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Reviewed, UniProtKB/Swiss-Prot Q14807 (KIF22_HUMAN)

Last modified June 16, 2009. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Kinesin-like protein KIF22
Alternative name(s):
    Kinesin-like DNA-binding protein
    Kinesin-like protein 4
Gene names
Name: KIF22
Synonyms: KID, KNSL4
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Subunit structure

Interacts with FAM83D. Ref.9 Ref.13

Subcellular location

Nucleus.

Post-translational modification

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

Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.10 Ref.11 Ref.12

Sequence similarities

Belongs to the kinesin-like protein family.

Contains 1 kinesin-motor domain.

Sequence caution

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CRKP461081EBI-715834,EBI-886

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 665665Kinesin-like protein KIF22
PRO_0000125433

Regions

Domain40 – 299260Kinesin-motor
Nucleotide binding127 – 1348ATP By similarity
Coiled coil465 – 50844 Potential

Amino acid modifications

Modified residue4121Phosphoserine Ref.12
Modified residue4271Phosphoserine Ref.12
Modified residue4521Phosphoserine Ref.11
Modified residue5431Phosphoserine Ref.10
Modified residue5621Phosphoserine Ref.10
Modified residue5811Phosphoserine Ref.10

Experimental info

Sequence conflict241Missing in BAA33063. Ref.2
Sequence conflict1221S → KV in BAA33063. Ref.2
Sequence conflict135 – 16935HTMLG…GRPWA → THAGQPRATWGDPAGSHGPP AAHKGGGCRGPAMG Ref.2
Sequence conflict2161S → N in BAD97151. Ref.5
Sequence conflict2701L → P in BAG35167. Ref.3
Sequence conflict3031V → A in BAA33063. Ref.2
Sequence conflict3811H → R in BAD97151. Ref.5
Sequence conflict418 – 45639APASA…SQGSQ → SSSLCLPETQPPTEAKAAWT RPCGAPPQLGPSACLPGEP in BAA33063. Ref.2
Sequence conflict505 – 5139ENHCPTMLR → RTIVPQCSG in BAA33063. Ref.2

Secondary structure

........................................................... 665
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q14807-1 [UniParc].

Last modified September 26, 2001. Version 5.
Checksum: C6C0AC96741DD387

FASTA66573,262
        10         20         30         40         50         60 
MAAGGSTQQR RREMAAASAA AISGAGRCRL SKIGATRRPP PARVRVAVRL RPFVDGTAGA 

        70         80         90        100        110        120 
SDPPCVRGMD SCSLEIANWR NHQETLKYQF DAFYGERSTQ QDIYAGSVQP ILRHLLEGQN 

       130        140        150        160        170        180 
ASVLAYGPTG AGKTHTMLGS PEQPGVIPRA LMDLLQLTRE EGAEGRPWAL SVTMSYLEIY 

       190        200        210        220        230        240 
QEKVLDLLDP ASGDLVIRED CRGNILIPGL SQKPISSFAD FERHFLPASR NRTVGATRLN 

       250        260        270        280        290        300 
QRSSRSHAVL LVKVDQRERL APFRQREGKL YLIDLAGSED NRRTGNKGLR LKESGAINTS 

       310        320        330        340        350        360 
LFVLGKVVDA LNQGLPRVPY RDSKLTRLLQ DSLGGSAHSI LIANIAPERR FYLDTVSALN 

       370        380        390        400        410        420 
FAARSKEVIN RPFTNESLQP HALGPVKLSQ KELLGPPEAK RARGPEEEEI GSPEPMAAPA 

       430        440        450        460        470        480 
SASQKLSPLQ KLSSMDPAML ERLLSLDRLL ASQGSQGAPL LSTPKRERMV LMKTVEEKDL 

       490        500        510        520        530        540 
EIERLKTKQK ELEAKMLAQK AEEKENHCPT MLRPLSHRTV TGAKPLKKAV VMPLQLIQEQ 

       550        560        570        580        590        600 
AASPNAEIHI LKNKGRKRKL ESLDALEPEE KAEDCWELQI SPELLAHGRQ KILDLLNEGS 

       610        620        630        640        650        660 
ARDLRSLQRI GPKKAQLIVG WRELHGPFSQ VEDLERVEGI TGKQMESFLK ANILGLAAGQ 


RCGAS 

« Hide

References

« Hide 'large scale' references
[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: 8599929] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Human genes for KNSL4 and MAZ are located close to one another on chromosome 16p11.2."
Song J., Murakami H., Yang Z.Q., Koga C., Adati N., Murata T., Geltinger C., Saito-Ohara F., Ikeuchi T., Matsumura M., Itakura K., Kanazawa I., Sun K., Yokoyama K.K.
Genomics 52:374-377(1998) [PubMed: 9790757] [Abstract]
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. 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[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].
[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].
Tissue: Kidney epithelium.
[6]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed: 10493829] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Lung.
[9]"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: 11146551] [Abstract]
Cited for: INTERACTION WITH SIAH1, DEGRADATION.
[10]"Phosphoproteome analysis of the human mitotic spindle."
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543; SER-562 AND SER-581, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, MASS SPECTROMETRY.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412 AND SER-427, MASS SPECTROMETRY.
[13]"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: 18485706] [Abstract]
Cited for: INTERACTION WITH FAM83D.
[14]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB017430 mRNA. Translation: BAA33019.2.
AB017335 Genomic DNA. Translation: BAA33063.1.
BT007259 mRNA. Translation: AAP35923.1.
AK312234 mRNA. Translation: BAG35167.1.
AK223431 mRNA. Translation: BAD97151.1.
AC002301 Genomic DNA. Translation: AAC08709.1. Sequence problems.
CH471238 Genomic DNA. Translation: EAW80007.1. Sequence problems.
BC004352 mRNA. Translation: AAH04352.1.
BC028155 mRNA. Translation: AAH28155.1.
IPIIPI00000769.
RefSeqNP_015556.1.
UniGeneHs.613351

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2EDUNMR-A570-660[»]
3BFNX-ray2.30A40-400[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ14807. 4 interactions.

PTM databases

PhosphoSiteQ14807.

Proteomic databases

PRIDEQ14807.

Genome annotation databases

EnsemblENSG00000079616. Homo sapiens. [Contig view]
GeneID3835.
KEGGhsa:3835.

Organism-specific databases

GeneCardsGC16P029709.
H-InvDBHIX0012922.
HIX0059648.
HGNCHGNC:6391. KIF22.
MIM603213. gene.
PharmGKBPA30180.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ14807.
OMAQ14807. LLNEGSA.

Gene expression databases

BgeeQ14807.
CleanExHS_KIF22.
GermOnlineENSG00000079616. Homo sapiens.

Family and domain databases

InterProIPR003583. Helix-hairpin-helix_DNA-bd.
IPR001752. Kinesin_motor.
IPR019821. Kinesin_motor_CS.
[Graphical view]
Gene3DG3DSA:3.40.850.10. kinesin_motor. 1 hit.
PfamPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00278. HhH1. 2 hits.
SM00129. KISc. 1 hit.
[Graphical view]
PROSITEPS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio15075.
SOURCESearch...

Entry information

Entry nameKIF22_HUMAN
AccessionPrimary (citable) accession number: Q14807
Secondary accession number(s): B2R5M0 expand/collapse secondary AC list , O60845, O94814, Q53F58, Q9BT46
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: September 26, 2001
Last modified: June 16, 2009
This is version 100 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents