Reviewed, UniProtKB/Swiss-Prot Q8TD19 (NEK9_HUMAN)

Names and origin

Protein names

Recommended name:
    Serine/threonine-protein kinase Nek9
    EC=2.7.11.1
Alternative name(s):
    Never in mitosis A-related kinase 9
      Short name=NimA-related protein kinase 9
    Nercc1 kinase
    NimA-related kinase 8
      Short name=Nek8

Gene names

Name:	NEK9
Synonyms:	KIAA1995, NEK8, NERCC

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	979 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression. Ref.6
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium.
Enzyme regulation	Activated during mitosis by intramolecular autophosphorylation. Activity and autophosphorylation is activated by manganese >> magnesium ions. Sensitive to increasing concentration of detergents. It is not cell-cycle regulated but activity is higher in G0-arrested cells.
Subunit structure	Homodimer. Binds to Ran GTPase. Has a greater affinity for Ran-GDP over Ran-GTP. Interacts with NEK6, NEK7 and BICD2. Interacts with SSRP1 and SUPT16H, the 2 subunits of the FACT complex. Ref.6
Subcellular location	Cytoplasm. Nucleus Ref.6.
Tissue specificity	Most abundant in heart, liver, kidney and testis. Also expressed in smooth muscle cells and fibroblasts.
Developmental stage	Expression varied mildly across the cell cycle, with highest expression observed in G1 and stationary-phase cells.
Domain	Dimerizes through its coiled-coil domain.
Post-translational modification	Autophosphorylated on serine and threonine residues. When complexed with FACT, exhibits markedly elevated phosphorylation on Thr-210. During mitosis, not phosphorylated on Thr-210. Phosphorylated by CDC2 in vitro. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14
Sequence similarities	Belongs to the protein kinase superfamily. NEK Ser/Thr protein kinase family. NIMA subfamily. Contains 1 protein kinase domain. Contains 6 RCC1 repeats.
Sequence caution	The sequence AAD31936.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW protein amino acid phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay. Source: HPA nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GABARAPL2	P60520	1	EBI-1044009,EBI-720116
NEK6	Q9HC98	1	EBI-1044009,EBI-740364

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 979	979	Serine/threonine-protein kinase Nek9		PRO_0000086435
Regions
	Domain	52 – 308	257	Protein kinase
	Repeat	388 – 444	57	RCC1 1
	Repeat	445 – 498	54	RCC1 2
	Repeat	499 – 550	52	RCC1 3
	Repeat	551 – 615	65	RCC1 4
	Repeat	616 – 668	53	RCC1 5
	Repeat	669 – 726	58	RCC1 6
	Nucleotide binding	58 – 66	9	ATP By similarity
	Region	732 – 891	160	Interaction with NEK6
	Coiled coil	892 – 939	48	Potential
	Compositional bias	752 – 760	9	Poly-Gly
	Compositional bias	765 – 888	124	Pro/Ser/Thr-rich
Sites
	Active site	176	1	Proton acceptor By similarity
	Binding site	81	1	ATP
Amino acid modifications
	Modified residue	2	1	Phosphoserine Ref.9
	Modified residue	13	1	Phosphoserine Ref.9
	Modified residue	16	1	Phosphoserine Ref.9
	Modified residue	20	1	Phosphoserine Ref.9
	Modified residue	28	1	Phosphoserine
	Modified residue	29	1	Phosphoserine Ref.9
	Modified residue	52	1	Phosphotyrosine
	Modified residue	76	1	Phosphoserine Ref.9
	Modified residue	203	1	Phosphoserine
	Modified residue	205	1	Phosphotyrosine
	Modified residue	210	1	Phosphothreonine; by autocatalysis Probable
	Modified residue	254	1	Phosphothreonine Ref.9
	Modified residue	331	1	Phosphoserine Ref.9
	Modified residue	332	1	Phosphoserine Ref.8 Ref.9
	Modified residue	333	1	Phosphothreonine Ref.8 Ref.10 Ref.12 Ref.14
	Modified residue	335	1	Phosphothreonine
	Modified residue	357	1	Phosphoserine
	Modified residue	358	1	Phosphothreonine Ref.8
	Modified residue	413	1	Phosphoserine
	Modified residue	731	1	N6-acetyllysine Ref.15
	Modified residue	735	1	Phosphoserine
	Modified residue	741	1	Phosphoserine Ref.9
	Modified residue	749	1	Phosphoserine
	Modified residue	750	1	Phosphoserine Ref.9
	Modified residue	793	1	Phosphoserine Ref.9
	Modified residue	795	1	Phosphothreonine
	Modified residue	801	1	Phosphoserine
	Modified residue	827	1	Phosphoserine Ref.9
	Modified residue	829	1	Phosphoserine Ref.9
	Modified residue	832	1	Phosphoserine
	Modified residue	836	1	Phosphoserine Ref.9
	Modified residue	838	1	Phosphoserine
	Modified residue	868	1	Phosphoserine Ref.8 Ref.9
	Modified residue	869	1	Phosphoserine Ref.7
	Modified residue	886	1	Phosphothreonine Ref.9
	Modified residue	944	1	Phosphoserine Ref.9
	Modified residue	974	1	Phosphoserine
	Modified residue	978	1	Phosphoserine Ref.9
Natural variations
	Natural variant	429	1	R → H: dbSNP rs10146482. Ref.1 Ref.3 Ref.16		VAR_027900
	Natural variant	828	1	P → T: dbSNP rs36014869. Ref.16		VAR_040926
	Natural variant	870	1	P → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.16		VAR_040927
Experimental info
	Mutagenesis	81	1	K → M: Loss of activity and autophosphorylation. Ref.2
	Mutagenesis	210	1	T → A: Significant reduction of autophosphorylation. Ref.1
	Mutagenesis	214	1	T → A: No effect on autophosphorylation. Ref.1
	Sequence conflict	351	1	V → I in AAL87410. Ref.2
	Sequence conflict	967	1	W → G in AAL87410. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8TD19-1 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 8583FDDE599324A2	FASTA	979	107,168
	10 20 30 40 50 60 MSVLGEYERH CDSINSDFGS ESGGCGDSSP GPSASQGPRA GGGAAEQEEL HYIPIRVLGR 70 80 90 100 110 120 GAFGEATLYR RTEDDSLVVW KEVDLTRLSE KERRDALNEI VILALLQHDN IIAYYNHFMD 130 140 150 160 170 180 NTTLLIELEY CNGGNLYDKI LRQKDKLFEE EMVVWYLFQI VSAVSCIHKA GILHRDIKTL 190 200 210 220 230 240 NIFLTKANLI KLGDYGLAKK LNSEYSMAET LVGTPYYMSP ELCQGVKYNF KSDIWAVGCV 250 260 270 280 290 300 IFELLTLKRT FDATNPLNLC VKIVQGIRAM EVDSSQYSLE LIQMVHSCLD QDPEQRPTAD 310 320 330 340 350 360 ELLDRPLLRK RRREMEEKVT LLNAPTKRPR SSTVTEAPIA VVTSRTSEVY VWGGGKSTPQ 370 380 390 400 410 420 KLDVIKSGCS ARQVCAGNTH FAVVTVEKEL YTWVNMQGGT KLHGQLGHGD KASYRQPKHV 430 440 450 460 470 480 EKLQGKAIRQ VSCGDDFTVC VTDEGQLYAF GSDYYGCMGV DKVAGPEVLE PMQLNFFLSN 490 500 510 520 530 540 PVEQVSCGDN HVVVLTRNKE VYSWGCGEYG RLGLDSEEDY YTPQKVDVPK ALIIVAVQCG 550 560 570 580 590 600 CDGTFLLTQS GKVLACGLNE FNKLGLNQCM SGIINHEAYH EVPYTTSFTL AKQLSFYKIR 610 620 630 640 650 660 TIAPGKTHTA AIDERGRLLT FGCNKCGQLG VGNYKKRLGI NLLGGPLGGK QVIRVSCGDE 670 680 690 700 710 720 FTIAATDDNH IFAWGNGGNG RLAMTPTERP HGSDICTSWP RPIFGSLHHV PDLSCRGWHT 730 740 750 760 770 780 ILIVEKVLNS KTIRSNSSGL SIGTVFQSSS PGGGGGGGGG EEEDSQQESE TPDPSGGFRG 790 800 810 820 830 840 TMEADRGMEG LISPTEAMGN SNGASSSCPG WLRKELENAE FIPMPDSPSP LSAAFSESEK 850 860 870 880 890 900 DTLPYEELQG LKVASEAPLE HKPQVEASSP RLNPAVTCAG KGTPLTPPAC ACSSLQVEVE 910 920 930 940 950 960 RLQGLVLKCL AEQQKLQQEN LQIFTQLQKL NKKLEGGQQV GMHSKGTQTA KEEMEMDPKP 970 DLDSDSWCLL GTDSCRPSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification, cloning, and characterization of Nek8, a novel NIMA-related kinase, and its candidate substrate Bicd2." Holland P.M., Milne A., Garka K., Johnson R.S., Willis C., Sims J.E., Rauch C.T., Bird T.A., Virca G.D. J. Biol. Chem. 277:16229-16240(2002) [PubMed: 11864968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PROTEIN SEQUENCE OF 61-70; 318-327; 331-352 AND 511-530, MUTAGENESIS OF THR-210 AND THR-214, VARIANT HIS-429. Tissue: Dendritic cell and Fibroblast.
[2]	"Nercc1, a mammalian NIMA-family kinase, binds the Ran GTPase and regulates mitotic progression." Roig J., Mikhailov A., Belham C., Avruch J. Genes Dev. 16:1640-1658(2002) [PubMed: 12101123] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE, MUTAGENESIS OF LYS-81.
[3]	"Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method." Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S., Takahashi Y., Kitajima S., Saga Y., Koseki H. DNA Res. 9:47-57(2002) [PubMed: 12056414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-429. Tissue: Brain.
[4]	"The DNA sequence and analysis of human chromosome 14." Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J. Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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.
[6]	"Nek9, a novel FACT-associated protein, modulates interphase progression." Tan B.C.-M., Lee S.-C. J. Biol. Chem. 279:9321-9330(2004) [PubMed: 14660563] [Abstract] Cited for: FUNCTION, INTERACTION WITH SSRP1 AND SUPT16H, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-210.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-869, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry." Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R., Keri G., Wehland J., Daub H. Mol. Cell. Proteomics 6:537-547(2007) [PubMed: 17192257] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-332; THR-333; THR-358 AND SER-868, MASS SPECTROMETRY.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-13; SER-16; SER-20; SER-29; SER-76; THR-254; SER-331; SER-332; SER-741; SER-750; SER-793; SER-827; SER-829; SER-836; SER-868; THR-886; SER-944 AND SER-978, MASS SPECTROMETRY.
[10]	"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 THR-333, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, MASS SPECTROMETRY.
[13]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-13; SER-16; SER-20; SER-28; SER-29; TYR-52; SER-76; SER-203; TYR-205; THR-254; SER-331; SER-332; THR-333; THR-335; SER-357; THR-358; SER-413; SER-735; SER-749; SER-750; SER-793; THR-795; SER-801; SER-827; SER-829; SER-832; SER-836; SER-838; SER-868; SER-869; THR-886; SER-944; SER-974 AND SER-978, MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, MASS SPECTROMETRY. Tissue: T-cell.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-731, MASS SPECTROMETRY.
[16]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed: 17344846] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] HIS-429; THR-828 AND SER-870.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY048580 mRNA. Translation: AAL05428.1. AY080896 mRNA. Translation: AAL87410.1. AB082526 mRNA. Translation: BAC02704.1. Different initiation. AC007055 Genomic DNA. Translation: AAD31936.1. Sequence problems. AC007055 Genomic DNA. Translation: AAD31938.1. AC007055 Genomic DNA. Translation: AAD31939.1. AC007055 Genomic DNA. Translation: AAD31940.1. BC009336 mRNA. Translation: AAH09336.2. BC093881 mRNA. Translation: AAH93881.1. BC112101 mRNA. Translation: AAI12102.1.
IPI	IPI00301609.
RefSeq	NP_149107.4.
UniGene	Hs.719118
3D structure databases
SMR	Q8TD19. Positions 51-311, 342-726.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8TD19. 10 interactions.
STRING	Q8TD19.
PTM databases
PhosphoSite	Q8TD19.
Proteomic databases
PeptideAtlas	Q8TD19.
PRIDE	Q8TD19.
Genome annotation databases
Ensembl	ENST00000238616; ENSP00000238616; ENSG00000119638; Homo sapiens. [Genome view]
GeneID	91754.
KEGG	hsa:91754.
UCSC	uc001xrl.1. human.
Organism-specific databases
CTD	91754.
GeneCards	GC14M074618.
H-InvDB	HIX0011824.
HGNC	HGNC:18591. NEK9.
HPA	HPA001405.
MIM	609798. gene.
PharmGKB	PA38593.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13112.
HOVERGEN	Q8TD19.
InParanoid	Q8TD19.
OMA	PGKTHTA.
OrthoDB	EOG9HHRN4.
PhylomeDB	Q8TD19.
Enzyme and pathway databases
BRENDA	2.7.11.1. 247.
Gene expression databases
ArrayExpress	Q8TD19.
Bgee	Q8TD19.
CleanEx	HS_NEK8. HS_NEK9.
Genevestigator	Q8TD19.
GermOnline	ENSG00000119638. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR000408. Reg_chr_condens. IPR009091. Reg_csome_cond/b-lactamase_inh. IPR017442. Se/Thr_prot_kinase-like_dom. IPR008271. Ser/Thr_prot_kinase_AS. IPR002290. Ser/Thr_prot_kinase_dom. [Graphical view]
Gene3D	G3DSA:2.130.10.30. Reg_csome_cond/b-lactamase_inh. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. PF00415. RCC1. 4 hits. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS00107. PROTEIN_KINASE_ATP. False negative. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. PS00625. RCC1_1. False negative. PS00626. RCC1_2. False negative. PS50012. RCC1_3. 6 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	77443.
SOURCE	Search...

Entry information

Entry name

NEK9_HUMAN

Accession

Primary (citable) accession number: Q8TD19
Secondary accession number(s): Q52LK6 , Q8NCN0, Q8TCY4, Q9UPI4, Q9Y6S4, Q9Y6S5, Q9Y6S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 15, 2003
Last sequence update:	October 17, 2006
Last modified:	February 9, 2010
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.