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Protein

Serine/threonine-protein kinase NIM1

Gene

NIM1K

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Activated by phosphorylation at Thr-229, probably by autophosphorylation.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031ATPPROSITE-ProRule annotationBy similarity
Active sitei196 – 1961Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi80 – 889ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • protein phosphorylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ8IY84.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase NIM1 (EC:2.7.11.1)
Alternative name(s):
NIM1 serine/threonine-protein kinase
Gene namesi
Name:NIM1K
Synonyms:NIM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:28646. NIM1K.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi229 – 2291T → A: Loss of autophosphorylation and kinase activity. 1 Publication
Mutagenesisi229 – 2291T → E: Constitutively active. 1 Publication

Polymorphism and mutation databases

BioMutaiNIM1.
DMDMi74759697.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 436436Serine/threonine-protein kinase NIM1PRO_0000247666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei229 – 2291Phosphothreonine; by autocatalysis1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8IY84.
PRIDEiQ8IY84.

PTM databases

PhosphoSiteiQ8IY84.

Expressioni

Gene expression databases

BgeeiQ8IY84.
GenevisibleiQ8IY84. HS.

Organism-specific databases

HPAiHPA007695.

Interactioni

Protein-protein interaction databases

BioGridi127945. 1 interaction.
STRINGi9606.ENSP00000313572.

Structurei

3D structure databases

ProteinModelPortaliQ8IY84.
SMRiQ8IY84. Positions 24-390.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 325252Protein kinasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00790000122947.
HOGENOMiHOG000233016.
HOVERGENiHBG082029.
InParanoidiQ8IY84.
KOiK16310.
OMAiESGCQTE.
PhylomeDBiQ8IY84.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8IY84-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAVYMNGGG LVNPHYARWD RRDSVESGCQ TESSKEGEEG QPRQLTPFEK
60 70 80 90 100
LTQDMSQDEK VVREITLGKR IGFYRIRGEI GSGNFSQVKL GIHSLTKEKV
110 120 130 140 150
AIKILDKTKL DQKTQRLLSR EISSMEKLHH PNIIRLYEVV ETLSKLHLVM
160 170 180 190 200
EYAGGGELFG KISTEGKLSE PESKLIFSQI VSAVKHMHEN QIIHRDLKAE
210 220 230 240 250
NVFYTSNTCV KVGDFGFSTV SKKGEMLNTF CGSPPYAAPE LFRDEHYIGI
260 270 280 290 300
YVDIWALGVL LYFMVTGTMP FRAETVAKLK KSILEGTYSV PPHVSEPCHR
310 320 330 340 350
LIRGVLQQIP TERYGIDCIM NDEWMQGVPY PTPLEPFQLD PKHLSETSTL
360 370 380 390 400
KEEENEVKST LEHLGITEEH IRNNQGRDAR SSITGVYRII LHRVQRKKAL
410 420 430
ESVPVMMLPD PKERDLKKGS RVYRGIRHTS KFCSIL
Length:436
Mass (Da):49,606
Last modified:March 1, 2003 - v1
Checksum:iC183F11F54E3B87C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211R → W.1 Publication
VAR_040945
Natural varianti64 – 641E → Q.1 Publication
VAR_040946
Natural varianti260 – 2601L → I.1 Publication
VAR_040947
Natural varianti320 – 3201M → I.1 Publication
VAR_040948
Natural varianti333 – 3331P → S in a lung neuroendocrine carcinoma sample; somatic mutation. 1 Publication
VAR_040949
Natural varianti411 – 4111P → T in a lung large cell carcinoma sample; somatic mutation. 1 Publication
VAR_040950

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122985 mRNA. Translation: BAG53833.1.
AC106800 Genomic DNA. No translation available.
AC114947 Genomic DNA. No translation available.
CH471119 Genomic DNA. Translation: EAW56053.1.
BC036422 mRNA. Translation: AAH36422.1.
CCDSiCCDS3943.1.
RefSeqiNP_699192.1. NM_153361.3.
XP_006714513.1. XM_006714450.1.
UniGeneiHs.25845.

Genome annotation databases

EnsembliENST00000326035; ENSP00000313572; ENSG00000177453.
ENST00000512796; ENSP00000420849; ENSG00000177453.
GeneIDi167359.
KEGGihsa:167359.
UCSCiuc003jno.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK122985 mRNA. Translation: BAG53833.1.
AC106800 Genomic DNA. No translation available.
AC114947 Genomic DNA. No translation available.
CH471119 Genomic DNA. Translation: EAW56053.1.
BC036422 mRNA. Translation: AAH36422.1.
CCDSiCCDS3943.1.
RefSeqiNP_699192.1. NM_153361.3.
XP_006714513.1. XM_006714450.1.
UniGeneiHs.25845.

3D structure databases

ProteinModelPortaliQ8IY84.
SMRiQ8IY84. Positions 24-390.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127945. 1 interaction.
STRINGi9606.ENSP00000313572.

Chemistry

BindingDBiQ8IY84.
ChEMBLiCHEMBL3542.
GuidetoPHARMACOLOGYi2291.

PTM databases

PhosphoSiteiQ8IY84.

Polymorphism and mutation databases

BioMutaiNIM1.
DMDMi74759697.

Proteomic databases

PaxDbiQ8IY84.
PRIDEiQ8IY84.

Protocols and materials databases

DNASUi167359.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000326035; ENSP00000313572; ENSG00000177453.
ENST00000512796; ENSP00000420849; ENSG00000177453.
GeneIDi167359.
KEGGihsa:167359.
UCSCiuc003jno.4. human.

Organism-specific databases

CTDi167359.
GeneCardsiGC05P043194.
HGNCiHGNC:28646. NIM1K.
HPAiHPA007695.
neXtProtiNX_Q8IY84.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00790000122947.
HOGENOMiHOG000233016.
HOVERGENiHBG082029.
InParanoidiQ8IY84.
KOiK16310.
OMAiESGCQTE.
PhylomeDBiQ8IY84.

Enzyme and pathway databases

SignaLinkiQ8IY84.

Miscellaneous databases

GenomeRNAii167359.
NextBioi88667.
PROiQ8IY84.

Gene expression databases

BgeeiQ8IY84.
GenevisibleiQ8IY84. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: BrainImported.
  6. "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.

Entry informationi

Entry nameiNIM1_HUMAN
AccessioniPrimary (citable) accession number: Q8IY84
Secondary accession number(s): B3KVM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: March 1, 2003
Last modified: June 24, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.