Q14807 (KIF22_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kinesin-like protein KIF22

Alternative name(s):
Kinesin-like DNA-binding protein
Kinesin-like protein 4

Gene names

Name:	KIF22
Synonyms:	KID, KNSL4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	665 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton 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.19
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 component	Cytoplasm Cytoskeleton Microtubule Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Dwarfism
Domain	Coiled coil
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA 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_component	chromatin Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome focal adhesion Inferred from direct assay. Source: HPA kinetochore Traceable author statement Ref.1. Source: ProtInc microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Inferred from electronic annotation. Source: InterPro nucleus Inferred from direct assay. Source: HPA spindle Inferred from electronic annotation. Source: Compara
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 665

665

Kinesin-like protein KIF22

PRO_0000125433

Regions

Domain

40 – 299

260

Kinesin-motor

Nucleotide binding

127 – 134

8

ATP By similarity

Coiled coil

465 – 508

44

Potential

Amino acid modifications

Modified residue

412

1

Phosphoserine Ref.13 Ref.14 Ref.15

Modified residue

427

1

Phosphoserine Ref.13 Ref.14

Modified residue

452

1

Phosphoserine Ref.11

Modified residue

543

1

Phosphoserine Ref.15

Modified residue

562

1

Phosphoserine Ref.15

Modified residue

581

1

Phosphoserine Ref.15

Natural variations

Alternative sequence

1 – 68

68

Missing in isoform 2.

VSP_046428

Natural variant

148

1

P → L in SEMDJL2. Ref.16 Ref.19
Corresponds to variant rs193922921 [ dbSNP | Ensembl ].

VAR_067345

Natural variant

148

1

P → S in SEMDJL2. Ref.16
Corresponds to variant rs193922920 [ dbSNP | Ensembl ].

VAR_067346

Natural variant

149

1

R → L in SEMDJL2. Ref.19

VAR_067347

Natural variant

149

1

R → Q in SEMDJL2. Ref.16 Ref.19
Corresponds to variant rs193922922 [ dbSNP | Ensembl ].

VAR_067348

Natural variant

232

1

R → Q. Ref.16

VAR_067349

Experimental info

Sequence conflict

24

1

Missing in BAA33063. Ref.2

Sequence conflict

122

1

S → KV in BAA33063. Ref.2

Sequence conflict

135 – 169

35

HTMLG…GRPWA → THAGQPRATWGDPAGSHGPP AAHKGGGCRGPAMG Ref.2

Sequence conflict

216

1

S → N in BAD97151. Ref.5

Sequence conflict

270

1

L → P in BAG35167. Ref.3

Sequence conflict

303

1

V → A in BAA33063. Ref.2

Sequence conflict

381

1

H → R in BAD97151. Ref.5

Sequence conflict

418 – 456

39

APASA…SQGSQ → SSSLCLPETQPPTEAKAAWT RPCGAPPQLGPSACLPGEP in BAA33063. Ref.2

Sequence conflict

505 – 513

9

ENHCPTMLR → RTIVPQCSG in BAA33063. Ref.2

Secondary structure

1

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665

Helix Strand Turn

Details...

Beta strand

45 – 50

6

Beta strand

85 – 89

5

Beta strand

91 – 94

4

Helix

100 – 107

8

Helix

109 – 111

3

Helix

112 – 115

4

Turn

116 – 118

3

Beta strand

121 – 127

7

Helix

133 – 137

5

Beta strand

141 – 144

4

Helix

146 – 161

16

Beta strand

167 – 180

14

Beta strand

183 – 189

7

Helix

218 – 228

11

Helix

243 – 245

3

Beta strand

246 – 260

15

Beta strand

265 – 274

10

Helix

299 – 312

14

Helix

320 – 322

3

Helix

324 – 328

5

Turn

329 – 331

3

Beta strand

332 – 334

3

Beta strand

338 – 345

8

Helix

349 – 351

3

Helix

352 – 362

11

Beta strand

364 – 369

6

Turn

577 – 579

3

Helix

582 – 598

17

Helix

601 – 606

6

Helix

612 – 625

14

Helix

631 – 636

6

Helix

642 – 658

17

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 26, 2001. Version 5. Checksum: C6C0AC96741DD387	FASTA	665	73,262
	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
	Isoform 2 [UniParc]. Checksum: 4B6D0F60A2426335	FASTA	597	66,307
	10 20 30 40 50 60 MDSCSLEIAN WRNHQETLKY QFDAFYGERS TQQDIYAGSV QPILRHLLEG QNASVLAYGP 70 80 90 100 110 120 TGAGKTHTML GSPEQPGVIP RALMDLLQLT REEGAEGRPW ALSVTMSYLE IYQEKVLDLL 130 140 150 160 170 180 DPASGDLVIR EDCRGNILIP GLSQKPISSF ADFERHFLPA SRNRTVGATR LNQRSSRSHA 190 200 210 220 230 240 VLLVKVDQRE RLAPFRQREG KLYLIDLAGS EDNRRTGNKG LRLKESGAIN TSLFVLGKVV 250 260 270 280 290 300 DALNQGLPRV PYRDSKLTRL LQDSLGGSAH SILIANIAPE RRFYLDTVSA LNFAARSKEV 310 320 330 340 350 360 INRPFTNESL QPHALGPVKL SQKELLGPPE AKRARGPEEE EIGSPEPMAA PASASQKLSP 370 380 390 400 410 420 LQKLSSMDPA MLERLLSLDR LLASQGSQGA PLLSTPKRER MVLMKTVEEK DLEIERLKTK 430 440 450 460 470 480 QKELEAKMLA QKAEEKENHC PTMLRPLSHR TVTGAKPLKK AVVMPLQLIQ EQAASPNAEI 490 500 510 520 530 540 HILKNKGRKR KLESLDALEP EEKAEDCWEL QISPELLAHG RQKILDLLNE GSARDLRSLQ 550 560 570 580 590 RIGPKKAQLI VGWRELHGPF SQVEDLERVE GITGKQMESF LKANILGLAA GQRCGAS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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.
[19]	"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. , 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.
[20]	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. , 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.

IPI

IPI00000769.
IPI01015810.

RefSeq

NP_001243198.1. NM_001256269.1.
NP_001243199.1. NM_001256270.1.
NP_015556.1. NM_007317.2.

UniGene

Hs.612151.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EDU	NMR	-	A	570-660	[»]
3BFN	X-ray	2.30	A	40-400	[»]

ProteinModelPortal

Q14807.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14807. 5 interactions.

MINT

MINT-156095.

STRING

9606.ENSP00000160827.

PTM databases

PhosphoSite

Q14807.

Polymorphism databases

DMDM

19863381.

Proteomic databases

PaxDb

Q14807.

PRIDE

Q14807.

Protocols and materials databases

DNASU

3835.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000160827; ENSP00000160827; ENSG00000079616.
ENST00000400751; ENSP00000383562; ENSG00000079616.

GeneID

3835.

KEGG

hsa:3835.

UCSC

uc002dts.3. human.

Organism-specific databases

CTD

3835.

GeneCards

GC16P029802.

HGNC

HGNC:6391. KIF22.

HPA

HPA041076.

MIM

603213. gene.
603546. phenotype.

neXtProt

NX_Q14807.

Orphanet

93360. Spondyloepimetaphyseal dysplasia with multiple dislocations.

PharmGKB

PA30180.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5059.

HOGENOM

HOG000007569.

HOVERGEN

HBG052252.

InParanoid

Q14807.

KO

K10403.

OMA

DCWELQI.

OrthoDB

EOG4548ZH.

PhylomeDB

Q14807.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q14807.

Bgee

Q14807.

CleanEx

HS_KIF22.

Genevestigator

Q14807.

GermOnline

ENSG00000079616. Homo sapiens.

Family and domain databases

Gene3D

3.40.850.10. 1 hit.

InterPro

IPR003583. Hlx-hairpin-Hlx_DNA-bd_motif.
IPR026986. KIF22.
IPR019821. Kinesin_motor_CS.
IPR001752. Kinesin_motor_dom.
[Graphical view]

PANTHER

PTHR24115:SF171. PTHR24115:SF171. 1 hit.

Pfam

PF00225. Kinesin. 1 hit.
[Graphical view]

PRINTS

PR00380. KINESINHEAVY.

SMART

SM00278. HhH1. 2 hits.
SM00129. KISc. 1 hit.
[Graphical view]

PROSITE

PS00411. KINESIN_MOTOR_DOMAIN1. 1 hit.
PS50067. KINESIN_MOTOR_DOMAIN2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL5470.

EvolutionaryTrace

Q14807.

GenomeRNAi

3835.

NextBio

15075.

SOURCE

Search...

Entry information

Entry name

KIF22_HUMAN

Accession

Primary (citable) accession number: Q14807
Secondary accession number(s): B2R5M0 , B7Z265, O60845, O94814, Q53F58, Q9BT46

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	September 26, 2001
Last modified:	May 1, 2013
This is version 138 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.