Q9NRH2 (SNRK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
SNF-related serine/threonine-protein kinase
EC=2.7.11.1

Alternative name(s):
SNF1-related kinase

Gene names

Name:	SNRK
Synonyms:	KIAA0096, SNFRK

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

General annotation (Comments)

Function	May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis. Ref.1 Ref.2 UniProtKB Q63553 Ref.9
Catalytic activity	ATP + a protein = ADP + a phosphoprotein. Ref.2 Ref.9
Cofactor	Magnesium. Ref.2 Ref.9
Enzyme regulation	Activated by phosphorylation on Thr-173. Ref.2
Subcellular location	Nucleus By similarity UniProtKB Q63553.
Tissue specificity	Expressed in hematopoietic progenitor cells and leukemic cell lines. Weakly expressed in the testis. Ref.1 Ref.9 Ref.10
Post-translational modification	Autophosphorylated. Phosphorylation on Thr-173 by STK11/LKB1 in complex with STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Ref.1 Ref.2 Ref.9
Sequence similarities	Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family. Contains 1 protein kinase domain. Contains 1 UBA domain.
Sequence caution	The sequence BAA07744.2 differs from that shown. Reason: Erroneous initiation. The sequence CAH18415.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing 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)
Biological_process	myeloid cell differentiation Traceable author statement Ref.1. Source: UniProtKB
Cellular_component	nucleus Inferred from sequence or structural similarity. Source: UniProtKB
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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 Ref.3 Ref.5 Ref.9 (identifier: Q9NRH2-1)

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 Ref.6 (identifier: Q9NRH2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     244-244: D → E
     245-765: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 765	765	SNF-related serine/threonine-protein kinase		PRO_0000225605
Regions
	Domain	16 – 269	254	Protein kinase
	Domain	291 – 334	44	UBA
	Nucleotide binding	22 – 30	9	ATP By similarity UniProtKB P57059
Sites
	Active site	139	1	Proton acceptor By similarity UniProtKB P57059
	Binding site	45	1	ATP By similarity UniProtKB P57059
Amino acid modifications
	Modified residue	173	1	Phosphothreonine; by LKB1 Ref.2
	Modified residue	390	1	Phosphoserine Ref.11
	Modified residue	569	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	244	1	D → E in isoform 2. Ref.6		VSP_051959
	Alternative sequence	245 – 765	521	Missing in isoform 2. Ref.6		VSP_051960
	Natural variant	260	1	L → S. Ref.12 Corresponds to variant rs35624204 [ dbSNP | Ensembl ].		VAR_041096
	Natural variant	391	1	P → S. Ref.12 Corresponds to variant rs56104180 [ dbSNP | Ensembl ].		VAR_041097
	Natural variant	611	1	G → S in an ovarian mucinous carcinoma sample; somatic mutation. Ref.12		VAR_041098
	Natural variant	748	1	P → L in an ovarian serous carcinoma sample; somatic mutation. Ref.12		VAR_041099
	Natural variant	765	1	I → M in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.12		VAR_041100
Experimental info
	Mutagenesis	173	1	T → A or E: Prevents phosphorylation and activation by STK11/LKB1 complex. Ref.2
	Sequence conflict	97	1	G → E in AAF86944. Ref.5
	Sequence conflict	116	1	A → P in AAF86944. Ref.5
	Sequence conflict	124	1	V → A in CAH18415. Ref.7
	Sequence conflict	181	1	S → P in CAH18415. Ref.7
	Sequence conflict	196	1	V → A in CAH18415. Ref.7
	Sequence conflict	211	1	G → E in BAA91023. Ref.6
	Sequence conflict	219	1	N → D in CAH18415. Ref.7
	Sequence conflict	259	1	S → Y in AAH71567. Ref.9
	Sequence conflict	445	1	V → A in CAH18415. Ref.7
	Sequence conflict	482	1	S → G in CAH18415. Ref.7
	Sequence conflict	486	1	L → V in AAH71567. Ref.9
	Sequence conflict	636	1	A → V in CAH18415. Ref.7
	Sequence conflict	722	1	K → R in AAH71567. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 06EF88CF7F8A393D	FASTA	765	84,276
	10 20 30 40 50 60 MAGFKRGYDG KIAGLYDLDK TLGRGHFAVV KLARHVFTGE KVAVKVIDKT KLDTLATGHL 70 80 90 100 110 120 FQEVRCMKLV QHPNIVRLYE VIDTQTKLYL ILELGDGGDM FDYIMKHEEG LNEDLAKKYF 130 140 150 160 170 180 AQIVHAISYC HKLHVVHRDL KPENVVFFEK QGLVKLTDFG FSNKFQPGKK LTTSCGSLAY 190 200 210 220 230 240 SAPEILLGDE YDAPAVDIWS LGVILFMLVC GQPPFQEAND SETLTMIMDC KYTVPSHVSK 250 260 270 280 290 300 ECKDLITRML QRDPKRRASL EEIENHPWLQ GVDPSPATKY NIPLVSYKNL SEEEHNSIIQ 310 320 330 340 350 360 RMVLGDIADR DAIVEALETN RYNHITATYF LLAERILREK QEKEIQTRSA SPSNIKAQFR 370 380 390 400 410 420 QSWPTKIDVP QDLEDDLTAT PLSHATVPQS PARAADSVLN GHRSKGLCDS AKKDDLPELA 430 440 450 460 470 480 GPALSTVPPA SLKPTASGRK CLFRVEEDEE EDEEDKKPMS LSTQVVLRRK PSVTNRLTSR 490 500 510 520 530 540 KSAPVLNQIF EEGESDDEFD MDENLPPKLS RLKMNIASPG TVHKRYHRRK SQGRGSSCSS 550 560 570 580 590 600 SETSDDDSES RRRLDKDSGF TYSWHRRDSS EGPPGSEGDG GGQSKPSNAS GGVDKASPSE 610 620 630 640 650 660 NNAGGGSPSS GSGGNPTNTS GTTRRCAGPS NSMQLASRSA GELVESLKLM SLCLGSQLHG 670 680 690 700 710 720 STKYIIDPQN GLSFSSVKVQ EKSTWKMCIS STGNAGQVPA VGGIKFFSDH MADTTTELER 730 740 750 760 IKSKNLKNNV LQLPLCEKTI SVNIQRNPKE GLLCASSPAS CCHVI
	Isoform 2 [UniParc]. Checksum: C800B93190F76B4E	FASTA	244	27,481
	10 20 30 40 50 60 MAGFKRGYDG KIAGLYDLDK TLGRGHFAVV KLARHVFTGE KVAVKVIDKT KLDTLATGHL 70 80 90 100 110 120 FQEVRCMKLV QHPNIVRLYE VIDTQTKLYL ILELGDGGDM FDYIMKHEEG LNEDLAKKYF 130 140 150 160 170 180 AQIVHAISYC HKLHVVHRDL KPENVVFFEK QGLVKLTDFG FSNKFQPGKK LTTSCGSLAY 190 200 210 220 230 240 SAPEILLGDE YDAPAVDIWS LGVILFMLVC GQPPFQEAND SETLTMIMDC KYTVPSHVSK ECKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of human and mouse SNRK sucrose non-fermenting protein (SNF-1)-related kinases." Kertesz N., Samson J., Debacker C., Wu H., Labastie M.-C. Gene 294:13-24(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION.
[2]	"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-173, MUTAGENESIS OF THR-173.
[3]	"Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N. DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Bone marrow.
[4]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[5]	Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Adrenal gland.
[6]	"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: Brain and Colon mucosa.
[7]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Liver.
[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.
[10]	"Molecular cloning and characterization of a novel mammalian protein kinase harboring a homology domain that defines a subfamily of serine/threonine kinases." Becker W., Heukelbach J., Kentrup H., Joost H.G. Eur. J. Biochem. 235:736-743(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[11]	"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-390, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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] SER-260; SER-391; SER-611; LEU-748 AND MET-765.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D43636 mRNA. Translation: BAA07744.2. Different initiation. AF226044 mRNA. Translation: AAF86944.1. AK000231 mRNA. Translation: BAA91023.1. AK314376 mRNA. Translation: BAG37003.1. CR749621 mRNA. Translation: CAH18415.1. Different initiation. CH471055 Genomic DNA. Translation: EAW64693.1. BC071567 mRNA. Translation: AAH71567.1.
IPI	IPI00470811. IPI00718873.
RefSeq	NP_001094064.1. NM_001100594.1. NP_060189.3. NM_017719.4.
UniGene	Hs.476052.
3D structure databases
ProteinModelPortal	Q9NRH2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NRH2. 1 interaction.
MINT	MINT-1338450.
STRING	9606.ENSP00000296088.
PTM databases
PhosphoSite	Q9NRH2.
Polymorphism databases
DMDM	90185235.
Proteomic databases
PaxDb	Q9NRH2.
PRIDE	Q9NRH2.
Protocols and materials databases
DNASU	54861.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296088; ENSP00000296088; ENSG00000163788. ENST00000429705; ENSP00000411375; ENSG00000163788. ENST00000454177; ENSP00000401246; ENSG00000163788.
GeneID	54861.
KEGG	hsa:54861.
UCSC	uc003cms.4. human. uc003cmu.3. human.
Organism-specific databases
CTD	54861.
GeneCards	GC03P043303.
HGNC	HGNC:30598. SNRK.
HPA	HPA042163.
MIM	612760. gene.
neXtProt	NX_Q9NRH2.
PharmGKB	PA142670894.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000059616.
HOVERGEN	HBG093970.
InParanoid	Q9NRH2.
KO	K08802.
OMA	TTSGRKC.
OrthoDB	EOG4GB75K.
Gene expression databases
ArrayExpress	Q9NRH2.
Bgee	Q9NRH2.
CleanEx	HS_SNRK.
Genevestigator	Q9NRH2.
GermOnline	ENSG00000163788. 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. IPR015940. UBA/transl_elong_EF1B_N_euk. [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. PS50030. UBA. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9NRH2.
ChEMBL	CHEMBL1908384.
ChiTaRS	SNRK. human.
GenomeRNAi	54861.
NextBio	57744.
SOURCE	Search...

Entry information

Entry name

SNRK_HUMAN

Accession

Primary (citable) accession number: Q9NRH2
Secondary accession number(s): B2RAV6 , Q14706, Q68D15, Q6IQ46, Q9NXI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 101 of the entry and version 2 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.