AC103830 Genomic DNA. No translation available.
AC108449 Genomic DNA. No translation available.
AL583912 mRNA. Translation: CAC29496.1.
CCDSiCCDS55217.1. [Q9NQT8-1]
RefSeqiNP_056069.2. NM_015254.3. [Q9NQT8-1]
UniGeneiHs.444767.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2COWNMR-A1685-1771[»]
3FM8X-ray2.30A/B440-545[»]
3GBJX-ray2.10A/B/C4-352[»]
3MDBX-ray2.95A/B440-545[»]
ProteinModelPortaliQ9NQT8.
SMRiQ9NQT8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116895. 12 interactors.
DIPiDIP-34586N.
IntActiQ9NQT8. 6 interactors.
STRINGi9606.ENSP00000427900.

PTM databases

iPTMnetiQ9NQT8.
PhosphoSitePlusiQ9NQT8.
SwissPalmiQ9NQT8.

Polymorphism and mutation databases

BioMutaiKIF13B.
DMDMi519668668.

Proteomic databases

EPDiQ9NQT8.
MaxQBiQ9NQT8.
PaxDbiQ9NQT8.
PeptideAtlasiQ9NQT8.
PRIDEiQ9NQT8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000524189; ENSP00000427900; ENSG00000197892. [Q9NQT8-1]
GeneIDi23303.
KEGGihsa:23303.
UCSCiuc003xhh.5. human. [Q9NQT8-1]

Organism-specific databases

CTDi23303.
DisGeNETi23303.
GeneCardsiKIF13B.
H-InvDBHIX0021580.
HGNCiHGNC:14405. KIF13B.
HPAiHPA025023.
HPA049655.
MIMi607350. gene.
neXtProtiNX_Q9NQT8.
OpenTargetsiENSG00000197892.
PharmGKBiPA30099.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0245. Eukaryota.
COG5059. LUCA.
GeneTreeiENSGT00840000129680.
HOGENOMiHOG000230729.
HOVERGENiHBG052244.
InParanoidiQ9NQT8.
KOiK17914.
OMAiSNDPMQS.
OrthoDBiEOG091G0091.
PhylomeDBiQ9NQT8.
TreeFamiTF105221.

Enzyme and pathway databases

BioCyciZFISH:G66-31795-MONOMER.
ReactomeiR-HSA-6811434. COPI-dependent Golgi-to-ER retrograde traffic.
R-HSA-983189. Kinesins.

Miscellaneous databases

ChiTaRSiKIF13B. human.
EvolutionaryTraceiQ9NQT8.
GenomeRNAii23303.
PROiQ9NQT8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197892.
CleanExiHS_KIF13B.
ExpressionAtlasiQ9NQT8. baseline and differential.
GenevisibleiQ9NQT8. HS.

Family and domain databases

Gene3Di2.30.30.190. 1 hit.
2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProiIPR000938. CAP-Gly_domain.
IPR000253. FHA_dom.
IPR022164. Kinesin-like.
IPR027640. Kinesin-like_fam.
IPR022140. Kinesin-like_KIF1-typ.
IPR032405. Kinesin_assoc.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 2 hits.
PfamiPF01302. CAP_GLY. 1 hit.
PF12473. DUF3694. 1 hit.
PF00498. FHA. 1 hit.
PF12423. KIF1B. 1 hit.
PF00225. Kinesin. 1 hit.
PF16183. Kinesin_assoc. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM01052. CAP_GLY. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF74924. SSF74924. 1 hit.
PROSITEiPS00845. CAP_GLY_1. 1 hit.
PS50245. CAP_GLY_2. 1 hit.
PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKI13B_HUMAN
AccessioniPrimary (citable) accession number: Q9NQT8
Secondary accession number(s): B4DGY5
, B5MC45, F8VPJ2, O75134, Q9BYJ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: June 26, 2013
Last modified: November 2, 2016
This is version 148 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.