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Q14807

- KIF22_HUMAN

UniProt

Q14807 - KIF22_HUMAN

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Protein

Kinesin-like protein KIF22

Gene

KIF22

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. ATPase activity Source: RefGenome
  2. ATP binding Source: UniProtKB-KW
  3. DNA binding Source: ProtInc
  4. microtubule motor activity Source: RefGenome

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. ATP catabolic process Source: GOC
  3. blood coagulation Source: Reactome
  4. DNA repair Source: InterPro
  5. microtubule-based movement Source: RefGenome
  6. mitotic nuclear division Source: ProtInc
Complete GO annotation...

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: RefGenome
  6. kinetochore Source: ProtInc
  7. microtubule Source: UniProtKB-KW
  8. nucleus Source: HPA
  9. spindle Source: Ensembl
Complete GO annotation...

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

BgeeiQ14807.
CleanExiHS_KIF22.
ExpressionAtlasiQ14807. baseline and differential.
GenevestigatoriQ14807.

Organism-specific databases

HPAiHPA041076.
HPA048213.

Interactioni

Subunit structurei

Interacts with FAM83D.2 Publications

Protein-protein interaction databases

BioGridi110033. 11 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 – 506Combined sources
Beta strandi85 – 895Combined sources
Beta strandi91 – 944Combined sources
Helixi100 – 1078Combined sources
Helixi109 – 1113Combined sources
Helixi112 – 1154Combined sources
Turni116 – 1183Combined sources
Beta strandi121 – 1277Combined sources
Helixi133 – 1375Combined sources
Beta strandi141 – 1444Combined sources
Helixi146 – 16116Combined sources
Beta strandi167 – 18014Combined sources
Beta strandi183 – 1897Combined sources
Helixi218 – 22811Combined sources
Helixi243 – 2453Combined sources
Beta strandi246 – 26015Combined sources
Beta strandi265 – 27410Combined sources
Helixi299 – 31214Combined sources
Helixi320 – 3223Combined sources
Helixi324 – 3285Combined sources
Turni329 – 3313Combined sources
Beta strandi332 – 3343Combined sources
Beta strandi338 – 3458Combined sources
Helixi349 – 3513Combined sources
Helixi352 – 36211Combined sources
Beta strandi364 – 3696Combined sources
Turni577 – 5793Combined sources
Helixi582 – 59817Combined sources
Helixi601 – 6066Combined sources
Helixi612 – 62514Combined sources
Helixi631 – 6366Combined sources
Helixi642 – 65817Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00770000120451.
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

        10         20         30         40         50
MAAGGSTQQR RREMAAASAA AISGAGRCRL SKIGATRRPP PARVRVAVRL
60 70 80 90 100
RPFVDGTAGA SDPPCVRGMD SCSLEIANWR NHQETLKYQF DAFYGERSTQ
110 120 130 140 150
QDIYAGSVQP ILRHLLEGQN ASVLAYGPTG AGKTHTMLGS PEQPGVIPRA
160 170 180 190 200
LMDLLQLTRE EGAEGRPWAL SVTMSYLEIY QEKVLDLLDP ASGDLVIRED
210 220 230 240 250
CRGNILIPGL SQKPISSFAD FERHFLPASR NRTVGATRLN QRSSRSHAVL
260 270 280 290 300
LVKVDQRERL APFRQREGKL YLIDLAGSED NRRTGNKGLR LKESGAINTS
310 320 330 340 350
LFVLGKVVDA LNQGLPRVPY RDSKLTRLLQ DSLGGSAHSI LIANIAPERR
360 370 380 390 400
FYLDTVSALN FAARSKEVIN RPFTNESLQP HALGPVKLSQ KELLGPPEAK
410 420 430 440 450
RARGPEEEEI GSPEPMAAPA SASQKLSPLQ KLSSMDPAML ERLLSLDRLL
460 470 480 490 500
ASQGSQGAPL LSTPKRERMV LMKTVEEKDL EIERLKTKQK ELEAKMLAQK
510 520 530 540 550
AEEKENHCPT MLRPLSHRTV TGAKPLKKAV VMPLQLIQEQ AASPNAEIHI
560 570 580 590 600
LKNKGRKRKL ESLDALEPEE KAEDCWELQI SPELLAHGRQ KILDLLNEGS
610 620 630 640 650
ARDLRSLQRI GPKKAQLIVG WRELHGPFSQ VEDLERVEGI TGKQMESFLK
660
ANILGLAAGQ RCGAS
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. Curated
The sequence EAW80007.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 11 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.
GeneTreei ENSGT00770000120451.
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

Bgeei Q14807.
CleanExi HS_KIF22.
ExpressionAtlasi Q14807. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 155 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

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