Q8IY84 (NIM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase NIM1
EC=2.7.11.1

Gene names

Name:

NIM1

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	436 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.1
Cofactor	Magnesium. Ref.1
Enzyme regulation	Activated by phosphorylation at Thr-229, probably by autophosphorylation. Ref.1
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. Contains 1 protein kinase domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from direct assay Ref.1. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.1. Source: UniProtKB protein serine/threonine kinase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 436	436	Serine/threonine-protein kinase NIM1		PRO_0000247666
Regions
	Domain	74 – 325	252	Protein kinase
	Nucleotide binding	80 – 88	9	ATP By similarity UniProtKB P28523
Sites
	Active site	196	1	Proton acceptor By similarity UniProtKB P28523
	Binding site	103	1	ATP By similarity UniProtKB P28523
Amino acid modifications
	Modified residue	229	1	Phosphothreonine; by autocatalysis Ref.1
Natural variations
	Natural variant	21	1	R → W. Ref.5		VAR_040945
	Natural variant	64	1	E → Q. Ref.5		VAR_040946
	Natural variant	260	1	L → I. Ref.5		VAR_040947
	Natural variant	320	1	M → I. Ref.5		VAR_040948
	Natural variant	333	1	P → S in a lung neuroendocrine carcinoma sample; somatic mutation. Ref.5		VAR_040949
	Natural variant	411	1	P → T in a lung large cell carcinoma sample; somatic mutation. Ref.5		VAR_040950
Experimental info
	Mutagenesis	229	1	T → A: Loss of autophosphorylation and kinase activity. Ref.1
	Mutagenesis	229	1	T → E: Constitutively active. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8IY84 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: C183F11F54E3B87C	FASTA	436	49,606
	10 20 30 40 50 60 MTAVYMNGGG LVNPHYARWD RRDSVESGCQ TESSKEGEEG QPRQLTPFEK LTQDMSQDEK 70 80 90 100 110 120 VVREITLGKR IGFYRIRGEI GSGNFSQVKL GIHSLTKEKV AIKILDKTKL DQKTQRLLSR 130 140 150 160 170 180 EISSMEKLHH PNIIRLYEVV ETLSKLHLVM EYAGGGELFG KISTEGKLSE PESKLIFSQI 190 200 210 220 230 240 VSAVKHMHEN QIIHRDLKAE NVFYTSNTCV KVGDFGFSTV SKKGEMLNTF CGSPPYAAPE 250 260 270 280 290 300 LFRDEHYIGI YVDIWALGVL LYFMVTGTMP FRAETVAKLK KSILEGTYSV PPHVSEPCHR 310 320 330 340 350 360 LIRGVLQQIP TERYGIDCIM NDEWMQGVPY PTPLEPFQLD PKHLSETSTL KEEENEVKST 370 380 390 400 410 420 LEHLGITEEH IRNNQGRDAR SSITGVYRII LHRVQRKKAL ESVPVMMLPD PKERDLKKGS 430 RVYRGIRHTS KFCSIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of the sucrose non-fermenting related kinase SNRK, as a novel LKB1 substrate." Jaleel M., McBride A., Lizcano J.M., Deak M., Toth R., Morrice N.A., Alessi D.R. FEBS Lett. 579:1417-1423(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ENZYME REGULATION, PHOSPHORYLATION AT THR-229, MUTAGENESIS OF THR-229.
[2]	"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]. Tissue: Amygdala.
[3]	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].
[4]	"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]. Tissue: Brain.
[5]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-21; GLN-64; ILE-260; ILE-320; SER-333 AND THR-411.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK122985 mRNA. Translation: BAG53833.1. CH471119 Genomic DNA. Translation: EAW56053.1. BC036422 mRNA. Translation: AAH36422.1.
IPI	IPI00217690.
RefSeq	NP_699192.1. NM_153361.3.
UniGene	Hs.25845.
3D structure databases
ProteinModelPortal	Q8IY84.
ModBase	Search...
PTM databases
PhosphoSite	Q8IY84.
Polymorphism databases
DMDM	74759697.
Proteomic databases
PaxDb	Q8IY84.
PRIDE	Q8IY84.
Protocols and materials databases
DNASU	167359.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	167359.
KEGG	hsa:167359.
UCSC	uc003jno.3. human.
Organism-specific databases
CTD	167359.
GeneCards	GC05P043193.
HPA	HPA007695.
neXtProt	NX_Q8IY84.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233016.
HOVERGEN	HBG082029.
InParanoid	Q8IY84.
KO	K16310.
OMA	SEPCHRL.
OrthoDB	EOG4TF0K5.
PhylomeDB	Q8IY84.
Gene expression databases
Bgee	Q8IY84.
Genevestigator	Q8IY84.
GermOnline	ENSG00000177453. Homo sapiens.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q8IY84.
ChEMBL	CHEMBL3542.
GenomeRNAi	167359.
NextBio	88667.

Entry information

Entry name

NIM1_HUMAN

Accession

Primary (citable) accession number: Q8IY84
Secondary accession number(s): B3KVM1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 88 of the entry and version 1 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.