CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012157
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Stromal interaction molecule 1 
Protein Synonyms/Alias
  
Gene Name
 STIM1 
Gene Synonyms/Alias
 GOK 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
156QYEETFRKLQLSGHAubiquitination[1]
267DLQERLHKAQEEHRTubiquitination[2]
279HRTVEVEKVHLEKKLubiquitination[1]
285EKVHLEKKLRDEINLubiquitination[1]
294RDEINLAKQEAQRLKubiquitination[1]
315ENERSRQKYAEEELEubiquitination[1]
330QVREALRKAEKELESubiquitination[1]
377EKQLLVAKEGAEKIKubiquitination[1]
413DHKILTAKQALSEVTubiquitination[1, 2]
Reference
 [1] 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]
 [2] 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] 
Functional Description
 Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Acts as Ca(2+) sensor in the endoplasmic reticulum via its EF-hand domain. Upon Ca(2+) depletion, translocates from the endoplasmic reticulum to the plasma membrane where it activates the Ca(2+) release-activated Ca(2+) (CRAC) channel subunit, TMEM142A/ORAI1. 
Sequence Annotation
 DOMAIN 63 98 EF-hand.
 DOMAIN 132 200 SAM.
 REGION 334 444 SOAR/CAD.
 MOTIF 642 645 Microtubule tip localization signal.
 MOD_RES 257 257 Phosphoserine.
 MOD_RES 519 519 Phosphoserine.
 MOD_RES 524 524 Phosphoserine (By similarity).
 MOD_RES 575 575 Phosphoserine.
 MOD_RES 608 608 Phosphoserine.
 MOD_RES 660 660 Phosphoserine.
 MOD_RES 665 665 Phosphothreonine.
 MOD_RES 668 668 Phosphoserine.
 CARBOHYD 131 131 N-linked (GlcNAc...).
 CARBOHYD 171 171 N-linked (GlcNAc...).  
Keyword
 3D-structure; Calcium; Calcium transport; Cell membrane; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Endoplasmic reticulum; Glycoprotein; Ion transport; Membrane; Metal-binding; Microtubule; Phosphoprotein; Polymorphism; Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 685 AA 
Protein Sequence
MDVCVRLALW LLWGLLLHQG QSLSHSHSEK ATGTSSGANS EESTAAEFCR IDKPLCHSED 60
EKLSFEAVRN IHKLMDDDAN GDVDVEESDE FLREDLNYHD PTVKHSTFHG EDKLISVEDL 120
WKAWKSSEVY NWTVDEVVQW LITYVELPQY EETFRKLQLS GHAMPRLAVT NTTMTGTVLK 180
MTDRSHRQKL QLKALDTVLF GPPLLTRHNH LKDFMLVVSI VIGVGGCWFA YIQNRYSKEH 240
MKKMMKDLEG LHRAEQSLHD LQERLHKAQE EHRTVEVEKV HLEKKLRDEI NLAKQEAQRL 300
KELREGTENE RSRQKYAEEE LEQVREALRK AEKELESHSS WYAPEALQKW LQLTHEVEVQ 360
YYNIKKQNAE KQLLVAKEGA EKIKKKRNTL FGTFHVAHSS SLDDVDHKIL TAKQALSEVT 420
AALRERLHRW QQIEILCGFQ IVNNPGIHSL VAALNIDPSW MGSTRPNPAH FIMTDDVDDM 480
DEEIVSPLSM QSPSLQSSVR QRLTEPQHGL GSQRDLTHSD SESSLHMSDR QRVAPKPPQM 540
SRAADEALNA MTSNGSHRLI EGVHPGSLVE KLPDSPALAK KALLALNHGL DKAHSLMELS 600
PSAPPGGSPH LDSSRSHSPS SPDPDTPSPV GDSRALQASR NTRIPHLAGK KAVAEEDNGS 660
IGEETDSSPG RKKFPLKIFK KPLKK 685 
Gene Ontology
 GO:0032541; C:cortical endoplasmic reticulum; IDA:UniProtKB.
 GO:0030176; C:integral to endoplasmic reticulum membrane; IDA:UniProtKB.
 GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005509; F:calcium ion binding; IDA:UniProtKB.
 GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
 GO:0032237; P:activation of store-operated calcium channel activity; IDA:UniProtKB.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
 GO:0005513; P:detection of calcium ion; IDA:UniProtKB. 
Interpro
 IPR001660; SAM.
 IPR013761; SAM/pointed.
 IPR011510; SAM_2. 
Pfam
 PF07647; SAM_2 
SMART
 SM00454; SAM 
PROSITE
 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS50105; SAM_DOMAIN 
PRINTS