CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014086
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Striatin-interacting protein 1 
Protein Synonyms/Alias
 Protein FAM40A 
Gene Name
 STRIP1 
Gene Synonyms/Alias
 FAM40A; KIAA1761 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
47AGLLPGGKAREFNRNubiquitination[1]
99PEFLMNRKCFEEDFRubiquitination[1, 2]
326PLPEDSIKVIRNMRAubiquitination[1, 2]
420TDRLTCPKGLPWAPKubiquitination[1]
536LAAAPTSKAKTDSINubiquitination[3]
538AAPTSKAKTDSINILubiquitination[1]
722KLLKVQTKYLGRQWRmethylation[4]
722KLLKVQTKYLGRQWRubiquitination[3]
742TMSAIYQKVRHRLNDubiquitination[1, 5, 6]
828LEREVFSKPISWEELubiquitination[1, 3, 7]
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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] 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]
 [4] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572
Functional Description
 Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 59 59 Phosphoserine (By similarity).
 MOD_RES 335 335 Phosphoserine.
 MOD_RES 560 560 Phosphoserine (By similarity).
 MOD_RES 831 831 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 837 AA 
Protein Sequence
MEPAVGGPGP LIVNNKQPQP PPPPPPAAAQ PPPGAPRAAA GLLPGGKARE FNRNQRKDSE 60
GYSESPDLEF EYADTDKWAA ELSELYSYTE GPEFLMNRKC FEEDFRIHVT DKKWTELDTN 120
QHRTHAMRLL DGLEVTAREK RLKVARAILY VAQGTFGECS SEAEVQSWMR YNIFLLLEVG 180
TFNALVELLN MEIDNSAACS SAVRKPAISL ADSTDLRVLL NIMYLIVETV HQECEGDKAE 240
WRTMRQTFRA ELGSPLYNNE PFAIMLFGMV TKFCSGHAPH FPMKKVLLLL WKTVLCTLGG 300
FEELQSMKAE KRSILGLPPL PEDSIKVIRN MRAASPPASA SDLIEQQQKR GRREHKALIK 360
QDNLDAFNER DPYKADDSRE EEEENDDDNS LEGETFPLER DEVMPPPLQH PQTDRLTCPK 420
GLPWAPKVRE KDIEMFLESS RSKFIGYTLG SDTNTVVGLP RPIHESIKTL KQHKYTSIAE 480
VQAQMEEEYL RSPLSGGEEE VEQVPAETLY QGLLPSLPQY MIALLKILLA AAPTSKAKTD 540
SINILADVLP EEMPTTVLQS MKLGVDVNRH KEVIVKAISA VLLLLLKHFK LNHVYQFEYM 600
AQHLVFANCI PLILKFFNQN IMSYITAKNS ISVLDYPHCV VHELPELTAE SLEAGDSNQF 660
CWRNLFSCIN LLRILNKLTK WKHSRTMMLV VFKSAPILKR ALKVKQAMMQ LYVLKLLKVQ 720
TKYLGRQWRK SNMKTMSAIY QKVRHRLNDD WAYGNDLDAR PWDFQAEECA LRANIERFNA 780
RRYDRAHSNP DFLPVDNCLQ SVLGQRVDLP EDFQMNYDLW LEREVFSKPI SWEELLQ 837 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
 GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB. 
Interpro
 IPR021819; DUF3402.
 IPR012486; N1221. 
Pfam
 PF11882; DUF3402
 PF07923; N1221 
SMART
  
PROSITE
  
PRINTS