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O60333 (KIF1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF1B

Short name=Klp
Gene names
Name:KIF1B
Synonyms:KIAA0591, KIAA1448
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1816 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Motor for anterograde transport of mitochondria. Has a microtubule plus end-directed motility. Isoform 2 is required for induction of neuronal apoptosis. Ref.14

Subunit structure

Interacts (via C-terminus end of the kinesin-motor domain) with CHP1; the interaction occurs in a calcium-dependent manner By similarity. Interacts with KBP. Ref.13

Subcellular location

Cytoplasmic vesicle By similarity. Cytoplasmcytoskeleton By similarity. Mitochondrion. Note: Colocalizes with synaptophysin at synaptic cytoplasmic transport vesicles in the neurites of hippocampal neurons By similarity. Ref.13

Tissue specificity

Isoform 3 is abundant in the skeletal muscle. It is also expressed in fetal brain, lung and kidney, and adult heart, placenta, testis, ovary and small intestine. Isoform 2 is abundant in the brain and also expressed in fetal heart, lung, liver and kidney, and adult skeletal muscle, placenta, liver, kidney, heart, spleen, thymus, prostate, testis, ovary, small intestine, colon and pancreas. Ref.2 Ref.3 Ref.6

Involvement in disease

Charcot-Marie-Tooth disease 2A1 (CMT2A1) [MIM:118210]: A dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22

Neuroblastoma 1 (NBLST1) [MIM:256700]: A common neoplasm of early childhood arising from embryonic cells that form the primitive neural crest and give rise to the adrenal medulla and the sympathetic nervous system.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Pheochromocytoma (PCC) [MIM:171300]: A catecholamine-producing tumor of chromaffin tissue of the adrenal medulla or sympathetic paraganglia. The cardinal symptom, reflecting the increased secretion of epinephrine and norepinephrine, is hypertension, which may be persistent or intermittent.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Sequence similarities

Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family. Unc-104 subfamily.

Contains 1 FHA domain.

Contains 1 kinesin motor domain.

Contains 1 PH domain.

Sequence caution

The sequence AAH01415.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAP35838.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAA25517.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAA95972.2 differs from that shown. Reason: Erroneous initiation.

The sequence BAB69038.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCytoplasm
Cytoplasmic vesicle
Cytoskeleton
Microtubule
Mitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCharcot-Marie-Tooth disease
Disease mutation
Neurodegeneration
Neuropathy
   DomainCoiled coil
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanterograde axon cargo transport

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton-dependent intracellular transport

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule-based movement

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion transport along microtubule

Inferred from electronic annotation. Source: Ensembl

neuromuscular synaptic transmission

Inferred from sequence or structural similarity. Source: UniProtKB

neuron-neuron synaptic transmission

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

kinesin complex

Inferred from electronic annotation. Source: InterPro

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuron projection

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

kinesin binding

Traceable author statement PubMed 10341097. Source: UniProtKB

microtubule motor activity

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12097473. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60333-1)

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.
Isoform 2 (identifier: O60333-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     289-294: Missing.
     394-434: IDPLIDDYSGSGSKYLKDFQNNKHRYLLASENQRPGHFSTA → T
Isoform 3 (identifier: O60333-3)

Also known as: Alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     289-294: Missing.
     394-434: IDPLIDDYSGSGSKYLKDFQNNKHRYLLASENQRPGHFSTA → T
     707-1196: YESKLQALQK...KPIVFEVFGH → ADSDSGDDSD...NLKAGRETTV
     1197-1816: Missing.
Note: Contains a phosphoserine at position 1141. Contains a phosphoserine at position 663. Contains a phosphoserine at position 665.
Isoform 4 (identifier: O60333-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1804-1816: SKLSRRCPSQSKY → PGHLASEIIREDKSVSFSCQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21
Chain2 – 18161815Kinesin-like protein KIF1B
PRO_0000125407

Regions

Domain5 – 354350Kinesin motor
Domain556 – 61257FHA
Domain1702 – 179998PH
Nucleotide binding97 – 1048ATP By similarity
Region270 – 35081Interaction with KBP
Coiled coil365 – 38622 Potential
Coiled coil470 – 50233 Potential
Coiled coil668 – 73770 Potential
Coiled coil841 – 86929 Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.21
Modified residue10571Phosphoserine Ref.15 Ref.18
Modified residue10751Phosphothreonine Ref.17
Modified residue14541Phosphoserine Ref.18
Modified residue14871Phosphoserine Ref.17 Ref.18
Modified residue16101Phosphoserine Ref.18
Modified residue16131Phosphoserine Ref.18

Natural variations

Alternative sequence289 – 2946Missing in isoform 2 and isoform 3.
VSP_002858
Alternative sequence394 – 43441IDPLI…HFSTA → T in isoform 2 and isoform 3.
VSP_002859
Alternative sequence707 – 1196490YESKL…EVFGH → ADSDSGDDSDKRSCEESWKL ITSLREKLPPSKLQTIVKKC GLPSSGKKREPIKMYQIPQR RRLSKDSKWVTISDLKIQAV KEICYEVALNDFRHSRQEIE ALAIVKMKELCAMYGKKDPN ERDSWRAVARDVWDTVGVGD EKIEDVMATGKGSTDVDDLK VHIDKLEDILQEVKKQNNMK DEEIKVLRNKMLKMEKVLPL IGSQEQKSPGSHKAKEPVGA GVSSTSENNVSKGDNGELAK EERVSQLMNGDPAFRRGRLR WMRQEQIRFKNLQQQEITKQ LRRQNVPHRFIPPENRKPRF PFKSNPKHRNSWSPGTHIII TEDEVIELRIPKDDEARKGN KEESQEKGGKGAFKDPQFPW GSQGMRSQDHIQVSKQHINN QQQPPQLRWRSNSLNNGQPK STRCQASASAESLNSHSGHP TADVQTFQAKRHIHQHRQSY CNYNTGGQLEGNAATSYQKQ TDKPSHCSQFVTPPRMRRQF SAPNLKAGRETTV in isoform 3.
VSP_002860
Alternative sequence1197 – 1816620Missing in isoform 3.
VSP_002861
Alternative sequence1804 – 181613SKLSR…SQSKY → PGHLASEIIREDKSVSFSCQ in isoform 4.
VSP_009381
Natural variant341S → L in a medulloblastoma sample; somatic mutation; loss of ability to induce apoptosis. Ref.14
VAR_063531
Natural variant981Q → L in CMT2A1. Ref.22
VAR_011515
Natural variant6921E → V Confers susceptibility to neuroblastoma; found as germline mutation in a neuroblastoma patient; loss of ability to induce apoptosis. Ref.14
VAR_063532
Natural variant8731T → I Confers susceptibility to neuroblastoma; found as germline mutation in a neuroblastoma patient; loss of ability to induce apoptosis. Ref.14
Corresponds to variant rs121908162 [ dbSNP | Ensembl ].
VAR_063533
Natural variant11331Y → C. Ref.14
Corresponds to variant rs2297881 [ dbSNP | Ensembl ].
VAR_063534
Natural variant12631P → S Confers susceptibility to neuroblastoma; found as germline mutation in a neuroblastoma patient; loss of ability to induce apoptosis. Ref.14
Corresponds to variant rs121908163 [ dbSNP | Ensembl ].
VAR_063535
Natural variant15271S → N Confers susceptibility to pheochromocytoma; found as germline mutation in a pheochromocytoma family; loss of ability to induce apoptosis. Ref.14
VAR_063536
Natural variant16001V → M. Ref.14
Corresponds to variant rs77172218 [ dbSNP | Ensembl ].
VAR_063537
Natural variant16741E → K in a pheochromocytoma sample; loss of ability to induce apoptosis. Ref.14
Corresponds to variant rs143669846 [ dbSNP | Ensembl ].
VAR_063538

Experimental info

Sequence conflict871E → G in BAA25517. Ref.8
Sequence conflict129 – 1313KIN → TNH in AAK49332. Ref.3
Sequence conflict129 – 1313KIN → TNH in AAK85155. Ref.4
Sequence conflict129 – 1313KIN → TNH in AAN17742. Ref.5
Sequence conflict1701E → D in AAK49332. Ref.3
Sequence conflict1701E → D in AAK85155. Ref.4
Sequence conflict1701E → D in AAN17742. Ref.5
Sequence conflict1741L → R in AAK49332. Ref.3
Sequence conflict1741L → R in AAK85155. Ref.4
Sequence conflict1741L → R in AAN17742. Ref.5
Sequence conflict219 – 2213AVF → VVY in AAK49332. Ref.3
Sequence conflict219 – 2213AVF → VVY in AAK85155. Ref.4
Sequence conflict219 – 2213AVF → VVY in AAN17742. Ref.5
Sequence conflict235 – 2395NLSTE → ILATV in AAK49332. Ref.3
Sequence conflict235 – 2395NLSTE → ILATV in AAK85155. Ref.4
Sequence conflict235 – 2395NLSTE → ILATV in AAN17742. Ref.5
Sequence conflict2441I → T in AAK49332. Ref.3
Sequence conflict2441I → T in AAK85155. Ref.4
Sequence conflict2441I → T in AAN17742. Ref.5
Sequence conflict2531E → D in AAK49332. Ref.3
Sequence conflict2531E → D in AAK85155. Ref.4
Sequence conflict2531E → D in AAN17742. Ref.5
Sequence conflict2561D → A in AAK49332. Ref.3
Sequence conflict2561D → A in AAK85155. Ref.4
Sequence conflict2561D → A in AAN17742. Ref.5
Sequence conflict2701N → I in AAK49332. Ref.3
Sequence conflict2701N → I in AAK85155. Ref.4
Sequence conflict2701N → I in AAN17742. Ref.5
Sequence conflict3631D → G in BAB69038. Ref.2

Secondary structure

............................ 1816
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 5.
Checksum: AD62F0515978C783

FASTA1,816204,476
        10         20         30         40         50         60 
MSGASVKVAV RVRPFNSRET SKESKCIIQM QGNSTSIINP KNPKEAPKSF SFDYSYWSHT 

        70         80         90        100        110        120 
SPEDPCFASQ NRVYNDIGKE MLLHAFEGYN VCIFAYGQTG AGKSYTMMGK QEESQAGIIP 

       130        140        150        160        170        180 
QLCEELFEKI NDNCNEEMSY SVEVSYMEIY CERVRDLLNP KNKGNLRVRE HPLLGPYVED 

       190        200        210        220        230        240 
LSKLAVTSYT DIADLMDAGN KARTVAATNM NETSSRSHAV FTIVFTQKKH DNETNLSTEK 

       250        260        270        280        290        300 
VSKISLVDLA GSERADSTGA KGTRLKEGAN INKSLTTLGK VISALAEVDN CTSKSKKKKK 

       310        320        330        340        350        360 
TDFIPYRDSV LTWLLRENLG GNSRTAMVAA LSPADINYDE TLSTLRYADR AKQIKCNAVI 

       370        380        390        400        410        420 
NEDPNAKLVR ELKEEVTRLK DLLRAQGLGD IIDIDPLIDD YSGSGSKYLK DFQNNKHRYL 

       430        440        450        460        470        480 
LASENQRPGH FSTASMGSLT SSPSSCSLSS QVGLTSVTSI QERIMSTPGG EEAIERLKES 

       490        500        510        520        530        540 
EKIIAELNET WEEKLRKTEA IRMEREALLA EMGVAIREDG GTLGVFSPKK TPHLVNLNED 

       550        560        570        580        590        600 
PLMSECLLYY IKDGITRVGQ ADAERRQDIV LSGAHIKEEH CIFRSERSNS GEVIVTLEPC 

       610        620        630        640        650        660 
ERSETYVNGK RVSQPVQLRS GNRIIMGKNH VFRFNHPEQA RAEREKTPSA ETPSEPVDWT 

       670        680        690        700        710        720 
FAQRELLEKQ GIDMKQEMEK RLQEMEILYK KEKEEADLLL EQQRLDYESK LQALQKQVET 

       730        740        750        760        770        780 
RSLAAETTEE EEEEEEVPWT QHEFELAQWA FRKWKSHQFT SLRDLLWGNA VYLKEANAIS 

       790        800        810        820        830        840 
VELKKKVQFQ FVLLTDTLYS PLPPELLPTE MEKTHEDRPF PRTVVAVEVQ DLKNGATHYW 

       850        860        870        880        890        900 
SLEKLKQRLD LMREMYDRAG EMASSAQDES ETTVTGSDPF YDRFHWFKLV GSSPIFHGCV 

       910        920        930        940        950        960 
NERLADRTPS PTFSTADSDI TELADEQQDE MEDFDDEAFV DDAGSDAGTE EGSDLFSDGH 

       970        980        990       1000       1010       1020 
DPFYDRSPWF ILVGRAFVYL SNLLYPVPLI HRVAIVSEKG EVRGFLRVAV QAIAADEEAP 

      1030       1040       1050       1060       1070       1080 
DYGSGIRQSG TAKISFDNEY FNQSDFSSVA MTRSGLSLEE LRIVEGQGQS SEVITPPEEI 

      1090       1100       1110       1120       1130       1140 
SRINDLDLKS STLLDGKMVM EGFSEEIGNH LKLGSAFTFR VTVLQASGIL PEYADIFCQF 

      1150       1160       1170       1180       1190       1200 
NFLHRHDEAF STEPLKNNGR GSPLAFYHVQ NIAVEITESF VDYIKTKPIV FEVFGHYQQH 

      1210       1220       1230       1240       1250       1260 
PLHLQGQELN SPPQPCRRFF PPPMPLSKPV PATKLNTMSK TSLGQSMSKY DLLVWFEISE 

      1270       1280       1290       1300       1310       1320 
LEPTGEYIPA VVDHTAGLPC QGTFLLHQGI QRRITVTIIH EKGSELHWKD VRELVVGRIR 

      1330       1340       1350       1360       1370       1380 
NKPEVDEAAV DAILSLNIIS AKYLKSSHNS SRTFYRFEAV WDSSLHNSLL LNRVTPYGEK 

      1390       1400       1410       1420       1430       1440 
IYMTLSAYLE LDHCIQPAVI TKDVCMVFYS RDAKISPPRS LRSLFGSGYS KSPDSNRVTG 

      1450       1460       1470       1480       1490       1500 
IYELSLCKMS DTGSPGMQRR RRKILDTSVA YVRGEENLAG WRPRGDSLIL EHQWELEKLE 

      1510       1520       1530       1540       1550       1560 
LLHEVEKTRH FLLLRERLGD SIPKSLSDSL SPSLSSGTLS TSTSISSQIS TTTFESAITP 

      1570       1580       1590       1600       1610       1620 
SESSGYDSGD IESLVDREKE LATKCLQLLT HTFNREFSQV HGSVSDCKLS DISPIGRDPS 

      1630       1640       1650       1660       1670       1680 
ESSFSSATLT PSSTCPSLVD SRSNSLDQKT PEANSRASSP CPEFEQFQIV PAVETPYLAR 

      1690       1700       1710       1720       1730       1740 
AGKNEFLNLV PDIEEIRPSS VVSKKGYLHF KEPLYSNWAK HFVVVRRPYV FIYNSDKDPV 

      1750       1760       1770       1780       1790       1800 
ERGIINLSTA QVEYSEDQQA MVKTPNTFAV CTKHRGVLLQ ALNDKDMNDW LYAFNPLLAG 

      1810 
TIRSKLSRRC PSQSKY 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 8AE6BB2665AF702C
Show »

FASTA1,770199,263
Isoform 3 (Alpha) [UniParc].

Checksum: 6F0D8846CD283811
Show »

FASTA1,153130,363
Isoform 4 [UniParc].

Checksum: A53CAAD5693880E7
Show »

FASTA1,823205,140

References

« Hide 'large scale' references
[1]"DNA encoding a kinesin-like protein (hklp) comprising biallelic markers."
Bougueleret L., Dufaure-Gare I., Grel P.
Patent number WO0063375, 26-OCT-2000
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[2]"Identification of the full-length KIAA0591 gene encoding a novel kinesin-related protein which is mapped to the neuroblastoma suppressor gene locus at 1p36.2."
Nagai M., Ichimiya S., Ozaki T., Seki N., Mihara M., Furuta S., Ohira M., Tomioka N., Nomura N., Sakiyama S., Kubo O., Takakura K., Hori T., Nakagawara A.
Int. J. Oncol. 16:907-916(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), TISSUE SPECIFICITY.
Tissue: Substantia nigra.
[3]"Genomic structure and mutational analysis of the human KIF1B gene which is homozygously deleted in neuroblastoma at chromosome 1p36.2."
Yang H.W., Chen Y.Z., Takita J., Soeda E., Piao H.Y., Hayashi Y.
Oncogene 20:5075-5083(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), TISSUE SPECIFICITY.
[4]"Identification of the human ortholog of mouse Kif1B, a kinesin superfamily motor protein."
Park M., Shin H., Lee Y.M., Moon E., Choi W., Kim W.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[5]"Identification of splicing variants of KIF1Bbeta."
Munirajan A.K., Ohira M., Nakagawara A.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[6]"Genomic structure and mutational analysis of the human KIF1Balpha gene located at 1p36.2 in neuroblastoma."
Chen Y.Y., Takita J., Chen Y.Z., Yang H.W., Hanada R., Yamamoto K., Hayashi Y.
Int. J. Oncol. 23:737-744(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
Tissue: Neuroblastoma.
[7]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[8]"Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:143-150(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[9]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1238-1816 (ISOFORMS 1/2).
Tissue: Placenta.
[11]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1238-1816 (ISOFORMS 1/2).
[12]"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. expand/collapse author list , 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] OF 1449-1816 (ISOFORMS 1/2).
[13]"The novel protein KBP regulates mitochondria localization by interaction with a kinesin-like protein."
Wozniak M.J., Melzer M., Dorner C., Haring H.U., Lammers R.
BMC Cell Biol. 6:35-35(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KBP, SUBCELLULAR LOCATION.
[14]"The kinesin KIF1Bbeta acts downstream from EglN3 to induce apoptosis and is a potential 1p36 tumor suppressor."
Schlisio S., Kenchappa R.S., Vredeveld L.C., George R.E., Stewart R., Greulich H., Shahriari K., Nguyen N.V., Pigny P., Dahia P.L., Pomeroy S.L., Maris J.M., Look A.T., Meyerson M., Peeper D.S., Carter B.D., Kaelin W.G. Jr.
Genes Dev. 22:884-893(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INVOLVEMENT IN NEUROBLASTOMA AND PHEOCHROMOCYTOMA, VARIANTS LEU-34; VAL-692; ILE-873; CYS-1133; SER-1263; ASN-1527; MET-1600 AND LYS-1674.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1057, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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].
[17]"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 THR-1075 AND SER-1487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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-1057; SER-1454; SER-1487; SER-1610 AND SER-1613, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1141 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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-663 AND SER-665 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(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].
[22]"Charcot-Marie-Tooth disease type 2A caused by mutation in a microtubule motor KIF1B-beta."
Zhao C., Takita J., Tanaka Y., Setou M., Nakagawa T., Takeda S., Yang H.W., Terada S., Nakata T., Takei Y., Saito M., Tsuji S., Hayashi Y., Hirokawa N.
Cell 105:587-597(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMT2A1 LEU-98.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AX039604 Genomic DNA. Translation: CAC16629.1.
AB017133 mRNA. Translation: BAB69038.1. Different initiation.
AF257176 mRNA. Translation: AAK49332.1.
AY043362 mRNA. Translation: AAK85155.1.
AB088210 mRNA. Translation: BAE02543.1.
AY139835 mRNA. Translation: AAN17742.1.
AB011163 mRNA. Translation: BAA25517.2. Different initiation.
AB040881 mRNA. Translation: BAA95972.2. Different initiation.
AL139424, AL358013 Genomic DNA. Translation: CAI95752.1.
AL139424, AL358013 Genomic DNA. Translation: CAI95753.1.
AL358013, AL139424 Genomic DNA. Translation: CAI95219.1.
AL358013, AL139424 Genomic DNA. Translation: CAI95220.1.
AL358013, AL139424 Genomic DNA. Translation: CAI95221.1.
AL358013 Genomic DNA. Translation: CAI95222.1.
AL139424, AL358013 Genomic DNA. Translation: CAI95754.1.
BC001415 mRNA. Translation: AAH01415.1. Different initiation.
BC115395 mRNA. Translation: AAI15396.1.
BT007174 mRNA. Translation: AAP35838.1. Different initiation.
AK022977 mRNA. Translation: BAB14341.1.
CCDSCCDS111.1. [O60333-2]
CCDS112.1. [O60333-3]
RefSeqNP_055889.2. NM_015074.3. [O60333-2]
NP_904325.2. NM_183416.3. [O60333-3]
UniGeneHs.97858.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EH0NMR-A531-647[»]
ProteinModelPortalO60333.
SMRO60333. Positions 4-380, 471-647.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116723. 15 interactions.
DIPDIP-33015N.
IntActO60333. 23 interactions.
MINTMINT-1682229.

Chemistry

BindingDBO60333.
ChEMBLCHEMBL5889.

PTM databases

PhosphoSiteO60333.

Proteomic databases

MaxQBO60333.
PaxDbO60333.
PRIDEO60333.

Protocols and materials databases

DNASU23095.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263934; ENSP00000263934; ENSG00000054523. [O60333-2]
ENST00000377081; ENSP00000366284; ENSG00000054523. [O60333-4]
ENST00000377083; ENSP00000366287; ENSG00000054523. [O60333-3]
ENST00000377086; ENSP00000366290; ENSG00000054523. [O60333-1]
ENST00000377093; ENSP00000366297; ENSG00000054523. [O60333-3]
GeneID23095.
KEGGhsa:23095.
UCSCuc001aqv.4. human. [O60333-3]
uc001aqw.4. human. [O60333-2]
uc001aqx.4. human. [O60333-1]
uc001aqz.3. human. [O60333-4]

Organism-specific databases

CTD23095.
GeneCardsGC01P010270.
HGNCHGNC:16636. KIF1B.
HPACAB015177.
HPA026434.
MIM118210. phenotype.
171300. phenotype.
256700. phenotype.
605995. gene.
neXtProtNX_O60333.
Orphanet99946. Autosomal dominant Charcot-Marie-Tooth disease type 2A1.
PharmGKBPA38176.
HUGESearch...
Search...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOVERGENHBG052251.
KOK10392.
OMANRDAITE.
OrthoDBEOG77Q4VS.
PhylomeDBO60333.
TreeFamTF105221.

Gene expression databases

ArrayExpressO60333.
BgeeO60333.
CleanExHS_KIF1B.
GenevestigatorO60333.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
2.60.200.20. 1 hit.
3.40.850.10. 1 hit.
InterProIPR000253. FHA_dom.
IPR022140. KIF1B.
IPR022164. Kinesin-like.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERPTHR24115. PTHR24115. 1 hit.
PfamPF12473. DUF3694. 1 hit.
PF00498. FHA. 1 hit.
PF12423. KIF1B. 1 hit.
PF00225. Kinesin. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS50006. FHA_DOMAIN. 1 hit.
PS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKIF1B. human.
EvolutionaryTraceO60333.
GeneWikiKIF1B.
GenomeRNAi23095.
NextBio44259.
PROO60333.
SOURCESearch...

Entry information

Entry nameKIF1B_HUMAN
AccessionPrimary (citable) accession number: O60333
Secondary accession number(s): A6NFS8 expand/collapse secondary AC list , A6NKQ4, Q4VXC3, Q4VXC4, Q4VXC5, Q4VXC6, Q96Q94, Q9BV80, Q9P280
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 157 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM