CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010726
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Calcium-transporting ATPase type 2C member 1 
Protein Synonyms/Alias
 ATPase 2C1; ATP-dependent Ca(2+) pump PMR1 
Gene Name
 ATP2C1 
Gene Synonyms/Alias
 KIAA1347; PMR1L; HUSSY-28 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MKVARFQKIPNGENEubiquitination[1, 2]
25IPVLTSKKASELPVSubiquitination[2]
146CHCVREGKLEHTLARubiquitination[2]
424RNNTLMGKPTEGALIubiquitination[2]
496YCTTYQSKGQTLTLTubiquitination[1, 3, 4, 5]
514RDVYQQEKARMGSAGubiquitination[1, 2]
589SRLGLYSKTSQSVSGubiquitination[1]
831LSSRSQTKSVFEIGLubiquitination[1]
907RSREKIQKHVSSTSSubiquitination[3]
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] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of the calcium. 
Sequence Annotation
 ACT_SITE 350 350 4-aspartylphosphate intermediate (By
 METAL 303 303 Calcium 2; via carbonyl oxygen (By
 METAL 304 304 Calcium 2; via carbonyl oxygen (By
 METAL 306 306 Calcium 2; via carbonyl oxygen (By
 METAL 308 308 Calcium 2 (By similarity).
 METAL 644 644 Magnesium (By similarity).
 METAL 648 648 Magnesium (By similarity).
 METAL 738 738 Calcium 2 (By similarity).
 METAL 742 742 Calcium 2 (By similarity).  
Keyword
 Alternative splicing; ATP-binding; Calcium; Calcium transport; Complete proteome; Disease mutation; Golgi apparatus; Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Polymorphism; Reference proteome; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 919 AA 
Protein Sequence
MKVARFQKIP NGENETMIPV LTSKKASELP VSEVASILQA DLQNGLNKCE VSHRRAFHGW 60
NEFDISEDEP LWKKYISQFK NPLIMLLLAS AVISVLMHQF DDAVSITVAI LIVVTVAFVQ 120
EYRSEKSLEE LSKLVPPECH CVREGKLEHT LARDLVPGDT VCLSVGDRVP ADLRLFEAVD 180
LSIDESSLTG ETTPCSKVTA PQPAATNGDL ASRSNIAFMG TLVRCGKAKG VVIGTGENSE 240
FGEVFKMMQA EEAPKTPLQK SMDLLGKQLS FYSFGIIGII MLVGWLLGKD ILEMFTISVS 300
LAVAAIPEGL PIVVTVTLAL GVMRMVKKRA IVKKLPIVET LGCCNVICSD KTGTLTKNEM 360
TVTHIFTSDG LHAEVTGVGY NQFGEVIVDG DVVHGFYNPA VSRIVEAGCV CNDAVIRNNT 420
LMGKPTEGAL IALAMKMGLD GLQQDYIRKA EYPFSSEQKW MAVKCVHRTQ QDRPEICFMK 480
GAYEQVIKYC TTYQSKGQTL TLTQQQRDVY QQEKARMGSA GLRVLALASG PELGQLTFLG 540
LVGIIDPPRT GVKEAVTTLI ASGVSIKMIT GDSQETAVAI ASRLGLYSKT SQSVSGEEID 600
AMDVQQLSQI VPKVAVFYRA SPRHKMKIIK SLQKNGSVVA MTGDGVNDAV ALKAADIGVA 660
MGQTGTDVCK EAADMILVDD DFQTIMSAIE EGKGIYNNIK NFVRFQLSTS IAALTLISLA 720
TLMNFPNPLN AMQILWINII MDGPPAQSLG VEPVDKDVIR KPPRNWKDSI LTKNLILKIL 780
VSSIIIVCGT LFVFWRELRD NVITPRDTTM TFTCFVFFDM FNALSSRSQT KSVFEIGLCS 840
NRMFCYAVLG SIMGQLLVIY FPPLQKVFQT ESLSILDLLF LLGLTSSVCI VAEIIKKVER 900
SREKIQKHVS STSSSFLEV 919 
Gene Ontology
 GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
 GO:0000139; C:Golgi membrane; IDA:UniProtKB.
 GO:0016021; C:integral to membrane; NAS:UniProtKB.
 GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IDA:UniProtKB.
 GO:0005388; F:calcium-transporting ATPase activity; IDA:UniProtKB.
 GO:0030145; F:manganese ion binding; IDA:UniProtKB.
 GO:0015410; F:manganese-transporting ATPase activity; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
 GO:0016339; P:calcium-dependent cell-cell adhesion; IMP:UniProtKB.
 GO:0006874; P:cellular calcium ion homeostasis; IDA:UniProtKB.
 GO:0030026; P:cellular manganese ion homeostasis; IDA:UniProtKB.
 GO:0008544; P:epidermis development; IMP:UniProtKB.
 GO:0032468; P:Golgi calcium ion homeostasis; IMP:UniProtKB.
 GO:0032472; P:Golgi calcium ion transport; IMP:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB. 
Interpro
 IPR006413; ATPase_P-typ_Ca-transp_PMR1.
 IPR006068; ATPase_P-typ_cation-transptr_C.
 IPR004014; ATPase_P-typ_cation-transptr_N.
 IPR023299; ATPase_P-typ_cyto_domN.
 IPR018303; ATPase_P-typ_P_site.
 IPR023298; ATPase_P-typ_TM_dom.
 IPR008250; ATPase_P-typ_transduc_dom_A.
 IPR001757; Cation_transp_P_typ_ATPase.
 IPR023214; HAD-like_dom. 
Pfam
 PF00689; Cation_ATPase_C
 PF00690; Cation_ATPase_N
 PF00122; E1-E2_ATPase
 PF00702; Hydrolase 
SMART
 SM00831; Cation_ATPase_N 
PROSITE
 PS00154; ATPASE_E1_E2 
PRINTS
 PR00119; CATATPASE.
 PR00120; HATPASE.