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Q9NQT8

- KI13B_HUMAN

UniProt

Q9NQT8 - KI13B_HUMAN

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Protein

Kinesin-like protein KIF13B

Gene

KIF13B

Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi103 – 1108ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. 14-3-3 protein binding Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. microtubule motor activity Source: UniProtKB
  4. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. metabolic process Source: GOC
  2. microtubule-based movement Source: UniProtKB
  3. protein targeting Source: UniProtKB
  4. regulation of axonogenesis Source: UniProtKB
  5. signal transduction Source: UniProtKB
  6. T cell activation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
ProteomesiUP000005640: 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

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

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1381 – 13811S → A: Abolishes phosphorylation by MARK2; when associated with A-1410. 1 Publication
Mutagenesisi1410 – 14101S → A: Abolishes phosphorylation by MARK2; when associated with A-1389. 1 Publication

Organism-specific databases

PharmGKBiPA30099.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18261826Kinesin-like protein KIF13BPRO_0000125448Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei661 – 6611Phosphoserine1 Publication
Modified residuei1379 – 13791Phosphoserine1 Publication
Modified residuei1381 – 13811Phosphoserine; by MARK21 Publication
Modified residuei1382 – 13821Phosphoserine1 Publication
Modified residuei1410 – 14101Phosphoserine; by MARK22 Publications
Modified residuei1432 – 14321Phosphoserine1 Publication
Modified residuei1438 – 14381Phosphoserine1 Publication
Modified residuei1644 – 16441Phosphoserine1 Publication

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.5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NQT8.
PaxDbiQ9NQT8.
PRIDEiQ9NQT8.

PTM databases

PhosphoSiteiQ9NQT8.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

CleanExiHS_KIF13B.
ExpressionAtlasiQ9NQT8. baseline and differential.
GenevestigatoriQ9NQT8.

Organism-specific databases

HPAiHPA025023.

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

Protein-protein interaction databases

BioGridi116895. 9 interactions.
DIPiDIP-34586N.
IntActiQ9NQT8. 5 interactions.
STRINGi9606.ENSP00000350459.

Structurei

Secondary structure

1
1826
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 127Combined sources
Helixi17 – 226Combined sources
Beta strandi28 – 314Combined sources
Beta strandi34 – 374Combined sources
Beta strandi54 – 574Combined sources
Beta strandi59 – 635Combined sources
Turni70 – 723Combined sources
Helixi76 – 9217Combined sources
Beta strandi97 – 1037Combined sources
Helixi109 – 1135Combined sources
Beta strandi117 – 1204Combined sources
Helixi122 – 13716Combined sources
Beta strandi142 – 15413Combined sources
Beta strandi157 – 1604Combined sources
Beta strandi189 – 1913Combined sources
Helixi194 – 20613Combined sources
Beta strandi222 – 23514Combined sources
Beta strandi241 – 25313Combined sources
Helixi272 – 29221Combined sources
Helixi305 – 3073Combined sources
Helixi309 – 3135Combined sources
Helixi315 – 3184Combined sources
Beta strandi323 – 3308Combined sources
Helixi334 – 3363Combined sources
Helixi337 – 35014Combined sources
Beta strandi449 – 4524Combined sources
Turni457 – 4604Combined sources
Beta strandi464 – 4663Combined sources
Beta strandi469 – 4768Combined sources
Beta strandi480 – 4823Combined sources
Beta strandi493 – 4975Combined sources
Beta strandi503 – 5075Combined sources
Beta strandi513 – 5153Combined sources
Beta strandi524 – 5263Combined sources
Beta strandi531 – 5344Combined sources
Turni535 – 5373Combined sources
Beta strandi538 – 5436Combined sources
Beta strandi1706 – 17083Combined sources
Beta strandi1710 – 17123Combined sources
Beta strandi1714 – 17218Combined sources
Beta strandi1724 – 17285Combined sources
Beta strandi1730 – 17345Combined sources
Beta strandi1736 – 17383Combined sources
Beta strandi1743 – 17464Combined sources
Beta strandi1760 – 17623Combined sources
Helixi1764 – 17663Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2COWNMR-A1685-1771[»]
3FM8X-ray2.30A/B440-545[»]
3GBJX-ray2.10A/B/C4-352[»]
3MDBX-ray2.95A/B440-545[»]
ProteinModelPortaliQ9NQT8.
SMRiQ9NQT8. Positions 5-351, 448-545, 1679-1773.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NQT8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 353349Kinesin motorPROSITE-ProRule annotationAdd
BLAST
Domaini471 – 53565FHAAdd
BLAST
Domaini1721 – 176343CAP-GlyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili364 – 43976Sequence AnalysisAdd
BLAST
Coiled coili607 – 710104Sequence AnalysisAdd
BLAST
Coiled coili752 – 77221Sequence AnalysisAdd
BLAST
Coiled coili1096 – 114348Sequence AnalysisAdd
BLAST

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

eggNOGiCOG5244.
GeneTreeiENSGT00770000120451.
HOGENOMiHOG000230729.
HOVERGENiHBG052244.
InParanoidiQ9NQT8.
KOiK17914.
OMAiMKALGSN.
OrthoDBiEOG72G16D.
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.
IPR022140. KIF1B.
IPR022164. Kinesin-like.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERiPTHR24115. PTHR24115. 1 hit.
PfamiPF01302. CAP_GLY. 1 hit.
PF12473. DUF3694. 2 hits.
PF00498. FHA. 1 hit.
PF12423. KIF1B. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSiPR00380. KINESINHEAVY.
SMARTiSM01052. CAP_GLY. 1 hit.
SM00240. FHA. 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. Align

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 BAA31614.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551V → C in AAF81263. (PubMed:10859302)Curated
Sequence conflicti191 – 1911V → A in AAF81263. (PubMed:10859302)Curated
Sequence conflicti226 – 2261F → L in AAF81263. (PubMed:10859302)Curated
Sequence conflicti237 – 2371V → A in AAF81263. (PubMed:10859302)Curated
Sequence conflicti278 – 2781K → E in AAF81263. (PubMed:10859302)Curated
Sequence conflicti356 – 3561H → N in AAF81263. (PubMed:10859302)Curated
Sequence conflicti797 – 7971H → L in AAF81263. (PubMed:10859302)Curated
Sequence conflicti858 – 8581S → P in AAF81263. (PubMed:10859302)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1471 – 14711V → I.
Corresponds to variant rs17526980 [ dbSNP | Ensembl ].
VAR_055982

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 14601460Missing in isoform 2. 1 PublicationVSP_056360Add
BLAST
Alternative sequencei1487 – 150721Missing in isoform 2. 1 PublicationVSP_056361Add
BLAST

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.

Polymorphism databases

DMDMi519668668.

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 .
CCDSi CCDS55217.1. [Q9NQT8-1 ]
RefSeqi NP_056069.2. NM_015254.3. [Q9NQT8-1 ]
UniGenei Hs.444767.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2COW NMR - A 1685-1771 [» ]
3FM8 X-ray 2.30 A/B 440-545 [» ]
3GBJ X-ray 2.10 A/B/C 4-352 [» ]
3MDB X-ray 2.95 A/B 440-545 [» ]
ProteinModelPortali Q9NQT8.
SMRi Q9NQT8. Positions 5-351, 448-545, 1679-1773.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116895. 9 interactions.
DIPi DIP-34586N.
IntActi Q9NQT8. 5 interactions.
STRINGi 9606.ENSP00000350459.

PTM databases

PhosphoSitei Q9NQT8.

Polymorphism databases

DMDMi 519668668.

Proteomic databases

MaxQBi Q9NQT8.
PaxDbi Q9NQT8.
PRIDEi Q9NQT8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000524189 ; ENSP00000427900 ; ENSG00000197892 . [Q9NQT8-1 ]
GeneIDi 23303.
KEGGi hsa:23303.

Organism-specific databases

CTDi 23303.
GeneCardsi GC08M028924.
H-InvDB HIX0021580.
HGNCi HGNC:14405. KIF13B.
HPAi HPA025023.
MIMi 607350. gene.
neXtProti NX_Q9NQT8.
PharmGKBi PA30099.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5244.
GeneTreei ENSGT00770000120451.
HOGENOMi HOG000230729.
HOVERGENi HBG052244.
InParanoidi Q9NQT8.
KOi K17914.
OMAi MKALGSN.
OrthoDBi EOG72G16D.
PhylomeDBi Q9NQT8.
TreeFami TF105221.

Miscellaneous databases

ChiTaRSi KIF13B. human.
EvolutionaryTracei Q9NQT8.
GenomeRNAii 23303.
NextBioi 35471874.
PROi Q9NQT8.
SOURCEi Search...

Gene expression databases

CleanExi HS_KIF13B.
ExpressionAtlasi Q9NQT8. baseline and differential.
Genevestigatori Q9NQT8.

Family and domain databases

Gene3Di 2.30.30.190. 1 hit.
2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProi IPR000938. CAP-Gly_domain.
IPR000253. FHA_dom.
IPR022140. KIF1B.
IPR022164. Kinesin-like.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR008984. SMAD_FHA_domain.
[Graphical view ]
PANTHERi PTHR24115. PTHR24115. 1 hit.
Pfami PF01302. CAP_GLY. 1 hit.
PF12473. DUF3694. 2 hits.
PF00498. FHA. 1 hit.
PF12423. KIF1B. 1 hit.
PF00225. Kinesin. 1 hit.
[Graphical view ]
PRINTSi PR00380. KINESINHEAVY.
SMARTi SM01052. CAP_GLY. 1 hit.
SM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
[Graphical view ]
SUPFAMi SSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF74924. SSF74924. 1 hit.
PROSITEi PS00845. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "GAKIN, a novel kinesin-like protein associates with the human homologue of the Drosophila discs large tumor suppressor in T lymphocytes."
    Hanada T., Lin L., Tibaldi E.V., Reinherz E.L., Chishti A.H.
    J. Biol. Chem. 275:28774-28784(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH DLG1 AND DLG4.
  2. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  3. Ohara O., Suyama M., Nagase T., Ishikawa K.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. "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] (ISOFORM 2).
    Tissue: Brain.
  5. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1096-1826 (ISOFORM 1).
    Tissue: Amygdala.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1644, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1379; SER-1382; SER-1432 AND SER-1438, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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-1410, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Par1b/MARK2 phosphorylates kinesin-like motor protein GAKIN/KIF13B to regulate axon formation."
    Yoshimura Y., Terabayashi T., Miki H.
    Mol. Cell. Biol. 30:2206-2219(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH 14-3-3, MUTAGENESIS OF SER-1381 AND SER-1410, PHOSPHORYLATION AT SER-1381 AND SER-1410.
  11. "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-661, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Solution structure of the CAP-Gly domain in human kinesin-like protein KIF13B."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1684-1771.

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 26, 2014
This is version 129 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

External Data

Dasty 3