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Q96L93 (KI16B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kinesin-like protein KIF16B
Alternative name(s):
Sorting nexin-23
Gene names
Name:KIF16B
Synonyms:C20orf23, KIAA1590, SNX23
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1317 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.9

Subunit structure

Interacts with RAB14 By similarity. Interacts with PTPN21. Ref.11

Subcellular location

Cytoplasmcytoskeleton Probable. Early endosome membrane. Note: It is unclear whether association with endosomes is mediated via phosphatidylinositol 3-phosphate (PtdIns3P)-binding or via its interaction with RAB14. Ref.9 Ref.13

Tissue specificity

Primarily expressed in brain. Also present in kidney, liver, intestine, placenta, leukocytes, heart and skeletal muscle (at protein level). Ref.9

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). Ref.9 Ref.13

Post-translational modification

Isoform 4 is ubiquitinated at Lys-685.

Sequence similarities

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

Contains 1 FHA domain.

Contains 1 kinesin motor domain.

Contains 1 PX (phox homology) domain.

Sequence caution

The sequence BAA90971.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAA90971.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence BAB13416.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAB15530.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAI43062.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI43179.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
Cytoskeleton
Endosome
Membrane
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandATP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGolgi to endosome transport

Inferred from sequence or structural similarity. Source: UniProtKB

early endosome to late endosome transport

Inferred from mutant phenotype Ref.9. Source: UniProtKB

endoderm development

Inferred from sequence or structural similarity. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.9. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

formation of primary germ layer

Inferred from sequence or structural similarity. Source: UniProtKB

microtubule-based movement

Inferred from electronic annotation. Source: InterPro

receptor catabolic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

regulation of receptor recycling

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentearly endosome

Inferred from direct assay Ref.9. Source: UniProtKB

early endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endosome

Inferred from direct assay Ref.13. Source: UniProtKB

kinesin complex

Inferred from electronic annotation. Source: InterPro

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphatidylinositol-3,4,5-trisphosphate binding

Inferred from direct assay Ref.9Ref.13. Source: UniProtKB

phosphatidylinositol-3,4-bisphosphate binding

Inferred from direct assay Ref.9Ref.13. Source: UniProtKB

phosphatidylinositol-3,5-bisphosphate binding

Inferred from direct assay Ref.13. Source: UniProtKB

phosphatidylinositol-3-phosphate binding

Inferred from direct assay Ref.9. Source: UniProtKB

plus-end-directed microtubule motor activity

Inferred from direct assay Ref.9. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96L93-1)

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: Q96L93-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1167-1317: RMVSRSLGAN...VFDYSSHGTG → LCRDLLCVLM...LWLISHLTRL
Note: Ubiquitinated at position 685.
Isoform 3 (identifier: Q96L93-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1208-1237: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q96L93-5)

The sequence of this isoform differs from the canonical sequence as follows:
     685-840: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q96L93-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1167-1207: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13171317Kinesin-like protein KIF16B
PRO_0000125466

Regions

Domain3 – 358356Kinesin motor
Domain478 – 52952FHA
Domain1182 – 1296115PX
Nucleotide binding102 – 1098ATP By similarity
Coiled coil370 – 42556 Potential
Coiled coil595 – 882288 Potential
Coiled coil936 – 1087152 Potential
Compositional bias597 – 1070474Glu-rich

Natural variations

Alternative sequence685 – 840156Missing in isoform 4.
VSP_015858
Alternative sequence1167 – 1317151RMVSR…SHGTG → LCRDLLCVLMPEPDAAACAN HPLLQQDLVQLSLDWKTEIP DLVLPNGVQVSSKFQTTLVD MIYFLHGNMEVNVPSLAEVQ LLLYTTVKVMGDSGHDQCQS LVLLNTHIALVKEDCVFYPR IRSRNIPPPGAQFDVIKCHA LSEFRCVVVPEKKNVSTVEL VFLQKLKPSVGSRNSPPEHL QEAPNVQLFTTPLYLQGSQN VAPEVWKLTFNSQDEALWLI SHLTRL in isoform 2.
VSP_010851
Alternative sequence1167 – 120741Missing in isoform 5.
VSP_041318
Alternative sequence1208 – 123730Missing in isoform 3.
VSP_010852
Natural variant7721K → T in a breast cancer sample; somatic mutation. Ref.14
VAR_036218
Natural variant8101G → R.
Corresponds to variant rs2236145 [ dbSNP | Ensembl ].
VAR_049700
Natural variant8241R → S.
Corresponds to variant rs2236144 [ dbSNP | Ensembl ].
VAR_019396
Natural variant9991K → N.
Corresponds to variant rs8116503 [ dbSNP | Ensembl ].
VAR_065248
Natural variant10271M → T. Ref.1 Ref.2 Ref.6
Corresponds to variant rs6034464 [ dbSNP | Ensembl ].
VAR_019397
Natural variant11191N → S.
Corresponds to variant rs8123195 [ dbSNP | Ensembl ].
VAR_019398

Experimental info

Mutagenesis1091S → A: Impairs plus end-directed microtubule-dependent motor activity, leading to impair EGFR recycling. Ref.9
Mutagenesis12201R → A: Abolishes PtdIns(3)P-binding. Ref.13
Mutagenesis12251R → A: Induces a 3-fold decrease in PtdIns(3)P-binding; when associated with A-1229 and A-1232. Ref.13
Mutagenesis12291K → A: Induces a 3-fold decrease in PtdIns(3)P-binding; when associated with A-1225 and A-1232. Ref.13
Mutagenesis12321K → A: Induces a 3-fold decrease in PtdIns(3)P-binding; when associated with A-1225 and A-1229. Ref.13
Mutagenesis12481L → A: Induces a 7-fold decrease in PtdIns(3)P-binding and abolishes endosome localization. Induces a 25-fold decrease in PtdIns(3)P-binding; when associated with A-1249. Ref.13
Mutagenesis12481L → V: Induces a 6-fold decrease in PtdIns(3)P-binding. Ref.13
Mutagenesis12491F → A: Induces a 5-fold decrease in PtdIns(3)P-binding and abolishes endosome localization. Induces a 25-fold decrease in PtdIns(3)P-binding; when associated with A-1248. Ref.13
Mutagenesis12601R → A: Induces a 30-fold decrease in PtdIns(3)P-binding. Ref.13
Sequence conflict181K → E in AK095322. Ref.7
Sequence conflict2741N → D in CAI46105. Ref.2
Sequence conflict5831R → H in BAA90971. Ref.7
Sequence conflict6491L → H in CAI46266. Ref.2
Sequence conflict1056 – 10572EQ → SE in AAH34984. Ref.6
Sequence conflict11001S → N in CAI46105. Ref.2
Sequence conflict11081S → L in AAH34984. Ref.6
Sequence conflict12441P → A in AAO17292. Ref.3
Sequence conflict12441P → A in BAB15530. Ref.7

Secondary structure

................. 1317
Helix Strand Turn

Details...

Sequences

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

Last modified July 19, 2004. Version 2.
Checksum: 278E9CB88D9C04DF

FASTA1,317152,011
        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 
LIPRICEGLF SRINETTRWD EASFRTEVSY LEIYNERVRD LLRRKSSKTF NLRVREHPKE 

       190        200        210        220        230        240 
GPYVEDLSKH LVQNYGDVEE LMDAGNINRT TAATGMNDVS SRSHAIFTIK FTQAKFDSEM 

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

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

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

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

       490        500        510        520        530        540 
GRDDASTEQD IVLHGLDLES EHCIFENIGG TVTLIPLSGS QCSVNGVQIV EATHLNQGAV 

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

       610        620        630        640        650        660 
QQREELEKLE SKRKLIEEME EKQKSDKAEL ERMQQEVETQ RKETEIVQLQ IRKQEESLKR 

       670        680        690        700        710        720 
RSFHIENKLK DLLAEKEKFE EERLREQQEI ELQKKRQEEE TFLRVQEELQ RLKELNNNEK 

       730        740        750        760        770        780 
AEKFQIFQEL DQLQKEKDEQ YAKLELEKKR LEEQEKEQVM LVAHLEEQLR EKQEMIQLLR 

       790        800        810        820        830        840 
RGEVQWVEEE KRDLEGIRES LLRVKEARAG GDEDGEELEK AQLRFFEFKR RQLVKLVNLE 

       850        860        870        880        890        900 
KDLVQQKDIL KKEVQEEQEI LECLKCEHDK ESRLLEKHDE SVTDVTEVPQ DFEKIKPVEY 

       910        920        930        940        950        960 
RLQYKERQLQ YLLQNHLPTL LEEKQRAFEI LDRGPLSLDN TLYQVEKEME EKEEQLAQYQ 

       970        980        990       1000       1010       1020 
ANANQLQKLQ ATFEFTANIA RQEEKVRKKE KEILESREKQ QREALERALA RLERRHSALQ 

      1030       1040       1050       1060       1070       1080 
RHSTLGMEIE EQRQKLASLN SGSREQSGLQ ASLEAEQEAL EKDQERLEYE IQQLKQKIYE 

      1090       1100       1110       1120       1130       1140 
VDGVQKDHHG TLEGKVASSS LPVSAEKSHL VPLMDARINA YIEEEVQRRL QDLHRVISEG 

      1150       1160       1170       1180       1190       1200 
CSTSADTMKD NEKLHNGTIQ RKLKYERMVS RSLGANPDDL KDPIKISIPR YVLCGQGKDA 

      1210       1220       1230       1240       1250       1260 
HFEFEVKITV LDETWTVFRR YSRFREMHKT LKLKYAELAA LEFPPKKLFG NKDERVIAER 

      1270       1280       1290       1300       1310 
RSHLEKYLRD FFSVMLQSAT SPLHINKVGL TLSKHTICEF SPFFKKGVFD YSSHGTG 

« Hide

Isoform 2 [UniParc].

Checksum: 85A4365F83AADDB9
Show »

FASTA1,392159,831
Isoform 3 [UniParc].

Checksum: 9BA79E2857090F5F
Show »

FASTA1,287148,211
Isoform 4 [UniParc].

Checksum: 078AB4C77FBAA4C3
Show »

FASTA1,161132,866
Isoform 5 [UniParc].

Checksum: 430E508AEE6E2E12
Show »

FASTA1,276147,398

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT THR-1027.
Tissue: Brain.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 557-1317 (ISOFORM 4), VARIANT THR-1027.
Tissue: Adipose tissue and Salivary gland.
[3]Guo J.H.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 916-1317 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1056-1317 (ISOFORM 3), VARIANT THR-1027.
Tissue: Hippocampus and Liver.
[7]"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 1-948 (ISOFORMS 1/2/3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1085-1317 (ISOFORMS 1/4).
Tissue: Colon, Lung and Tongue.
[8]"A new member (SNX23) of the sorting nexin family."
Hong W.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1114-1317 (ISOFORMS 1/4).
[9]"Modulation of receptor recycling and degradation by the endosomal kinesin KIF16B."
Hoepfner S., Severin F., Cabezas A., Habermann B., Runge A., Gillooly D., Stenmark H., Zerial M.
Cell 121:437-450(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DOMAIN PX, PHOSPHATIDYLINOSITOL-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-109.
[10]"The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-685 (ISOFORM 4).
Tissue: Lung adenocarcinoma.
[11]"PTPD1 supports receptor stability and mitogenic signaling in bladder cancer cells."
Carlucci A., Porpora M., Garbi C., Galgani M., Santoriello M., Mascolo M., di Lorenzo D., Altieri V., Quarto M., Terracciano L., Gottesman M.E., Insabato L., Feliciello A.
J. Biol. Chem. 285:39260-39270(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPN21.
[12]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The structural basis of novel endosome anchoring activity of KIF16B kinesin."
Blatner N.R., Wilson M.I., Lei C., Hong W., Murray D., Williams R.L., Cho W.
EMBO J. 26:3709-3719(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1179-1312, SUBCELLULAR LOCATION, PHOSPHATIDYLINOSITOL-BINDING, DOMAIN PX, MUTAGENESIS OF ARG-1220; ARG-1225; LYS-1229; LYS-1232; LEU-1248; PHE-1249 AND ARG-1260.
[14]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-772.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB046810 mRNA. Translation: BAB13416.2. Different initiation.
BX647572 mRNA. Translation: CAI46105.1.
BX648426 mRNA. Translation: CAI46266.1.
AY166853 mRNA. Translation: AAO17292.1.
AL049794, AL117376, AL118509 Genomic DNA. Translation: CAI22745.2.
AL117376, AL049794, AL118509 Genomic DNA. Translation: CAI43180.2.
AL117376 Genomic DNA. Translation: CAI43181.2.
AL118509, AL049794, AL117376 Genomic DNA. Translation: CAI43063.2.
AL118509, AL049794, AL117376 Genomic DNA. Translation: CAM28305.1.
AL049794, AL117376, AL118509 Genomic DNA. Translation: CAM28307.1.
AL118509, AL117376 Genomic DNA. Translation: CAI43062.1. Sequence problems.
AL117376, AL118509 Genomic DNA. Translation: CAI43179.1. Sequence problems.
CH471133 Genomic DNA. Translation: EAX10290.1.
BC034984 mRNA. Translation: AAH34984.2.
BC110317 mRNA. Translation: AAI10318.1.
BC150261 mRNA. Translation: AAI50262.1.
AY044654 mRNA. Translation: AAK98768.1.
AK000142 mRNA. Translation: BAA90971.1. Sequence problems.
AK026698 mRNA. Translation: BAB15530.1. Different initiation.
AK095322 mRNA. No translation available.
CCDSCCDS13122.1. [Q96L93-1]
CCDS56178.1. [Q96L93-2]
RefSeqNP_001186794.1. NM_001199865.1.
NP_001186795.1. NM_001199866.1. [Q96L93-2]
NP_078980.3. NM_024704.4. [Q96L93-1]
UniGeneHs.101774.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2V14X-ray2.20A1179-1312[»]
ProteinModelPortalQ96L93.
SMRQ96L93. Positions 2-356, 406-563, 1179-1312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120754. 4 interactions.
IntActQ96L93. 2 interactions.
MINTMINT-5225330.

PTM databases

PhosphoSiteQ96L93.

Polymorphism databases

DMDM50403793.

Proteomic databases

MaxQBQ96L93.
PaxDbQ96L93.
PRIDEQ96L93.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354981; ENSP00000347076; ENSG00000089177. [Q96L93-1]
ENST00000355755; ENSP00000347995; ENSG00000089177. [Q96L93-4]
ENST00000408042; ENSP00000384164; ENSG00000089177. [Q96L93-2]
GeneID55614.
KEGGhsa:55614.
UCSCuc002wpe.1. human. [Q96L93-4]
uc002wpf.1. human. [Q96L93-6]
uc002wpg.2. human. [Q96L93-1]
uc010gci.2. human. [Q96L93-2]

Organism-specific databases

CTD55614.
GeneCardsGC20M016201.
HGNCHGNC:15869. KIF16B.
HPAHPA051198.
neXtProtNX_Q96L93.
PharmGKBPA162393227.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOVERGENHBG099335.
KOK17916.
OMALHIDKVG.
OrthoDBEOG77Q4VS.
PhylomeDBQ96L93.
TreeFamTF105221.

Enzyme and pathway databases

BRENDA3.6.4.4. 2681.

Gene expression databases

ArrayExpressQ96L93.
BgeeQ96L93.
CleanExHS_KIF16B.
GenevestigatorQ96L93.

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.
IPR027640. Kinesin-like_fam.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
IPR027417. P-loop_NTPase.
IPR001683. Phox.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PANTHERPTHR24115. PTHR24115. 1 hit.
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]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEPS00411. KINESIN_MOTOR_1. 1 hit.
PS50067. KINESIN_MOTOR_2. 1 hit.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKIF16B. human.
EvolutionaryTraceQ96L93.
GeneWikiKIF16B.
GenomeRNAi55614.
NextBio60192.
PROQ96L93.

Entry information

Entry nameKI16B_HUMAN
AccessionPrimary (citable) accession number: Q96L93
Secondary accession number(s): A6NKJ9 expand/collapse secondary AC list , A7E2A8, B1AKG3, B1AKT7, C9JDN5, C9JI52, C9JSM8, C9JWJ7, Q2TBF5, Q5HYC0, Q5HYK1, Q5JWW3, Q5TFK5, Q86VL9, Q86YS5, Q8IYU0, Q9BQJ8, Q9BQM0, Q9BQM1, Q9BQM5, Q9H5U0, Q9HCI2, Q9NXN9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 128 of the entry and version 2 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

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 20

Human chromosome 20: entries, gene names and cross-references to MIM