CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022811
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tuftelin-interacting protein 11 
Protein Synonyms/Alias
 Septin and tuftelin-interacting protein 1; STIP-1 
Gene Name
 TFIP11 
Gene Synonyms/Alias
 STIP; HSPC006 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
86NFISAGLKKGAAEEAubiquitination[1]
87FISAGLKKGAAEEAEubiquitination[1]
159IGQKLLQKMGYVPGRubiquitination[1, 2, 3]
170VPGRGLGKNAQGIINubiquitination[1]
182IINPIEAKQRKGKGAubiquitination[1]
241KKPKYSYKTVEELKAubiquitination[1]
249TVEELKAKGRISKKLubiquitination[1]
261KKLTAPQKELSQVKVubiquitination[1]
267QKELSQVKVIDMTGRubiquitination[1]
308QQLPQSGKEAKAPGFubiquitination[4]
311PQSGKEAKAPGFALPubiquitination[1]
375RVISNLSKVLEMVEEubiquitination[1]
410IFETLQDKYYEEYRMubiquitination[1, 4]
443FKEWDPLKDCTYGTEubiquitination[1]
573LYSPIRSKLSSALQKubiquitination[1]
580KLSSALQKWHPSDSSubiquitination[1]
741LTHTERRKDFQYEAMubiquitination[1]
774SSVPMNFKDLIETKAubiquitination[1]
780FKDLIETKAEEHNIVubiquitination[3, 5, 6]
799IGKRHEGKQLYTFGRubiquitination[1]
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] 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]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] 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]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] 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
Functional Description
 May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix. May also be involved in pre-mRNA splicing. 
Sequence Annotation
 DOMAIN 149 195 G-patch.
 MOD_RES 59 59 Phosphoserine.
 MOD_RES 98 98 Phosphoserine.
 MOD_RES 144 144 Phosphoserine.
 MOD_RES 210 210 Phosphoserine.  
Keyword
 Alternative splicing; Biomineralization; Complete proteome; Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 837 AA 
Protein Sequence
MSLSHLYRDG EGRIDDDDDE RENFEITDWD LQNEFNPNRQ RHWQTKEEAT YGVWAERDSD 60
DERPSFGGKR ARDYSAPVNF ISAGLKKGAA EEAELEDSDD EEKPVKQDDF PKDFGPRKLK 120
TGGNFKPSQK GFAGGTKSFM DFGSWERHTK GIGQKLLQKM GYVPGRGLGK NAQGIINPIE 180
AKQRKGKGAV GAYGSERTTQ SMQDFPVVDS EEEAEEEFQK ELSQWRKDPS GSKKKPKYSY 240
KTVEELKAKG RISKKLTAPQ KELSQVKVID MTGREQKVYY SYSQISHKHN VPDDGLPLQS 300
QQLPQSGKEA KAPGFALPEL EHNLQLLIDL TEQEIIQNDR QLQYERDMVV NLFHELEKMT 360
EVLDHEERVI SNLSKVLEMV EECERRMQPD CSNPLTLDEC ARIFETLQDK YYEEYRMSDR 420
VDLAVAIVYP LMKEYFKEWD PLKDCTYGTE IISKWKSLLE NDQLLSHGGQ DLSADAFHRL 480
IWEVWMPFVR NIVTQWQPRN CDPMVDFLDS WVHIIPVWIL DNILDQLIFP KLQKEVENWN 540
PLTDTVPIHS WIHPWLPLMQ ARLEPLYSPI RSKLSSALQK WHPSDSSAKL ILQPWKDVFT 600
PGSWEAFMVK NIVPKLGMCL GELVINPHQQ HMDAFYWVID WEGMISVSSL VGLLEKHFFP 660
KWLQVLCSWL SNSPNYEEIT KWYLGWKSMF SDQVLAHPSV KDKFNEALDI MNRAVSSNVG 720
AYMQPGAREN IAYLTHTERR KDFQYEAMQE RREAENMAQR GIGVAASSVP MNFKDLIETK 780
AEEHNIVFMP VIGKRHEGKQ LYTFGRIVIY IDRGVVFVQG EKTWVPTSLQ SLIDMAK 837 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0016607; C:nuclear speck; IDA:LIFEdb.
 GO:0005578; C:proteinaceous extracellular matrix; IEA:Compara.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
 GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR000467; G_patch_dom.
 IPR022783; GCFC_dom.
 IPR024933; STIP.
 IPR022159; TIP_N. 
Pfam
 PF01585; G-patch
 PF07842; GCFC
 PF12457; TIP_N 
SMART
 SM00443; G_patch 
PROSITE
 PS50174; G_PATCH 
PRINTS