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Q14807 (KIF22_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
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.10 Ref.12

Subcellular location

Nucleus. Cytoplasmcytoskeleton Probable.

Tissue specificity

Expressed in bone, cartilage, joint capsule, ligament, skin, and primary cultured chondrocytes. Ref.16

Post-translational modification

Ubiquitinated; mediated by SIAH1 and leading to its subsequent proteasomal degradation Probable. Ref.10

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Ref.20

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.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Dwarfism
   DomainCoiled coil
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: InterPro

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

microtubule-based movement

Traceable author statement. Source: Reactome

mitosis

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentchromatin

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from direct assay. Source: HPA

kinesin complex

Inferred from electronic annotation. Source: InterPro

kinetochore

Traceable author statement Ref.1. Source: ProtInc

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay. Source: HPA

spindle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA binding

Traceable author statement Ref.1. Source: ProtInc

microtubule motor activity

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14807-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14807-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.
Note: No experimental confirmation available.

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.13 Ref.14 Ref.15
Modified residue4271Phosphoserine Ref.13 Ref.14
Modified residue4521Phosphoserine Ref.11
Modified residue5431Phosphoserine Ref.15
Modified residue5621Phosphoserine Ref.15
Modified residue5811Phosphoserine Ref.15

Natural variations

Alternative sequence1 – 6868Missing in isoform 2.
VSP_046428
Natural variant1481P → L in SEMDJL2. Ref.16 Ref.20
Corresponds to variant rs193922921 [ dbSNP | Ensembl ].
VAR_067345
Natural variant1481P → S in SEMDJL2. Ref.16
Corresponds to variant rs193922920 [ dbSNP | Ensembl ].
VAR_067346
Natural variant1491R → L in SEMDJL2. Ref.20
VAR_067347
Natural variant1491R → Q in SEMDJL2. Ref.16 Ref.20
Corresponds to variant rs193922922 [ dbSNP | Ensembl ].
VAR_067348
Natural variant2321R → Q. Ref.16
VAR_067349

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
Isoform 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

Isoform 2 [UniParc].

Checksum: 4B6D0F60A2426335
Show »

FASTA59766,307

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [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] [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]"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] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]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].
[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]"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] [Europe PMC] [Abstract]
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]"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] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Recurrent dominant mutations affecting two adjacent residues in the motor domain of the monomeric kinesin KIF22 result in skeletal dysplasia and joint laxity."
Boyden E.D., Campos-Xavier A.B., Kalamajski S., Cameron T.L., Suarez P., Tanackovic G., Andria G., Ballhausen D., Briggs M.D., Hartley C., Cohn D.H., Davidson H.R., Hall C., Ikegawa S., Jouk P.S., Konig R., Megarbane A., Nishimura G. expand/collapse author list , Lachman R.S., Mortier G., Rimoin D.L., Rogers R.C., Rossi M., Sawada H., Scott R., Unger S., Valadares E.R., Bateman J.F., Warman M.L., Superti-Furga A., Bonafe L.
Am. J. Hum. Genet. 89:767-772(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SEMDJL2 LEU-148; GLN-149 AND LEU-149.
[21]Erratum
Boyden E.D., Campos-Xavier A.B., Kalamajski S., Cameron T.L., Suarez P., Tanackovic G., Andria G., Ballhausen D., Briggs M.D., Hartley C., Cohn D.H., Davidson H.R., Hall C., Ikegawa S., Jouk P.S., Konig R., Megarbane A., Nishimura G. expand/collapse author list , Lachman R.S., Mortier G., Rimoin D.L., Rogers R.C., Rossi M., Sawada H., Scott R., Unger S., Valadares E.R., Bateman J.F., Warman M.L., Superti-Furga A., Bonafe L.
Am. J. Hum. Genet. 90:170-170(2012)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001243198.1. NM_001256269.1.
NP_001243199.1. NM_001256270.1.
NP_015556.1. NM_007317.2.
UniGeneHs.612151.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EDUNMR-A570-660[»]
3BFNX-ray2.30A40-400[»]
ProteinModelPortalQ14807.
SMRQ14807. Positions 40-397, 570-660.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110033. 10 interactions.
IntActQ14807. 6 interactions.
MINTMINT-156095.
STRING9606.ENSP00000160827.

Chemistry

ChEMBLCHEMBL5470.

PTM databases

PhosphoSiteQ14807.

Polymorphism databases

DMDM19863381.

Proteomic databases

PaxDbQ14807.
PRIDEQ14807.

Protocols and materials databases

DNASU3835.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000160827; ENSP00000160827; ENSG00000079616. [Q14807-1]
ENST00000400751; ENSP00000383562; ENSG00000079616. [Q14807-2]
ENST00000561482; ENSP00000454957; ENSG00000079616. [Q14807-2]
GeneID3835.
KEGGhsa:3835.
UCSCuc002dts.4. human. [Q14807-1]

Organism-specific databases

CTD3835.
GeneCardsGC16P029802.
HGNCHGNC:6391. KIF22.
HPAHPA041076.
HPA048213.
MIM603213. gene.
603546. phenotype.
neXtProtNX_Q14807.
Orphanet93360. Spondyloepimetaphyseal dysplasia with multiple dislocations.
PharmGKBPA30180.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5059.
HOGENOMHOG000007569.
HOVERGENHBG052252.
InParanoidQ14807.
KOK10403.
OMAAGQRCGP.
OrthoDBEOG7Z69BZ.
PhylomeDBQ14807.
TreeFamTF105233.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ14807.

Gene expression databases

ArrayExpressQ14807.
BgeeQ14807.
CleanExHS_KIF22.
GenevestigatorQ14807.

Family and domain databases

Gene3D3.40.850.10. 1 hit.
InterProIPR003583. 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]
PANTHERPTHR24115. PTHR24115. 1 hit.
PTHR24115:SF171. PTHR24115:SF171. 1 hit.
PfamPF00225. Kinesin. 1 hit.
[Graphical view]
PRINTSPR00380. KINESINHEAVY.
SMARTSM00278. HhH1. 2 hits.
SM00129. KISc. 1 hit.
[Graphical view]
SUPFAMSSF47781. SSF47781. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEPS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14807.
GeneWikiKIF22.
GenomeRNAi3835.
NextBio15075.
PROQ14807.
SOURCESearch...

Entry information

Entry nameKIF22_HUMAN
AccessionPrimary (citable) accession number: Q14807
Secondary accession number(s): B2R5M0 expand/collapse secondary AC list , B7Z265, O60845, O94814, Q53F58, Q9BT46
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: September 26, 2001
Last modified: April 16, 2014
This is version 148 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

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