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Q9NRH2 (SNRK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length765 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 765765SNF-related serine/threonine-protein kinase
PRO_0000225605

Regions

Domain16 – 269254Protein kinase
Domain291 – 33444UBA
Nucleotide binding22 – 309ATP By similarity UniProtKB P57059

Sites

Active site1391Proton acceptor By similarity UniProtKB P57059
Binding site451ATP By similarity UniProtKB P57059

Amino acid modifications

Modified residue1731Phosphothreonine; by LKB1 Ref.2
Modified residue3901Phosphoserine Ref.12

Natural variations

Alternative sequence2441D → E in isoform 2. Ref.6
VSP_051959
Alternative sequence245 – 765521Missing in isoform 2. Ref.6
VSP_051960
Natural variant2601L → S. Ref.13
Corresponds to variant rs35624204 [ dbSNP | Ensembl ].
VAR_041096
Natural variant3911P → S. Ref.13
Corresponds to variant rs56104180 [ dbSNP | Ensembl ].
VAR_041097
Natural variant6111G → S in an ovarian mucinous carcinoma sample; somatic mutation. Ref.13
VAR_041098
Natural variant7481P → L in an ovarian serous carcinoma sample; somatic mutation. Ref.13
VAR_041099
Natural variant7651I → M in a breast pleomorphic lobular carcinoma sample; somatic mutation. Ref.13
VAR_041100

Experimental info

Mutagenesis1731T → A or E: Prevents phosphorylation and activation by STK11/LKB1 complex. Ref.2
Sequence conflict971G → E in AAF86944. Ref.5
Sequence conflict1161A → P in AAF86944. Ref.5
Sequence conflict1241V → A in CAH18415. Ref.7
Sequence conflict1811S → P in CAH18415. Ref.7
Sequence conflict1961V → A in CAH18415. Ref.7
Sequence conflict2111G → E in BAA91023. Ref.6
Sequence conflict2191N → D in CAH18415. Ref.7
Sequence conflict2591S → Y in AAH71567. Ref.9
Sequence conflict4451V → A in CAH18415. Ref.7
Sequence conflict4821S → G in CAH18415. Ref.7
Sequence conflict4861L → V in AAH71567. Ref.9
Sequence conflict6361A → V in CAH18415. Ref.7
Sequence conflict7221K → R in AAH71567. Ref.9

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 06EF88CF7F8A393D

FASTA76584,276
        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 

« Hide

Isoform 2 [UniParc].

Checksum: C800B93190F76B4E
Show »

FASTA24427,481

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"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. expand/collapse author list , 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.
CCDSCCDS43075.1. [Q9NRH2-1]
RefSeqNP_001094064.1. NM_001100594.1. [Q9NRH2-1]
NP_060189.3. NM_017719.4. [Q9NRH2-1]
XP_005265302.1. XM_005265245.1. [Q9NRH2-1]
XP_005265303.1. XM_005265246.1. [Q9NRH2-1]
UniGeneHs.476052.

3D structure databases

ProteinModelPortalQ9NRH2.
SMRQ9NRH2. Positions 14-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120211. 4 interactions.
IntActQ9NRH2. 1 interaction.
MINTMINT-1338450.
STRING9606.ENSP00000296088.

Chemistry

BindingDBQ9NRH2.
ChEMBLCHEMBL1908384.
GuidetoPHARMACOLOGY2202.

PTM databases

PhosphoSiteQ9NRH2.

Polymorphism databases

DMDM90185235.

Proteomic databases

MaxQBQ9NRH2.
PaxDbQ9NRH2.
PRIDEQ9NRH2.

Protocols and materials databases

DNASU54861.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296088; ENSP00000296088; ENSG00000163788. [Q9NRH2-1]
ENST00000429705; ENSP00000411375; ENSG00000163788. [Q9NRH2-1]
ENST00000454177; ENSP00000401246; ENSG00000163788. [Q9NRH2-1]
GeneID54861.
KEGGhsa:54861.
UCSCuc003cms.4. human. [Q9NRH2-1]
uc003cmu.3. human. [Q9NRH2-2]

Organism-specific databases

CTD54861.
GeneCardsGC03P043303.
HGNCHGNC:30598. SNRK.
HPAHPA042163.
MIM612760. gene.
neXtProtNX_Q9NRH2.
PharmGKBPA142670894.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000059616.
HOVERGENHBG093970.
InParanoidQ9NRH2.
KOK08802.
OMATTSGRKC.
OrthoDBEOG7CZK55.
PhylomeDBQ9NRH2.
TreeFamTF351991.

Enzyme and pathway databases

SignaLinkQ9NRH2.

Gene expression databases

ArrayExpressQ9NRH2.
BgeeQ9NRH2.
CleanExHS_SNRK.
GenevestigatorQ9NRH2.

Family and domain databases

InterProIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50030. UBA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNRK. human.
GeneWikiSNRK.
GenomeRNAi54861.
NextBio57744.
PROQ9NRH2.
SOURCESearch...

Entry information

Entry nameSNRK_HUMAN
AccessionPrimary (citable) accession number: Q9NRH2
Secondary accession number(s): B2RAV6 expand/collapse secondary AC list , Q14706, Q68D15, Q6IQ46, Q9NXI7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM