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Q96L93

- KI16B_HUMAN

UniProt

Q96L93 - KI16B_HUMAN

Protein

Kinesin-like protein KIF16B

Gene

KIF16B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi102 – 1098ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatidylinositol-3,4,5-trisphosphate binding Source: UniProtKB
    3. phosphatidylinositol-3,4-bisphosphate binding Source: UniProtKB
    4. phosphatidylinositol-3,5-bisphosphate binding Source: UniProtKB
    5. phosphatidylinositol-3-phosphate binding Source: UniProtKB
    6. plus-end-directed microtubule motor activity Source: UniProtKB

    GO - Biological processi

    1. early endosome to late endosome transport Source: UniProtKB
    2. endoderm development Source: UniProtKB
    3. epidermal growth factor receptor signaling pathway Source: UniProtKB
    4. fibroblast growth factor receptor signaling pathway Source: UniProtKB
    5. formation of primary germ layer Source: UniProtKB
    6. Golgi to endosome transport Source: UniProtKB
    7. microtubule-based movement Source: InterPro
    8. receptor catabolic process Source: UniProtKB
    9. regulation of receptor recycling Source: UniProtKB

    Keywords - Molecular functioni

    Motor protein

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi3.6.4.4. 2681.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinesin-like protein KIF16B
    Alternative name(s):
    Sorting nexin-23
    Gene namesi
    Name:KIF16B
    Synonyms:C20orf23, KIAA1590, SNX23
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15869. KIF16B.

    Subcellular locationi

    Cytoplasmcytoskeleton Curated. 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.

    GO - Cellular componenti

    1. early endosome Source: UniProtKB
    2. early endosome membrane Source: UniProtKB-SubCell
    3. endosome Source: UniProtKB
    4. kinesin complex Source: InterPro
    5. microtubule Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Endosome, Membrane, Microtubule

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi109 – 1091S → A: Impairs plus end-directed microtubule-dependent motor activity, leading to impair EGFR recycling. 1 Publication
    Mutagenesisi1220 – 12201R → A: Abolishes PtdIns(3)P-binding. 1 Publication
    Mutagenesisi1225 – 12251R → A: Induces a 3-fold decrease in PtdIns(3)P-binding; when associated with A-1229 and A-1232. 1 Publication
    Mutagenesisi1229 – 12291K → A: Induces a 3-fold decrease in PtdIns(3)P-binding; when associated with A-1225 and A-1232. 1 Publication
    Mutagenesisi1232 – 12321K → A: Induces a 3-fold decrease in PtdIns(3)P-binding; when associated with A-1225 and A-1229. 1 Publication
    Mutagenesisi1248 – 12481L → 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. 1 Publication
    Mutagenesisi1248 – 12481L → V: Induces a 6-fold decrease in PtdIns(3)P-binding. 1 Publication
    Mutagenesisi1249 – 12491F → 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. 1 Publication
    Mutagenesisi1260 – 12601R → A: Induces a 30-fold decrease in PtdIns(3)P-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA162393227.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13171317Kinesin-like protein KIF16BPRO_0000125466Add
    BLAST

    Post-translational modificationi

    Isoform 4 is ubiquitinated at Lys-685.

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ96L93.
    PaxDbiQ96L93.
    PRIDEiQ96L93.

    PTM databases

    PhosphoSiteiQ96L93.

    Expressioni

    Tissue specificityi

    Primarily expressed in brain. Also present in kidney, liver, intestine, placenta, leukocytes, heart and skeletal muscle (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ96L93.
    BgeeiQ96L93.
    CleanExiHS_KIF16B.
    GenevestigatoriQ96L93.

    Organism-specific databases

    HPAiHPA051198.

    Interactioni

    Subunit structurei

    Interacts with RAB14 By similarity. Interacts with PTPN21.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi120754. 4 interactions.
    IntActiQ96L93. 2 interactions.
    MINTiMINT-5225330.

    Structurei

    Secondary structure

    1
    1317
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1184 – 119613
    Beta strandi1201 – 121010
    Beta strandi1213 – 12197
    Helixi1221 – 123414
    Helixi1236 – 12405
    Helixi1254 – 127724
    Helixi1294 – 13007
    Helixi1302 – 13043

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V14X-ray2.20A1179-1312[»]
    ProteinModelPortaliQ96L93.
    SMRiQ96L93. Positions 2-356, 406-563, 1179-1312.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96L93.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 358356Kinesin motorPROSITE-ProRule annotationAdd
    BLAST
    Domaini478 – 52952FHAAdd
    BLAST
    Domaini1182 – 1296115PXPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili370 – 42556Sequence AnalysisAdd
    BLAST
    Coiled coili595 – 882288Sequence AnalysisAdd
    BLAST
    Coiled coili936 – 1087152Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi597 – 1070474Glu-richAdd
    BLAST

    Domaini

    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).2 Publications

    Sequence similaritiesi

    Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation
    Contains 1 FHA domain.Curated
    Contains 1 kinesin motor domain.PROSITE-ProRule annotation
    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5059.
    HOVERGENiHBG099335.
    KOiK17916.
    OMAiLHIDKVG.
    OrthoDBiEOG77Q4VS.
    PhylomeDBiQ96L93.
    TreeFamiTF105221.

    Family and domain databases

    Gene3Di2.60.200.20. 1 hit.
    3.30.1520.10. 1 hit.
    3.40.850.10. 1 hit.
    InterProiIPR000253. 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]
    PANTHERiPTHR24115. PTHR24115. 1 hit.
    PfamiPF00498. FHA. 1 hit.
    PF00225. Kinesin. 1 hit.
    PF00787. PX. 1 hit.
    [Graphical view]
    PRINTSiPR00380. KINESINHEAVY.
    SMARTiSM00240. FHA. 1 hit.
    SM00129. KISc. 1 hit.
    SM00312. PX. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF64268. SSF64268. 1 hit.
    PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    PS50195. PX. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96L93-1) [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

    MASVKVAVRV RPMNRREKDL EAKFIIQMEK SKTTITNLKI PEGGTGDSGR     50
    ERTKTFTYDF SFYSADTKSP DYVSQEMVFK TLGTDVVKSA FEGYNACVFA 100
    YGQTGSGKSY TMMGNSGDSG LIPRICEGLF SRINETTRWD EASFRTEVSY 150
    LEIYNERVRD LLRRKSSKTF NLRVREHPKE GPYVEDLSKH LVQNYGDVEE 200
    LMDAGNINRT TAATGMNDVS SRSHAIFTIK FTQAKFDSEM PCETVSKIHL 250
    VDLAGSERAD ATGATGVRLK EGGNINKSLV TLGNVISALA DLSQDAANTL 300
    AKKKQVFVPY RDSVLTWLLK DSLGGNSKTI MIATISPADV NYGETLSTLR 350
    YANRAKNIIN KPTINEDANV KLIRELRAEI ARLKTLLAQG NQIALLDSPT 400
    ALSMEEKLQQ NEARVQELTK EWTNKWNETQ NILKEQTLAL RKEGIGVVLD 450
    SELPHLIGID DDLLSTGIIL YHLKEGQTYV GRDDASTEQD IVLHGLDLES 500
    EHCIFENIGG TVTLIPLSGS QCSVNGVQIV EATHLNQGAV ILLGRTNMFR 550
    FNHPKEAAKL REKRKSGLLS SFSLSMTDLS KSRENLSAVM LYNPGLEFER 600
    QQREELEKLE SKRKLIEEME EKQKSDKAEL ERMQQEVETQ RKETEIVQLQ 650
    IRKQEESLKR RSFHIENKLK DLLAEKEKFE EERLREQQEI ELQKKRQEEE 700
    TFLRVQEELQ RLKELNNNEK AEKFQIFQEL DQLQKEKDEQ YAKLELEKKR 750
    LEEQEKEQVM LVAHLEEQLR EKQEMIQLLR RGEVQWVEEE KRDLEGIRES 800
    LLRVKEARAG GDEDGEELEK AQLRFFEFKR RQLVKLVNLE KDLVQQKDIL 850
    KKEVQEEQEI LECLKCEHDK ESRLLEKHDE SVTDVTEVPQ DFEKIKPVEY 900
    RLQYKERQLQ YLLQNHLPTL LEEKQRAFEI LDRGPLSLDN TLYQVEKEME 950
    EKEEQLAQYQ ANANQLQKLQ ATFEFTANIA RQEEKVRKKE KEILESREKQ 1000
    QREALERALA RLERRHSALQ RHSTLGMEIE EQRQKLASLN SGSREQSGLQ 1050
    ASLEAEQEAL EKDQERLEYE IQQLKQKIYE VDGVQKDHHG TLEGKVASSS 1100
    LPVSAEKSHL VPLMDARINA YIEEEVQRRL QDLHRVISEG CSTSADTMKD 1150
    NEKLHNGTIQ RKLKYERMVS RSLGANPDDL KDPIKISIPR YVLCGQGKDA 1200
    HFEFEVKITV LDETWTVFRR YSRFREMHKT LKLKYAELAA LEFPPKKLFG 1250
    NKDERVIAER RSHLEKYLRD FFSVMLQSAT SPLHINKVGL TLSKHTICEF 1300
    SPFFKKGVFD YSSHGTG 1317
    Length:1,317
    Mass (Da):152,011
    Last modified:July 19, 2004 - v2
    Checksum:i278E9CB88D9C04DF
    GO
    Isoform 2 (identifier: Q96L93-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1167-1317: RMVSRSLGAN...VFDYSSHGTG → LCRDLLCVLM...LWLISHLTRL

    Note: Ubiquitinated at position 685.

    Show »
    Length:1,392
    Mass (Da):159,831
    Checksum:i85A4365F83AADDB9
    GO
    Isoform 3 (identifier: Q96L93-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1208-1237: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,287
    Mass (Da):148,211
    Checksum:i9BA79E2857090F5F
    GO
    Isoform 4 (identifier: Q96L93-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         685-840: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,161
    Mass (Da):132,866
    Checksum:i078AB4C77FBAA4C3
    GO
    Isoform 5 (identifier: Q96L93-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1167-1207: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,276
    Mass (Da):147,398
    Checksum:i430E508AEE6E2E12
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181K → E in AK095322. (PubMed:14702039)Curated
    Sequence conflicti274 – 2741N → D in CAI46105. (PubMed:17974005)Curated
    Sequence conflicti583 – 5831R → H in BAA90971. (PubMed:14702039)Curated
    Sequence conflicti649 – 6491L → H in CAI46266. (PubMed:17974005)Curated
    Sequence conflicti1056 – 10572EQ → SE in AAH34984. (PubMed:15489334)Curated
    Sequence conflicti1100 – 11001S → N in CAI46105. (PubMed:17974005)Curated
    Sequence conflicti1108 – 11081S → L in AAH34984. (PubMed:15489334)Curated
    Sequence conflicti1244 – 12441P → A in AAO17292. 1 PublicationCurated
    Sequence conflicti1244 – 12441P → A in BAB15530. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti772 – 7721K → T in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036218
    Natural varianti810 – 8101G → R.
    Corresponds to variant rs2236145 [ dbSNP | Ensembl ].
    VAR_049700
    Natural varianti824 – 8241R → S.
    Corresponds to variant rs2236144 [ dbSNP | Ensembl ].
    VAR_019396
    Natural varianti999 – 9991K → N.
    Corresponds to variant rs8116503 [ dbSNP | Ensembl ].
    VAR_065248
    Natural varianti1027 – 10271M → T.3 Publications
    Corresponds to variant rs6034464 [ dbSNP | Ensembl ].
    VAR_019397
    Natural varianti1119 – 11191N → S.
    Corresponds to variant rs8123195 [ dbSNP | Ensembl ].
    VAR_019398

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei685 – 840156Missing in isoform 4. 1 PublicationVSP_015858Add
    BLAST
    Alternative sequencei1167 – 1317151RMVSR…SHGTG → LCRDLLCVLMPEPDAAACAN HPLLQQDLVQLSLDWKTEIP DLVLPNGVQVSSKFQTTLVD MIYFLHGNMEVNVPSLAEVQ LLLYTTVKVMGDSGHDQCQS LVLLNTHIALVKEDCVFYPR IRSRNIPPPGAQFDVIKCHA LSEFRCVVVPEKKNVSTVEL VFLQKLKPSVGSRNSPPEHL QEAPNVQLFTTPLYLQGSQN VAPEVWKLTFNSQDEALWLI SHLTRL in isoform 2. 2 PublicationsVSP_010851Add
    BLAST
    Alternative sequencei1167 – 120741Missing in isoform 5. 1 PublicationVSP_041318Add
    BLAST
    Alternative sequencei1208 – 123730Missing in isoform 3. 1 PublicationVSP_010852Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS13122.1. [Q96L93-1]
    CCDS56178.1. [Q96L93-2]
    RefSeqiNP_001186794.1. NM_001199865.1.
    NP_001186795.1. NM_001199866.1. [Q96L93-2]
    NP_078980.3. NM_024704.4. [Q96L93-1]
    UniGeneiHs.101774.

    Genome annotation databases

    EnsembliENST00000354981; ENSP00000347076; ENSG00000089177. [Q96L93-1]
    ENST00000355755; ENSP00000347995; ENSG00000089177. [Q96L93-4]
    ENST00000408042; ENSP00000384164; ENSG00000089177. [Q96L93-2]
    GeneIDi55614.
    KEGGihsa:55614.
    UCSCiuc002wpe.1. human. [Q96L93-4]
    uc002wpf.1. human. [Q96L93-6]
    uc002wpg.2. human. [Q96L93-1]
    uc010gci.2. human. [Q96L93-2]

    Polymorphism databases

    DMDMi50403793.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS13122.1. [Q96L93-1 ]
    CCDS56178.1. [Q96L93-2 ]
    RefSeqi NP_001186794.1. NM_001199865.1.
    NP_001186795.1. NM_001199866.1. [Q96L93-2 ]
    NP_078980.3. NM_024704.4. [Q96L93-1 ]
    UniGenei Hs.101774.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V14 X-ray 2.20 A 1179-1312 [» ]
    ProteinModelPortali Q96L93.
    SMRi Q96L93. Positions 2-356, 406-563, 1179-1312.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120754. 4 interactions.
    IntActi Q96L93. 2 interactions.
    MINTi MINT-5225330.

    PTM databases

    PhosphoSitei Q96L93.

    Polymorphism databases

    DMDMi 50403793.

    Proteomic databases

    MaxQBi Q96L93.
    PaxDbi Q96L93.
    PRIDEi Q96L93.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354981 ; ENSP00000347076 ; ENSG00000089177 . [Q96L93-1 ]
    ENST00000355755 ; ENSP00000347995 ; ENSG00000089177 . [Q96L93-4 ]
    ENST00000408042 ; ENSP00000384164 ; ENSG00000089177 . [Q96L93-2 ]
    GeneIDi 55614.
    KEGGi hsa:55614.
    UCSCi uc002wpe.1. human. [Q96L93-4 ]
    uc002wpf.1. human. [Q96L93-6 ]
    uc002wpg.2. human. [Q96L93-1 ]
    uc010gci.2. human. [Q96L93-2 ]

    Organism-specific databases

    CTDi 55614.
    GeneCardsi GC20M016201.
    HGNCi HGNC:15869. KIF16B.
    HPAi HPA051198.
    neXtProti NX_Q96L93.
    PharmGKBi PA162393227.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5059.
    HOVERGENi HBG099335.
    KOi K17916.
    OMAi LHIDKVG.
    OrthoDBi EOG77Q4VS.
    PhylomeDBi Q96L93.
    TreeFami TF105221.

    Enzyme and pathway databases

    BRENDAi 3.6.4.4. 2681.

    Miscellaneous databases

    ChiTaRSi KIF16B. human.
    EvolutionaryTracei Q96L93.
    GeneWikii KIF16B.
    GenomeRNAii 55614.
    NextBioi 60192.
    PROi Q96L93.

    Gene expression databases

    ArrayExpressi Q96L93.
    Bgeei Q96L93.
    CleanExi HS_KIF16B.
    Genevestigatori Q96L93.

    Family and domain databases

    Gene3Di 2.60.200.20. 1 hit.
    3.30.1520.10. 1 hit.
    3.40.850.10. 1 hit.
    InterProi IPR000253. 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 ]
    PANTHERi PTHR24115. PTHR24115. 1 hit.
    Pfami PF00498. FHA. 1 hit.
    PF00225. Kinesin. 1 hit.
    PF00787. PX. 1 hit.
    [Graphical view ]
    PRINTSi PR00380. KINESINHEAVY.
    SMARTi SM00240. FHA. 1 hit.
    SM00129. KISc. 1 hit.
    SM00312. PX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    SSF52540. SSF52540. 1 hit.
    SSF64268. SSF64268. 1 hit.
    PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    PS50195. PX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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.
      , 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-772.

    Entry informationi

    Entry nameiKI16B_HUMAN
    AccessioniPrimary (citable) accession number: Q96L93
    Secondary accession number(s): A6NKJ9
    , A7E2A8, B1AKG3, B1AKT7, C9JDN5, C9JI52, C9JSM8, C9JWJ7, Q2TBF5, Q5HYC0, Q5HYK1, Q5JWW3, Q5TFK5, Q86VL9, Q86YS5, Q8IYU0, Q9BQJ8, Q9BQM0, Q9BQM1, Q9BQM5, Q9H5U0, Q9HCI2, Q9NXN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: July 19, 2004
    Last modified: October 1, 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 20
      Human chromosome 20: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3