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Q14807

- KIF22_HUMAN

UniProt

Q14807 - KIF22_HUMAN

Protein

Kinesin-like protein KIF22

Gene

KIF22

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 5 (26 Sep 2001)
      Previous versions | rss
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    Functioni

    Kinesin family that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi127 – 1348ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: ProtInc
    3. microtubule motor activity Source: ProtInc

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. blood coagulation Source: Reactome
    3. DNA repair Source: InterPro
    4. microtubule-based movement Source: Reactome
    5. mitotic nuclear division Source: ProtInc

    Keywords - Molecular functioni

    Motor protein

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_121399. MHC class II antigen presentation.
    REACT_25201. Kinesins.
    SignaLinkiQ14807.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Kinesin-like protein KIF22
    Alternative name(s):
    Kinesin-like DNA-binding protein
    Kinesin-like protein 4
    Gene namesi
    Name:KIF22
    Synonyms:KID, KNSL4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:6391. KIF22.

    Subcellular locationi

    GO - Cellular componenti

    1. chromatin Source: Ensembl
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. focal adhesion Source: HPA
    5. kinesin complex Source: InterPro
    6. kinetochore Source: ProtInc
    7. microtubule Source: UniProtKB-KW
    8. nucleus Source: HPA
    9. spindle Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Microtubule, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Spondyloepimetaphyseal dysplasia with joint laxity, 2 (SEMDJL2) [MIM:603546]: A bone disease characterized by short stature, distinctive midface retrusion, progressive knee malalignment (genu valgum and/or varum), generalized ligamentous laxity, and mild spinal deformity. Intellectual development is not impaired. Radiographic characteristics include significantly retarded epiphyseal ossification that evolves into epiphyseal dysplasia and precocious osteoarthritis, metaphyseal irregularities and vertical striations, constricted femoral neck, slender metacarpals and metatarsals, and mild thoracolumbar kyphosis or scoliosis with normal or mild platyspondyly. The most distinctive features for differential diagnosis of SEMDJL2 are the slender metacarpals and phalanges and the progressive degeneration of carpal bones; however, these 2 features are evident only in older children and young adults. The soft consistency of cartilage in the airways leads to laryngotracheomalacia with proneness to respiratory obstruction and inspiratory stridor in infancy and childhood.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti148 – 1481P → L in SEMDJL2. 2 Publications
    Corresponds to variant rs193922921 [ dbSNP | Ensembl ].
    VAR_067345
    Natural varianti148 – 1481P → S in SEMDJL2. 1 Publication
    Corresponds to variant rs193922920 [ dbSNP | Ensembl ].
    VAR_067346
    Natural varianti149 – 1491R → L in SEMDJL2. 1 Publication
    VAR_067347
    Natural varianti149 – 1491R → Q in SEMDJL2. 2 Publications
    Corresponds to variant rs193922922 [ dbSNP | Ensembl ].
    VAR_067348

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi603546. phenotype.
    Orphaneti93360. Spondyloepimetaphyseal dysplasia with multiple dislocations.
    PharmGKBiPA30180.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 665665Kinesin-like protein KIF22PRO_0000125433Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei412 – 4121Phosphoserine3 Publications
    Modified residuei427 – 4271Phosphoserine2 Publications
    Modified residuei452 – 4521Phosphoserine1 Publication
    Modified residuei543 – 5431Phosphoserine1 Publication
    Modified residuei562 – 5621Phosphoserine1 Publication
    Modified residuei581 – 5811Phosphoserine1 Publication

    Post-translational modificationi

    Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation.Curated

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14807.
    PaxDbiQ14807.
    PRIDEiQ14807.

    PTM databases

    PhosphoSiteiQ14807.

    Expressioni

    Tissue specificityi

    Expressed in bone, cartilage, joint capsule, ligament, skin, and primary cultured chondrocytes.1 Publication

    Gene expression databases

    ArrayExpressiQ14807.
    BgeeiQ14807.
    CleanExiHS_KIF22.
    GenevestigatoriQ14807.

    Organism-specific databases

    HPAiHPA041076.
    HPA048213.

    Interactioni

    Subunit structurei

    Interacts with FAM83D.2 Publications

    Protein-protein interaction databases

    BioGridi110033. 10 interactions.
    IntActiQ14807. 6 interactions.
    MINTiMINT-156095.
    STRINGi9606.ENSP00000160827.

    Structurei

    Secondary structure

    1
    665
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi45 – 506
    Beta strandi85 – 895
    Beta strandi91 – 944
    Helixi100 – 1078
    Helixi109 – 1113
    Helixi112 – 1154
    Turni116 – 1183
    Beta strandi121 – 1277
    Helixi133 – 1375
    Beta strandi141 – 1444
    Helixi146 – 16116
    Beta strandi167 – 18014
    Beta strandi183 – 1897
    Helixi218 – 22811
    Helixi243 – 2453
    Beta strandi246 – 26015
    Beta strandi265 – 27410
    Helixi299 – 31214
    Helixi320 – 3223
    Helixi324 – 3285
    Turni329 – 3313
    Beta strandi332 – 3343
    Beta strandi338 – 3458
    Helixi349 – 3513
    Helixi352 – 36211
    Beta strandi364 – 3696
    Turni577 – 5793
    Helixi582 – 59817
    Helixi601 – 6066
    Helixi612 – 62514
    Helixi631 – 6366
    Helixi642 – 65817

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EDUNMR-A570-660[»]
    3BFNX-ray2.30A40-400[»]
    ProteinModelPortaliQ14807.
    SMRiQ14807. Positions 40-369, 570-660.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14807.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 368326Kinesin motorPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili465 – 50844Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Kinesin family.PROSITE-ProRule annotation
    Contains 1 kinesin motor domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5059.
    HOGENOMiHOG000007569.
    HOVERGENiHBG052252.
    InParanoidiQ14807.
    KOiK10403.
    OMAiAGQRCGP.
    OrthoDBiEOG7Z69BZ.
    PhylomeDBiQ14807.
    TreeFamiTF105233.

    Family and domain databases

    Gene3Di3.40.850.10. 1 hit.
    InterProiIPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    IPR026986. KIF22.
    IPR027640. Kinesin-like_fam.
    IPR019821. Kinesin_motor_CS.
    IPR001752. Kinesin_motor_dom.
    IPR027417. P-loop_NTPase.
    IPR010994. RuvA_2-like.
    [Graphical view]
    PANTHERiPTHR24115. PTHR24115. 1 hit.
    PTHR24115:SF171. PTHR24115:SF171. 1 hit.
    PfamiPF00225. Kinesin. 1 hit.
    [Graphical view]
    PRINTSiPR00380. KINESINHEAVY.
    SMARTiSM00278. HhH1. 2 hits.
    SM00129. KISc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47781. SSF47781. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEiPS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14807-1) [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

    MAAGGSTQQR RREMAAASAA AISGAGRCRL SKIGATRRPP PARVRVAVRL    50
    RPFVDGTAGA SDPPCVRGMD SCSLEIANWR NHQETLKYQF DAFYGERSTQ 100
    QDIYAGSVQP ILRHLLEGQN ASVLAYGPTG AGKTHTMLGS PEQPGVIPRA 150
    LMDLLQLTRE EGAEGRPWAL SVTMSYLEIY QEKVLDLLDP ASGDLVIRED 200
    CRGNILIPGL SQKPISSFAD FERHFLPASR NRTVGATRLN QRSSRSHAVL 250
    LVKVDQRERL APFRQREGKL YLIDLAGSED NRRTGNKGLR LKESGAINTS 300
    LFVLGKVVDA LNQGLPRVPY RDSKLTRLLQ DSLGGSAHSI LIANIAPERR 350
    FYLDTVSALN FAARSKEVIN RPFTNESLQP HALGPVKLSQ KELLGPPEAK 400
    RARGPEEEEI GSPEPMAAPA SASQKLSPLQ KLSSMDPAML ERLLSLDRLL 450
    ASQGSQGAPL LSTPKRERMV LMKTVEEKDL EIERLKTKQK ELEAKMLAQK 500
    AEEKENHCPT MLRPLSHRTV TGAKPLKKAV VMPLQLIQEQ AASPNAEIHI 550
    LKNKGRKRKL ESLDALEPEE KAEDCWELQI SPELLAHGRQ KILDLLNEGS 600
    ARDLRSLQRI GPKKAQLIVG WRELHGPFSQ VEDLERVEGI TGKQMESFLK 650
    ANILGLAAGQ RCGAS 665
    Length:665
    Mass (Da):73,262
    Last modified:September 26, 2001 - v5
    Checksum:iC6C0AC96741DD387
    GO
    Isoform 2 (identifier: Q14807-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-68: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:597
    Mass (Da):66,307
    Checksum:i4B6D0F60A2426335
    GO

    Sequence cautioni

    The sequence AAC08709.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence EAW80007.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241Missing in BAA33063. (PubMed:9790757)Curated
    Sequence conflicti122 – 1221S → KV in BAA33063. (PubMed:9790757)Curated
    Sequence conflicti135 – 16935HTMLG…GRPWA → THAGQPRATWGDPAGSHGPP AAHKGGGCRGPAMG(PubMed:9790757)CuratedAdd
    BLAST
    Sequence conflicti216 – 2161S → N in BAD97151. 1 PublicationCurated
    Sequence conflicti270 – 2701L → P in BAG35167. (PubMed:14702039)Curated
    Sequence conflicti303 – 3031V → A in BAA33063. (PubMed:9790757)Curated
    Sequence conflicti381 – 3811H → R in BAD97151. 1 PublicationCurated
    Sequence conflicti418 – 45639APASA…SQGSQ → SSSLCLPETQPPTEAKAAWT RPCGAPPQLGPSACLPGEP in BAA33063. (PubMed:9790757)CuratedAdd
    BLAST
    Sequence conflicti505 – 5139ENHCPTMLR → RTIVPQCSG in BAA33063. (PubMed:9790757)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti148 – 1481P → L in SEMDJL2. 2 Publications
    Corresponds to variant rs193922921 [ dbSNP | Ensembl ].
    VAR_067345
    Natural varianti148 – 1481P → S in SEMDJL2. 1 Publication
    Corresponds to variant rs193922920 [ dbSNP | Ensembl ].
    VAR_067346
    Natural varianti149 – 1491R → L in SEMDJL2. 1 Publication
    VAR_067347
    Natural varianti149 – 1491R → Q in SEMDJL2. 2 Publications
    Corresponds to variant rs193922922 [ dbSNP | Ensembl ].
    VAR_067348
    Natural varianti232 – 2321R → Q.1 Publication
    VAR_067349

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6868Missing in isoform 2. 1 PublicationVSP_046428Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017430 mRNA. Translation: BAA33019.2.
    AB017335 Genomic DNA. Translation: BAA33063.1.
    BT007259 mRNA. Translation: AAP35923.1.
    AK294380 mRNA. Translation: BAH11751.1.
    AK312234 mRNA. Translation: BAG35167.1.
    AK316389 mRNA. Translation: BAH14760.1.
    AK223431 mRNA. Translation: BAD97151.1.
    AC002301 Genomic DNA. Translation: AAC08709.1. Sequence problems.
    AC009133 Genomic DNA. No translation available.
    CH471238 Genomic DNA. Translation: EAW80005.1.
    CH471238 Genomic DNA. Translation: EAW80007.1. Sequence problems.
    BC004352 mRNA. Translation: AAH04352.1.
    BC028155 mRNA. Translation: AAH28155.1.
    CCDSiCCDS10653.1. [Q14807-1]
    CCDS58444.1. [Q14807-2]
    RefSeqiNP_001243198.1. NM_001256269.1. [Q14807-2]
    NP_001243199.1. NM_001256270.1. [Q14807-2]
    NP_015556.1. NM_007317.2. [Q14807-1]
    UniGeneiHs.612151.

    Genome annotation databases

    EnsembliENST00000160827; ENSP00000160827; ENSG00000079616. [Q14807-1]
    ENST00000400751; ENSP00000383562; ENSG00000079616. [Q14807-2]
    ENST00000561482; ENSP00000454957; ENSG00000079616. [Q14807-2]
    GeneIDi3835.
    KEGGihsa:3835.
    UCSCiuc002dts.4. human. [Q14807-1]

    Polymorphism databases

    DMDMi19863381.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB017430 mRNA. Translation: BAA33019.2 .
    AB017335 Genomic DNA. Translation: BAA33063.1 .
    BT007259 mRNA. Translation: AAP35923.1 .
    AK294380 mRNA. Translation: BAH11751.1 .
    AK312234 mRNA. Translation: BAG35167.1 .
    AK316389 mRNA. Translation: BAH14760.1 .
    AK223431 mRNA. Translation: BAD97151.1 .
    AC002301 Genomic DNA. Translation: AAC08709.1 . Sequence problems.
    AC009133 Genomic DNA. No translation available.
    CH471238 Genomic DNA. Translation: EAW80005.1 .
    CH471238 Genomic DNA. Translation: EAW80007.1 . Sequence problems.
    BC004352 mRNA. Translation: AAH04352.1 .
    BC028155 mRNA. Translation: AAH28155.1 .
    CCDSi CCDS10653.1. [Q14807-1 ]
    CCDS58444.1. [Q14807-2 ]
    RefSeqi NP_001243198.1. NM_001256269.1. [Q14807-2 ]
    NP_001243199.1. NM_001256270.1. [Q14807-2 ]
    NP_015556.1. NM_007317.2. [Q14807-1 ]
    UniGenei Hs.612151.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EDU NMR - A 570-660 [» ]
    3BFN X-ray 2.30 A 40-400 [» ]
    ProteinModelPortali Q14807.
    SMRi Q14807. Positions 40-369, 570-660.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110033. 10 interactions.
    IntActi Q14807. 6 interactions.
    MINTi MINT-156095.
    STRINGi 9606.ENSP00000160827.

    Chemistry

    ChEMBLi CHEMBL5470.

    PTM databases

    PhosphoSitei Q14807.

    Polymorphism databases

    DMDMi 19863381.

    Proteomic databases

    MaxQBi Q14807.
    PaxDbi Q14807.
    PRIDEi Q14807.

    Protocols and materials databases

    DNASUi 3835.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000160827 ; ENSP00000160827 ; ENSG00000079616 . [Q14807-1 ]
    ENST00000400751 ; ENSP00000383562 ; ENSG00000079616 . [Q14807-2 ]
    ENST00000561482 ; ENSP00000454957 ; ENSG00000079616 . [Q14807-2 ]
    GeneIDi 3835.
    KEGGi hsa:3835.
    UCSCi uc002dts.4. human. [Q14807-1 ]

    Organism-specific databases

    CTDi 3835.
    GeneCardsi GC16P029802.
    HGNCi HGNC:6391. KIF22.
    HPAi HPA041076.
    HPA048213.
    MIMi 603213. gene.
    603546. phenotype.
    neXtProti NX_Q14807.
    Orphaneti 93360. Spondyloepimetaphyseal dysplasia with multiple dislocations.
    PharmGKBi PA30180.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5059.
    HOGENOMi HOG000007569.
    HOVERGENi HBG052252.
    InParanoidi Q14807.
    KOi K10403.
    OMAi AGQRCGP.
    OrthoDBi EOG7Z69BZ.
    PhylomeDBi Q14807.
    TreeFami TF105233.

    Enzyme and pathway databases

    Reactomei REACT_121399. MHC class II antigen presentation.
    REACT_25201. Kinesins.
    SignaLinki Q14807.

    Miscellaneous databases

    EvolutionaryTracei Q14807.
    GeneWikii KIF22.
    GenomeRNAii 3835.
    NextBioi 15075.
    PROi Q14807.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14807.
    Bgeei Q14807.
    CleanExi HS_KIF22.
    Genevestigatori Q14807.

    Family and domain databases

    Gene3Di 3.40.850.10. 1 hit.
    InterProi IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
    IPR026986. KIF22.
    IPR027640. Kinesin-like_fam.
    IPR019821. Kinesin_motor_CS.
    IPR001752. Kinesin_motor_dom.
    IPR027417. P-loop_NTPase.
    IPR010994. RuvA_2-like.
    [Graphical view ]
    PANTHERi PTHR24115. PTHR24115. 1 hit.
    PTHR24115:SF171. PTHR24115:SF171. 1 hit.
    Pfami PF00225. Kinesin. 1 hit.
    [Graphical view ]
    PRINTSi PR00380. KINESINHEAVY.
    SMARTi SM00278. HhH1. 2 hits.
    SM00129. KISc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47781. SSF47781. 1 hit.
    SSF52540. SSF52540. 2 hits.
    PROSITEi PS00411. KINESIN_MOTOR_1. 1 hit.
    PS50067. KINESIN_MOTOR_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Kid, a novel kinesin-like DNA binding protein, is localized to chromosomes and the mitotic spindle."
      Tokai N., Fujimoto-Nishiyama A., Toyoshima Y., Yonemura S., Tsukita S., Inoue J., Yamamoto T.
      EMBO J. 15:457-467(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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] (ISOFORMS 1 AND 2).
      Tissue: Adrenal gland, Amygdala and Testis.
    4. "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] (ISOFORM 1).
    5. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Kidney epithelium.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 1).
      Tissue: Brain and Lung.
    10. "SIAH-1 interacts with alpha-tubulin and degrades the kinesin Kid by the proteasome pathway during mitosis."
      Germani A., Bruzzoni-Giovanelli H., Fellous A., Gisselbrecht S., Varin-Blank N., Calvo F.
      Oncogene 19:5997-6006(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIAH1, DEGRADATION.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. "The spindle protein CHICA mediates localization of the chromokinesin Kid to the mitotic spindle."
      Santamaria A., Nagel S., Sillje H.H.W., Nigg E.A.
      Curr. Biol. 18:723-729(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FAM83D.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-427, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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-412; SER-543; SER-562 AND SER-581, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Whole-exome sequencing identifies mutations of KIF22 in spondyloepimetaphyseal dysplasia with joint laxity, leptodactylic type."
      Min B.J., Kim N., Chung T., Kim O.H., Nishimura G., Chung C.Y., Song H.R., Kim H.W., Lee H.R., Kim J., Kang T.H., Seo M.E., Yang S.D., Kim D.H., Lee S.B., Kim J.I., Seo J.S., Choi J.Y.
      , Kang D., Kim D., Park W.Y., Cho T.J.
      Am. J. Hum. Genet. 89:760-766(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, VARIANTS SEMDJL2 SER-148; LEU-148 AND GLN-149, VARIANT GLN-232.
    17. "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].
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Solution structure of RSGI RUH-070, a C-terminal domain of kinesin-like protein KIF22 from human."
      RIKEN structural genomics initiative (RSGI)
      Submitted (AUG-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 570-660.
    20. Cited for: VARIANTS SEMDJL2 LEU-148; GLN-149 AND LEU-149.

    Entry informationi

    Entry nameiKIF22_HUMAN
    AccessioniPrimary (citable) accession number: Q14807
    Secondary accession number(s): B2R5M0
    , B7Z265, O60845, O94814, Q53F58, Q9BT46
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: September 26, 2001
    Last modified: October 1, 2014
    This is version 153 of the entry and version 5 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 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3