CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022071
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 SNF-related serine/threonine-protein kinase 
Protein Synonyms/Alias
 SNF1-related kinase 
Gene Name
 SNRK 
Gene Synonyms/Alias
 KIAA0096; SNFRK 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11FKRGYDGKIAGLYDLacetylation[1]
45TGEKVAVKVIDKTKLubiquitination[2]
150ENVVFFEKQGLVKLTubiquitination[2]
738LQLPLCEKTISVNIQubiquitination[2]
749VNIQRNPKEGLLCASubiquitination[2]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis. 
Sequence Annotation
 DOMAIN 16 269 Protein kinase.
 DOMAIN 291 334 UBA.
 NP_BIND 22 30 ATP (By similarity).
 ACT_SITE 139 139 Proton acceptor (By similarity).
 BINDING 45 45 ATP (By similarity).
 MOD_RES 173 173 Phosphothreonine; by LKB1.
 MOD_RES 390 390 Phosphoserine.
 MOD_RES 569 569 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 765 AA 
Protein Sequence
MAGFKRGYDG KIAGLYDLDK TLGRGHFAVV KLARHVFTGE KVAVKVIDKT KLDTLATGHL 60
FQEVRCMKLV QHPNIVRLYE VIDTQTKLYL ILELGDGGDM FDYIMKHEEG LNEDLAKKYF 120
AQIVHAISYC HKLHVVHRDL KPENVVFFEK QGLVKLTDFG FSNKFQPGKK LTTSCGSLAY 180
SAPEILLGDE YDAPAVDIWS LGVILFMLVC GQPPFQEAND SETLTMIMDC KYTVPSHVSK 240
ECKDLITRML QRDPKRRASL EEIENHPWLQ GVDPSPATKY NIPLVSYKNL SEEEHNSIIQ 300
RMVLGDIADR DAIVEALETN RYNHITATYF LLAERILREK QEKEIQTRSA SPSNIKAQFR 360
QSWPTKIDVP QDLEDDLTAT PLSHATVPQS PARAADSVLN GHRSKGLCDS AKKDDLPELA 420
GPALSTVPPA SLKPTASGRK CLFRVEEDEE EDEEDKKPMS LSTQVVLRRK PSVTNRLTSR 480
KSAPVLNQIF EEGESDDEFD MDENLPPKLS RLKMNIASPG TVHKRYHRRK SQGRGSSCSS 540
SETSDDDSES RRRLDKDSGF TYSWHRRDSS EGPPGSEGDG GGQSKPSNAS GGVDKASPSE 600
NNAGGGSPSS GSGGNPTNTS GTTRRCAGPS NSMQLASRSA GELVESLKLM SLCLGSQLHG 660
STKYIIDPQN GLSFSSVKVQ EKSTWKMCIS STGNAGQVPA VGGIKFFSDH MADTTTELER 720
IKSKNLKNNV LQLPLCEKTI SVNIQRNPKE GLLCASSPAS CCHVI 765 
Gene Ontology
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
 GO:0030099; P:myeloid cell differentiation; TAS:UniProtKB. 
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. 
Pfam
 PF00069; Pkinase 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS50030; UBA 
PRINTS