| Tag | Content |
|---|
| CPLM ID | CPLM-014060 |
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 |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 86 | NFISAGLKKGAAEEA | acetylation | [1] | | 155 | HTKGIGQKLLQKMGY | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
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 (By similarity). |
Sequence Annotation | DOMAIN 149 195 G-patch.
MOD_RES 59 59 Phosphoserine (By similarity).
MOD_RES 95 95 Phosphoserine (By similarity).
MOD_RES 98 98 Phosphoserine (By similarity).
MOD_RES 144 144 Phosphoserine (By similarity).
MOD_RES 210 210 Phosphoserine (By similarity). |
Keyword | Biomineralization; Complete proteome; Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 837 AA |
Protein Sequence | MSLSHLYRDG EGHLDDDDDE RENFEITDWD LQNEFNPNRQ RHWQTKEEAT YGVWAERDSD 60
EERPSFGGKR ARDYSAPVNF ISAGLKKGAA EEADSEDSDA EEKPVKQEDF PKDLGPKKLK 120
TGGNFKPSQK GFAGGTKSFM DFGSWERHTK GIGQKLLQKM GYVPGRGLGK NAQGIINPIE 180
AKQRKGKGAV GAYGSERTTQ SLQDFPVADS EEEAEEEFQK ELSQWRKDPS GSKKKPKYSY 240
KTVEELKAKG RVSKKLTAPQ KELSQVKVID MTGREQKVYY SYSQISHKHS VPDEGVPLLA 300
QLPPTAGKEA KVPGFALPEL EHNLQLLIER TEQEIIQSDR QLQYERDMVV SLSHELEKTA 360
EVLAHEERVI SNLSKVLALV EECEHRMQPH GADPLTLDEC ARIFETLQDK YYEEYRLADR 420
ADLAVAIVYP LVKDYFKDWH PLEDSNYGTQ IISKWKSLLE NDQLLSHSSQ DLSSDAFHRL 480
MWEVWMPFVR NVVAQWQPRN CEPMVDFLDS WAHIIPVWIL DNILDQLIFP KLQKEVDNWN 540
PLTDTVPIHS WIHPWLPLMQ ARLEPLYSPV RSKLSSALQK WHPSDASAKL ILQPWKEVLT 600
PGSWEAFMLR NIVPKLGMCL GELVINPHQQ HMDAFYWVMD 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; IEA:Compara. GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0016607; C:nuclear speck; IEA:Compara. GO:0005578; C:proteinaceous extracellular matrix; IEA:Compara. GO:0005681; C:spliceosomal complex; ISS:UniProtKB. GO:0003677; F:DNA binding; IEA:InterPro. GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW. GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |