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B1AVY7 (KI16B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF16B
Gene names
Name:Kif16b
Synonyms:Kiaa1590
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plus end-directed microtubule-dependent motor protein involved in endosome transport and receptor recycling and degradation. Regulates the plus end motility of early endosomes and the balance between recycling and degradation of receptors such as EGF receptor (EGFR) and FGF receptor (FGFR). Regulates the Golgi to endosome transport of FGFR-containing vesicles during early development, a key process for developing basement membrane and epiblast and primitive endoderm lineages during early postimplantation development. Ref.6

Subunit structure

Interacts with PTPN21 By similarity. Interacts with RAB14. Ref.6

Subcellular location

Cytoplasmcytoskeleton By similarity. Early endosome membrane By similarity. Note: It is unclear whether association with endosomes is mediated via phosphatidylinositol 3-phosphate (PtdIns3P)-binding or via its interaction with RAB14.

Domain

The PX domain mediates binding to phosphatidylinositol 3-phosphate (PtdIns3P), phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2), phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). Does not bind phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) By similarity.

Disruption phenotype

Embryonic death. Embryos are arrested at the blastocyst stage: the primitive endoderm and epiblast cannot be distinguished and appear as cell clumps resembling the inner cell mass (ICM) of the blastocyst. Embryos do not develop an epiblast epithelium and the uterine reaction appears to be incomplete. Development of the primitive endoderm and a basement membrane derived from it are severely affected in embryos at 4.5 dpc. Ref.6

Sequence similarities

Belongs to the kinesin-like protein family.

Contains 1 FHA domain.

Contains 1 kinesin-motor domain.

Contains 1 PX (phox homology) domain.

Sequence caution

The sequence BAC98211.1 differs from that shown. Reason: Partially unspliced pre-RNA.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
Cytoskeleton
Endosome
Membrane
Microtubule
   DomainCoiled coil
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to endosome transport

Inferred from mutant phenotype Ref.6. Source: UniProtKB

early endosome to late endosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

endoderm development

Inferred from mutant phenotype Ref.6. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.6. Source: UniProtKB

formation of primary germ layer

Inferred from mutant phenotype Ref.6. Source: UniProtKB

microtubule-based movement

Inferred from electronic annotation. Source: InterPro

receptor catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of receptor recycling

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentearly endosome

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3,4-bisphosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3,5-bisphosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-3-phosphate binding

Inferred from sequence or structural similarity. Source: UniProtKB

plus-end-directed microtubule motor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13121312Kinesin-like protein KIF16B
PRO_0000409500

Regions

Domain1 – 277277Kinesin-motor
Domain?480 – ?54465FHA
Domain1177 – 1291115PX
Nucleotide binding102 – 1098ATP Potential
Coiled coil366 – 42560 Potential
Coiled coil835 – 91379 Potential
Coiled coil941 – 1073133 Potential
Compositional bias597 – 798202Glu-rich

Amino acid modifications

Modified residue11451Phosphoserine Ref.5

Sequences

Sequence LengthMass (Da)Tools
B1AVY7 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 4397E49FF4E93881

FASTA1,312150,058
        10         20         30         40         50         60 
MASVKVAVRV RPMNRREKDL EAKFIIQMEK SKTTITNLKI PEGGTGDSGR ERTKTFTYDF 

        70         80         90        100        110        120 
SFYSADTKSP DYVSQEMVFK TLGTDVVKSA FEGYNACVFA YGQTGSGKSY TMMGNSGDSG 

       130        140        150        160        170        180 
LIPRICEALF SRINETTRWD EASFRTEVSY LEIYNERVRD LLRRKSSKTF NLRVREHPKE 

       190        200        210        220        230        240 
GPYVEDLSKH LVQNYSDVEE LMDAGNINRT TAATGMNDVS SRSHAIFTIK FTQAKFDAEM 

       250        260        270        280        290        300 
PCETVSKIHL VDLAGSERAD ATGATGVRLK EGGNINKSLV TLGNVISALA DLSQDAANPL 

       310        320        330        340        350        360 
VKKKQVFVPY RDSVLTWLLK DSLGGNSKTI MIATISPADV NYGETLSTLR YANRAKNIIN 

       370        380        390        400        410        420 
KPTINEDANV KLIRELRAEI ARLKTLLAQG NQIALLDSPT ALSMEEKLHQ NEARVQELTK 

       430        440        450        460        470        480 
EWTNKWNETQ NILKEQTLAL RKEGIGVVLD SELPHLIGID DDLLSTGIIL YHLKEGQTYV 

       490        500        510        520        530        540 
GREDASTEQD IVLHGLDLES EHCVFENAGG TVTLIPLRGS QCSVNGVQIV DATQLNQGAV 

       550        560        570        580        590        600 
ILLGRTNMFR FNHPKEAAKL REKRKSGLLS SFSLSMTDLS KSCENLSAVM LYNPGLEFER 

       610        620        630        640        650        660 
QQREELEKLE SKRKLIEEME EKQKSDKAEL ERMQQEVETR RKETEIVQRQ IRKQEESLKR 

       670        680        690        700        710        720 
RSFHIENKLK DLLAEKERFE EERLREQQGL EQQRRQEEES LFRIREELRK LQELNSHEQA 

       730        740        750        760        770        780 
EKVQIFQELD RLHQEQNAQS AKLRLEKRRL EEEEKEQVQR VAHLEEQLRK RQDTAPLLCP 

       790        800        810        820        830        840 
GEAQRAQEEK RELESIREAL LQAKEMRAGG DHTCRDELER AQQYFLEFKR RQLVKLASLE 

       850        860        870        880        890        900 
KDLVQQKDLL SKEVQEEKVA LEHVKCDAGG DPSFLATDDG NILGGPPDLD KIKTAETRLQ 

       910        920        930        940        950        960 
SREHQLQDLL QNHLPALLEE KQRVLDALDS GVLGLDTTLC QVEKEVGEKE EQIAQYQANA 

       970        980        990       1000       1010       1020 
SQLQQLRATF EFTANVARQE EKVRRKEKEI LESQEKQQRE ALEQAVAKLE QRRSALQRCS 

      1030       1040       1050       1060       1070       1080 
TLDLEIQEQR QKLGSLHTSE WSGWQASLET DGEALEMDPA RLEHEIHQLK QKICEVDGVQ 

      1090       1100       1110       1120       1130       1140 
RPHHGILEGQ AVLSSLPPSG GNSHLAPLMD ARISAYIEEE VQRRLHDLHR AIGDANHTPA 

      1150       1160       1170       1180       1190       1200 
DVMKSNEELH NGTTQRKLKY ERMYSRSLGT NRDDLKDPIK ISIPRYVLCG QGKDEHFEFE 

      1210       1220       1230       1240       1250       1260 
VKISVLDETW TVFRRYSRFR EMHKTLKLKY AELAALEFPP KKLFGNKDER VVAERRTHLE 

      1270       1280       1290       1300       1310 
KYLREFFSVM LQSETSPLHI NKVGLTLSKH TICEFSPFFK KGVFDYSSHG TG 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"Identification and classification of 16 new kinesin superfamily (KIF) proteins in mouse genome."
Nakagawa T., Tanaka Y., Matsuoka E., Kondo S., Okada Y., Noda Y., Kanai Y., Hirokawa N.
Proc. Natl. Acad. Sci. U.S.A. 94:9654-9659(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-239.
Strain: ICR.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-1312.
Strain: C57BL/6J.
Tissue: Gonad.
[4]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 487-1161.
Tissue: Embryonic tail.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145, MASS SPECTROMETRY.
Tissue: Macrophage.
[6]"KIF16B/Rab14 molecular motor complex is critical for early embryonic development by transporting FGF receptor."
Ueno H., Huang X., Tanaka Y., Hirokawa N.
Dev. Cell 20:60-71(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH RAB14.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL731712, AL731790, AL929136 Genomic DNA. Translation: CAM13299.1.
AL731790, AL731712, AL929136 Genomic DNA. Translation: CAM13408.1.
AL929136, AL731712, AL731790 Genomic DNA. Translation: CAM24500.1.
AB001423 mRNA. Translation: BAA22383.1.
AK033018 mRNA. Translation: BAC28130.2.
AK160835 mRNA. Translation: BAE36039.1.
AK129401 Transcribed RNA. Translation: BAC98211.1. Sequence problems.
IPIIPI00353998.
RefSeqNP_001074602.1. NM_001081133.2.
UniGeneMm.251934.

3D structure databases

ProteinModelPortalB1AVY7.
SMRB1AVY7. Positions 2-389, 428-563, 1174-1307.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000042551.

Proteomic databases

PaxDbB1AVY7.
PRIDEB1AVY7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000043589; ENSMUSP00000042551; ENSMUSG00000038844.
GeneID16558.
KEGGmmu:16558.
UCSCuc008mpz.1. mouse.

Organism-specific databases

CTD55614.
MGIMGI:1098240. Kif16b.
RougeSearch...

Phylogenomic databases

eggNOGCOG5059.
GeneTreeENSGT00700000104366.
HOGENOMHOG000044239.
HOVERGENHBG099559.
InParanoidQ3TUD2.
KOK10392.
OMAIAERRSH.
OrthoDBEOG4255RZ.

Gene expression databases

ArrayExpressB1AVY7.
BgeeB1AVY7.
GenevestigatorB1AVY7.

Family and domain databases

Gene3D2.60.200.20. 1 hit.
3.30.1520.10. 1 hit.
3.40.850.10. 1 hit.
InterProIPR000253. FHA_dom.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR001683. Phox.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamPF00498. FHA. 1 hit.
PF00225. Kinesin. 1 hit.
PF00787. PX. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00240. FHA. 1 hit.
SM00129. KISc. 1 hit.
SM00312. PX. 1 hit.
[Graphical view]
SUPFAMSSF64268. PX. 1 hit.
SSF49879. SMAD_FHA. 1 hit.
PROSITEPS50006. FHA_DOMAIN. False negative.
PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio290039.
SOURCESearch...

Entry information

Entry nameKI16B_MOUSE
AccessionPrimary (citable) accession number: B1AVY7
Secondary accession number(s): O35056 expand/collapse secondary AC list , Q3TUD2, Q6ZPM0, Q8BZZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: April 8, 2008
Last modified: May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families