CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019570
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transient receptor potential cation channel subfamily M member 7 
Protein Synonyms/Alias
 Channel-kinase 1; Long transient receptor potential channel 7; LTrpC-7; LTrpC7 
Gene Name
 TRPM7 
Gene Synonyms/Alias
 CHAK1; LTRPC7 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
667RSMAYEAKQSDLVDDubiquitination[1]
827ILDSNEGKNEMEIQMubiquitination[2]
837MEIQMKSKKLPITRKubiquitination[2]
1168FLTEEDQKKLHDFEEacetylation[3]
1253LKTLTAQKASEASKVubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [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]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Essential ion channel and serine/threonine-protein kinase. Divalent cation channel permeable to calcium and magnesium. Has a central role in magnesium ion homeostasis and in the regulation of anoxic neuronal cell death. The kinase activity is essential for the channel function. May be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell. Phosphorylates annexin A1 (ANXA1). 
Sequence Annotation
 DOMAIN 1594 1824 Alpha-type protein kinase.
 NP_BIND 1794 1800 ATP (By similarity).
 ACT_SITE 1767 1767 Proton acceptor (By similarity).
 METAL 1753 1753 Zinc (By similarity).
 METAL 1810 1810 Zinc (By similarity).
 METAL 1812 1812 Zinc (By similarity).
 METAL 1816 1816 Zinc (By similarity).
 BINDING 1624 1624 ATP (By similarity).
 BINDING 1648 1648 ATP (By similarity).
 BINDING 1720 1720 ATP (By similarity).
 BINDING 1769 1769 ATP (By similarity).
 BINDING 1777 1777 ATP (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 1224 1224 Phosphoserine (By similarity).
 MOD_RES 1301 1301 Phosphoserine (By similarity).
 MOD_RES 1386 1386 Phosphoserine (By similarity).
 MOD_RES 1387 1387 Phosphoserine (By similarity).
 MOD_RES 1405 1405 Phosphothreonine (By similarity).
 MOD_RES 1467 1467 Phosphothreonine (By similarity).
 MOD_RES 1477 1477 Phosphoserine.
 MOD_RES 1493 1493 Phosphoserine (By similarity).
 MOD_RES 1500 1500 Phosphoserine (By similarity).
 MOD_RES 1569 1569 Phosphoserine (By similarity).
 MOD_RES 1851 1851 Phosphoserine (By similarity).  
Keyword
 Acetylation; Amyotrophic lateral sclerosis; ATP-binding; Calcium; Calcium channel; Calcium transport; Coiled coil; Complete proteome; Ion channel; Ion transport; Kinase; Membrane; Metal-binding; Neurodegeneration; Nucleotide-binding; Parkinsonism; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase; Transmembrane; Transmembrane helix; Transport; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1865 AA 
Protein Sequence
MSQKSWIEST LTKRECVYII PSSKDPHRCL PGCQICQQLV RCFCGRLVKQ HACFTASLAM 60
KYSDVKLGDH FNQAIEEWSV EKHTEQSPTD AYGVINFQGG SHSYRAKYVR LSYDTKPEVI 120
LQLLLKEWQM ELPKLVISVH GGMQKFELHP RIKQLLGKGL IKAAVTTGAW ILTGGVNTGV 180
AKHVGDALKE HASRSSRKIC TIGIAPWGVI ENRNDLVGRD VVAPYQTLLN PLSKLNVLNN 240
LHSHFILVDD GTVGKYGAEV RLRRELEKTI NQQRIHARIG QGVPVVALIF EGGPNVILTV 300
LEYLQESPPV PVVVCEGTGR AADLLAYIHK QTEEGGNLPD AAEPDIISTI KKTFNFGQNE 360
ALHLFQTLME CMKRKELITV FHIGSDEHQD IDVAILTALL KGTNASAFDQ LILTLAWDRV 420
DIAKNHVFVY GQQWLVGSLE QAMLDALVMD RVAFVKLLIE NGVSMHKFLT IPRLEELYNT 480
KQGPTNPMLF HLVRDVKQGN LPPGYKITLI DIGLVIEYLM GGTYRCTYTR KRFRLIYNSL 540
GGNNRRSGRN TSSSTPQLRK SHESFGNRAD KKEKMRHNHF IKTAQPYRPK IDTVMEEGKK 600
KRTKDEIVDI DDPETKRFPY PLNELLIWAC LMKRQVMARF LWQHGEESMA KALVACKIYR 660
SMAYEAKQSD LVDDTSEELK QYSNDFGQLA VELLEQSFRQ DETMAMKLLT YELKNWSNST 720
CLKLAVSSRL RPFVAHTCTQ MLLSDMWMGR LNMRKNSWYK VILSILVPPA ILLLEYKTKA 780
EMSHIPQSQD AHQMTMDDSE NNFQNITEEI PMEVFKEVRI LDSNEGKNEM EIQMKSKKLP 840
ITRKFYAFYH APIVKFWFNT LAYLGFLMLY TFVVLVQMEQ LPSVQEWIVI AYIFTYAIEK 900
VREIFMSEAG KVNQKIKVWF SDYFNISDTI AIISFFIGFG LRFGAKWNFA NAYDNHVFVA 960
GRLIYCLNII FWYVRLLDFL AVNQQAGPYV MMIGKMVANM FYIVVIMALV LLSFGVPRKA 1020
ILYPHEAPSW TLAKDIVFHP YWMIFGEVYA YEIDVCANDS VIPQICGPGT WLTPFLQAVY 1080
LFVQYIIMVN LLIAFFNNVY LQVKAISNIV WKYQRYHFIM AYHEKPVLPP PLIILSHIVS 1140
LFCCICKRRK KDKTSDGPKL FLTEEDQKKL HDFEEQCVEM YFNEKDDKFH SGSEERIRVT 1200
FERVEQMCIQ IKEVGDRVNY IKRSLQSLDS QIGHLQDLSA LTVDTLKTLT AQKASEASKV 1260
HNEITRELSI SKHLAQNLID DGPVRPSVWK KHGVVNTLSS SLPQGDLESN NPFHCNILMK 1320
DDKDPQCNIF GQDLPAVPQR KEFNFPEAGS SSGALFPSAV SPPELRQRLH GVELLKIFNK 1380
NQKLGSSSTS IPHLSSPPTK FFVSTPSQPS CKSHLETGTK DQETVCSKAT EGDNTEFGAF 1440
VGHRDSMDLQ RFKETSNKIK ILSNNNTSEN TLKRVSSLAG FTDCHRTSIP VHSKQAEKIS 1500
RRPSTEDTHE VDSKAALIPD WLQDRPSNRE MPSEEGTLNG LTSPFKPAMD TNYYYSAVER 1560
NNLMRLSQSI PFTPVPPRGE PVTVYRLEES SPNILNNSMS SWSQLGLCAK IEFLSKEEMG 1620
GGLRRAVKVQ CTWSEHDILK SGHLYIIKSF LPEVVNTWSS IYKEDTVLHL CLREIQQQRA 1680
AQKLTFAFNQ MKPKSIPYSP RFLEVFLLYC HSAGQWFAVE ECMTGEFRKY NNNNGDEIIP 1740
TNTLEEIMLA FSHWTYEYTR GELLVLDLQG VGENLTDPSV IKAEEKRSCD MVFGPANLGE 1800
DAIKNFRAKH HCNSCCRKLK LPDLKRNDYT PDKIIFPQDE PSDLNLQPGN STKESESTNS 1860
VRLML 1865 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0001726; C:ruffle; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005262; F:calcium channel activity; IEA:UniProtKB-KW.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
 GO:0031032; P:actomyosin structure organization; IEA:Compara.
 GO:0016340; P:calcium-dependent cell-matrix adhesion; IEA:Compara.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0046777; P:protein autophosphorylation; IEA:Compara. 
Interpro
 IPR005821; Ion_trans_dom.
 IPR011009; Kinase-like_dom.
 IPR004166; MHCK_EF2_kinase. 
Pfam
 PF02816; Alpha_kinase
 PF00520; Ion_trans 
SMART
 SM00811; Alpha_kinase 
PROSITE
 PS51158; ALPHA_KINASE 
PRINTS