Reviewed, UniProtKB/Swiss-Prot Q14807 (KIF22_HUMAN)

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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	665 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.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.

Ontologies

Keywords
Cellular component	Microtubule Nucleus
Domain	Coiled coil
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA repair Inferred from electronic annotation. Source: InterPro microtubule-based movement Inferred from electronic annotation. Source: InterPro mitosis Ref.1 Traceable author statement. Source: ProtInc
Cellular component	kinetochore Ref.1 Traceable author statement. Source: ProtInc microtubule Inferred from electronic annotation. Source: UniProtKB-KW nucleus Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Ref.1 Traceable author statement. Source: ProtInc microtubule motor activity Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CRK	P46108	1	EBI-715834,EBI-886

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.12

Modified residue

427

1

Phosphoserine Ref.12

Modified residue

452

1

Phosphoserine Ref.11

Modified residue

543

1

Phosphoserine Ref.10

Modified residue

562

1

Phosphoserine Ref.10

Modified residue

581

1

Phosphoserine Ref.10

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)
	Q14807-1 [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

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: 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. , 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. , 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

EMBLGenBankDDBJ

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.

IPI

IPI00000769.

RefSeq

NP_015556.1.

UniGene

Hs.613351

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

Q14807. 4 interactions.

PTM databases

PhosphoSite

Q14807.

Proteomic databases

PRIDE

Q14807.

Genome annotation databases

Ensembl

ENSG00000079616. Homo sapiens. [Contig view]

GeneID

3835.

KEGG

hsa:3835.

Organism-specific databases

GeneCards

GC16P029709.

H-InvDB

HIX0012922.
HIX0059648.

HGNC

HGNC:6391. KIF22.

MIM

603213. gene.

PharmGKB

PA30180.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q14807.

OMA

Q14807. LLNEGSA.

Gene expression databases

Bgee

Q14807.

CleanEx

HS_KIF22.

GermOnline

ENSG00000079616. Homo sapiens.

Family and domain databases

InterPro

IPR003583. Helix-hairpin-helix_DNA-bd.
IPR001752. Kinesin_motor.
IPR019821. Kinesin_motor_CS.
[Graphical view]

Gene3D

G3DSA:3.40.850.10. kinesin_motor. 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 Resources

NextBio

15075.

SOURCE

Search...

Entry information

Entry name

KIF22_HUMAN

Accession

Primary (citable) accession number: Q14807
Secondary accession number(s): B2R5M0 , 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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)