TFP11_HUMAN - dbPTM
TFP11_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TFP11_HUMAN
UniProt AC Q9UBB9
Protein Name Tuftelin-interacting protein 11
Gene Name TFIP11
Organism Homo sapiens (Human).
Sequence Length 837
Subcellular Localization Cytoplasm. Nucleus. In the nucleus localizes to unique speckle domains in close proximity to nuclear speckles and not identical to paraspeckles..
Protein Description Involved in pre-mRNA splicing, specifically in spliceosome disassembly during late-stage splicing events. Intron turnover seems to proceed through reactions in two lariat-intron associated complexes termed Intron Large (IL) and Intron Small (IS). In cooperation with DHX15 seems to mediate the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. May play a role in the differentiation of ameloblasts and odontoblasts or in the forming of the enamel extracellular matrix..
Protein Sequence MSLSHLYRDGEGRIDDDDDERENFEITDWDLQNEFNPNRQRHWQTKEEATYGVWAERDSDDERPSFGGKRARDYSAPVNFISAGLKKGAAEEAELEDSDDEEKPVKQDDFPKDFGPRKLKTGGNFKPSQKGFAGGTKSFMDFGSWERHTKGIGQKLLQKMGYVPGRGLGKNAQGIINPIEAKQRKGKGAVGAYGSERTTQSMQDFPVVDSEEEAEEEFQKELSQWRKDPSGSKKKPKYSYKTVEELKAKGRISKKLTAPQKELSQVKVIDMTGREQKVYYSYSQISHKHNVPDDGLPLQSQQLPQSGKEAKAPGFALPELEHNLQLLIDLTEQEIIQNDRQLQYERDMVVNLFHELEKMTEVLDHEERVISNLSKVLEMVEECERRMQPDCSNPLTLDECARIFETLQDKYYEEYRMSDRVDLAVAIVYPLMKEYFKEWDPLKDCTYGTEIISKWKSLLENDQLLSHGGQDLSADAFHRLIWEVWMPFVRNIVTQWQPRNCDPMVDFLDSWVHIIPVWILDNILDQLIFPKLQKEVENWNPLTDTVPIHSWIHPWLPLMQARLEPLYSPIRSKLSSALQKWHPSDSSAKLILQPWKDVFTPGSWEAFMVKNIVPKLGMCLGELVINPHQQHMDAFYWVIDWEGMISVSSLVGLLEKHFFPKWLQVLCSWLSNSPNYEEITKWYLGWKSMFSDQVLAHPSVKDKFNEALDIMNRAVSSNVGAYMQPGARENIAYLTHTERRKDFQYEAMQERREAENMAQRGIGVAASSVPMNFKDLIETKAEEHNIVFMPVIGKRHEGKQLYTFGRIVIYIDRGVVFVQGEKTWVPTSLQSLIDMAK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MSLSHLYRD
------CCHHHCCCC		38.2823401153
4Phosphorylation----MSLSHLYRDGE
----CCHHHCCCCCC		12.2530108239
50PhosphorylationWQTKEEATYGVWAER
CCCHHHHCCCEEECC		24.8823927012
51PhosphorylationQTKEEATYGVWAERD
CCHHHHCCCEEECCC		19.4123927012
59PhosphorylationGVWAERDSDDERPSF
CEEECCCCCCCCCCC		53.8629255136
65PhosphorylationDSDDERPSFGGKRAR
CCCCCCCCCCCCCCC		42.6222167270
69MethylationERPSFGGKRARDYSA
CCCCCCCCCCCCCCC		43.17115979977
69AcetylationERPSFGGKRARDYSA
CCCCCCCCCCCCCCC		43.1725953088
74PhosphorylationGGKRARDYSAPVNFI
CCCCCCCCCCCCHHH		10.9427642862
75PhosphorylationGKRARDYSAPVNFIS
CCCCCCCCCCCHHHC		30.3123898821
82PhosphorylationSAPVNFISAGLKKGA
CCCCHHHCHHHHCCH		16.4923898821
86UbiquitinationNFISAGLKKGAAEEA
HHHCHHHHCCHHHHH		48.52-
86AcetylationNFISAGLKKGAAEEA
HHHCHHHHCCHHHHH		48.5223954790
87UbiquitinationFISAGLKKGAAEEAE
HHCHHHHCCHHHHHC		59.84-
87AcetylationFISAGLKKGAAEEAE
HHCHHHHCCHHHHHC		59.8430583175
98PhosphorylationEEAELEDSDDEEKPV
HHHCCCCCCCCCCCC		37.2729255136
126UbiquitinationLKTGGNFKPSQKGFA
CCCCCCCCCCCCCCC		48.00-
126AcetylationLKTGGNFKPSQKGFA
CCCCCCCCCCCCCCC		48.007432175
128PhosphorylationTGGNFKPSQKGFAGG
CCCCCCCCCCCCCCC		45.1525867546
130UbiquitinationGNFKPSQKGFAGGTK
CCCCCCCCCCCCCCC		61.40-
137AcetylationKGFAGGTKSFMDFGS
CCCCCCCCCCCCCCC		45.007432185
144PhosphorylationKSFMDFGSWERHTKG
CCCCCCCCHHHHCCH		26.2522617229
155UbiquitinationHTKGIGQKLLQKMGY
HCCHHHHHHHHHCCC		46.05-
155AcetylationHTKGIGQKLLQKMGY
HCCHHHHHHHHHCCC		46.0525953088
159UbiquitinationIGQKLLQKMGYVPGR
HHHHHHHHCCCCCCC		33.9721890473
159 (in isoform 1)Ubiquitination-33.9721890473
159UbiquitinationIGQKLLQKMGYVPGR
HHHHHHHHCCCCCCC		33.9721890473
162PhosphorylationKLLQKMGYVPGRGLG
HHHHHCCCCCCCCCC		10.4419690332
166MethylationKMGYVPGRGLGKNAQ
HCCCCCCCCCCCCCC		30.9754559941
170UbiquitinationVPGRGLGKNAQGIIN
CCCCCCCCCCCCCCC		54.90-
182UbiquitinationIINPIEAKQRKGKGA
CCCHHHHHHHCCCCC		37.53-
182AcetylationIINPIEAKQRKGKGA
CCCHHHHHHHCCCCC		37.5325953088
187AcetylationEAKQRKGKGAVGAYG
HHHHHCCCCCCCCCC		46.89133955
187UbiquitinationEAKQRKGKGAVGAYG
HHHHHCCCCCCCCCC		46.89-
193PhosphorylationGKGAVGAYGSERTTQ
CCCCCCCCCCCCCCC		18.43-
195PhosphorylationGAVGAYGSERTTQSM
CCCCCCCCCCCCCCC		15.9528857561
198PhosphorylationGAYGSERTTQSMQDF
CCCCCCCCCCCCCCC		25.7423403867
199PhosphorylationAYGSERTTQSMQDFP
CCCCCCCCCCCCCCC		25.5228464451
201PhosphorylationGSERTTQSMQDFPVV
CCCCCCCCCCCCCCC		19.1328464451
210PhosphorylationQDFPVVDSEEEAEEE
CCCCCCCCHHHHHHH		34.9919664994
223PhosphorylationEEFQKELSQWRKDPS
HHHHHHHHHHHCCCC		28.8722210691
240PhosphorylationKKKPKYSYKTVEELK
CCCCCCCCCCHHHHH		13.95-
241AcetylationKKPKYSYKTVEELKA
CCCCCCCCCHHHHHH		39.9025953088
241UbiquitinationKKPKYSYKTVEELKA
CCCCCCCCCHHHHHH		39.90-
249UbiquitinationTVEELKAKGRISKKL
CHHHHHHCCCCCCCC		47.32-
257PhosphorylationGRISKKLTAPQKELS
CCCCCCCCCCHHHHH		45.21-
261UbiquitinationKKLTAPQKELSQVKV
CCCCCCHHHHHCCEE		60.61-
261AcetylationKKLTAPQKELSQVKV
CCCCCCHHHHHCCEE		60.6126051181
264PhosphorylationTAPQKELSQVKVIDM
CCCHHHHHCCEEEEC		33.74-
267UbiquitinationQKELSQVKVIDMTGR
HHHHHCCEEEECCCC		26.32-
279PhosphorylationTGREQKVYYSYSQIS
CCCCEEEEEEHHHHC		8.1721945579
280PhosphorylationGREQKVYYSYSQISH
CCCEEEEEEHHHHCC		12.2421945579
281PhosphorylationREQKVYYSYSQISHK
CCEEEEEEHHHHCCC		10.7121945579
282PhosphorylationEQKVYYSYSQISHKH
CEEEEEEHHHHCCCC		6.6221945579
283PhosphorylationQKVYYSYSQISHKHN
EEEEEEHHHHCCCCC		18.3321945579
286PhosphorylationYYSYSQISHKHNVPD
EEEHHHHCCCCCCCC		20.8821945579
288AcetylationSYSQISHKHNVPDDG
EHHHHCCCCCCCCCC		30.0425953088
288UbiquitinationSYSQISHKHNVPDDG
EHHHHCCCCCCCCCC		30.04-
300PhosphorylationDDGLPLQSQQLPQSG
CCCCCCCCCCCCCCC		27.81-
306PhosphorylationQSQQLPQSGKEAKAP
CCCCCCCCCCCCCCC		50.3128555341
308AcetylationQQLPQSGKEAKAPGF
CCCCCCCCCCCCCCC		60.8025953088
308 (in isoform 1)Ubiquitination-60.8021890473
308UbiquitinationQQLPQSGKEAKAPGF
CCCCCCCCCCCCCCC		60.8021906983
311UbiquitinationPQSGKEAKAPGFALP
CCCCCCCCCCCCCCH		57.09-
344PhosphorylationQNDRQLQYERDMVVN
HCHHHHHHHHHHHHH		22.8628509920
371PhosphorylationDHEERVISNLSKVLE
CHHHHHHHHHHHHHH		28.9423312004
375UbiquitinationRVISNLSKVLEMVEE
HHHHHHHHHHHHHHH		54.74-
379SulfoxidationNLSKVLEMVEECERR
HHHHHHHHHHHHHHH		3.9321406390
392PhosphorylationRRMQPDCSNPLTLDE
HHCCCCCCCCCCHHH		49.1923401153
396PhosphorylationPDCSNPLTLDECARI
CCCCCCCCHHHHHHH		33.1630576142
410 (in isoform 1)Ubiquitination-36.4521890473
410UbiquitinationIFETLQDKYYEEYRM
HHHHHHHHHHHHHCC		36.452190698
437UbiquitinationPLMKEYFKEWDPLKD
HHHHHHHHHCCCCCC		57.92-
443UbiquitinationFKEWDPLKDCTYGTE
HHHCCCCCCCCCHHH		57.03-
454UbiquitinationYGTEIISKWKSLLEN
CHHHHHHHHHHHHHH		48.51-
567PhosphorylationQARLEPLYSPIRSKL
HHHHHHHHHHHHHHH		24.1023186163
568PhosphorylationARLEPLYSPIRSKLS
HHHHHHHHHHHHHHH		22.8727050516
573UbiquitinationLYSPIRSKLSSALQK
HHHHHHHHHHHHHHH		42.41-
580AcetylationKLSSALQKWHPSDSS
HHHHHHHHHCCCCHH		48.6025953088
580UbiquitinationKLSSALQKWHPSDSS
HHHHHHHHHCCCCHH		48.60-
589UbiquitinationHPSDSSAKLILQPWK
CCCCHHHCEEEECHH		37.70-
603PhosphorylationKDVFTPGSWEAFMVK
HCCCCCCCHHHHHHC		23.9724719451
701AcetylationVLAHPSVKDKFNEAL
CCCCHHHHHHHHHHH		60.587367805
716PhosphorylationDIMNRAVSSNVGAYM
HHHHHHHHCCCCHHC		18.4021945579
717PhosphorylationIMNRAVSSNVGAYMQ
HHHHHHHCCCCHHCC		29.0021945579
722PhosphorylationVSSNVGAYMQPGARE
HHCCCCHHCCCCHHH		7.1421945579
737PhosphorylationNIAYLTHTERRKDFQ
CCEEEECHHHHHHHH		26.4228555341
741UbiquitinationLTHTERRKDFQYEAM
EECHHHHHHHHHHHH		69.94-
745PhosphorylationERRKDFQYEAMQERR
HHHHHHHHHHHHHHH		12.9728796482
767PhosphorylationRGIGVAASSVPMNFK
HCCCHHCCCCCCCHH		23.33-
768PhosphorylationGIGVAASSVPMNFKD
CCCHHCCCCCCCHHH		26.05-
771SulfoxidationVAASSVPMNFKDLIE
HHCCCCCCCHHHHHH		9.6121406390
774UbiquitinationSSVPMNFKDLIETKA
CCCCCCHHHHHHHHH		46.77-
779PhosphorylationNFKDLIETKAEEHNI
CHHHHHHHHHHHCCE		28.67-
780UbiquitinationFKDLIETKAEEHNIV
HHHHHHHHHHHCCEE		40.8021906983
799UbiquitinationIGKRHEGKQLYTFGR
CCCCCCCCEEEEECE		33.86-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TFP11_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TFP11_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TFP11_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPPC4_HUMANTRAPPC4physical
21988832
PRP31_HUMANPRPF31physical
25416956
FA50B_HUMANFAM50Bphysical
25416956
NFU1_HUMANNFU1physical
25416956
RRP7A_HUMANRRP7Aphysical
25416956
DPOLL_HUMANPOLLphysical
25416956
FA156_HUMANFAM156Aphysical
25416956
S30BP_HUMANSAP30BPphysical
25416956
TFPT_HUMANTFPTphysical
25416956
SHLB1_HUMANSH3GLB1physical
25416956
ARMX1_HUMANARMCX1physical
25416956
HOOK1_HUMANHOOK1physical
25416956
K1C20_HUMANKRT20physical
25416956
CCHCR_HUMANCCHCR1physical
25416956
CA109_HUMANC1orf109physical
25416956
VP37C_HUMANVPS37Cphysical
25416956
IMP3_HUMANIMP3physical
25416956
RCOR3_HUMANRCOR3physical
25416956
LIN37_HUMANLIN37physical
25416956
COQ8A_HUMANADCK3physical
25416956
CCNL1_HUMANCCNL1physical
25416956
TSH3_HUMANTSHZ3physical
25416956
CC146_HUMANCCDC146physical
25416956
SH24A_HUMANSH2D4Aphysical
25416956
CARD9_HUMANCARD9physical
25416956
MET17_HUMANMETTL17physical
25416956
LENG1_HUMANLENG1physical
25416956
GCC1_HUMANGCC1physical
25416956
CC121_HUMANCCDC121physical
25416956
CENPU_HUMANCENPUphysical
25416956
ZC21C_HUMANZC2HC1Cphysical
25416956
CCD68_HUMANCCDC68physical
25416956
T3JAM_HUMANTRAF3IP3physical
25416956
PBX4_HUMANPBX4physical
25416956
THAP7_HUMANTHAP7physical
25416956
RHNO1_HUMANRHNO1physical
25416956
F161A_HUMANFAM161Aphysical
25416956
ZGPAT_HUMANZGPATphysical
25416956
BMF_HUMANBMFphysical
25416956
MTFR2_HUMANMTFR2physical
25416956
HAUS1_HUMANHAUS1physical
25416956
CC151_HUMANCCDC151physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
SFR1_HUMANSFR1physical
25416956
IKIP_HUMANIKBIPphysical
25416956
SNX20_HUMANSNX20physical
25416956
CCD42_HUMANCCDC42physical
25416956
ZN417_HUMANZNF417physical
25416956
LCA5L_HUMANLCA5Lphysical
25416956
C2CD6_HUMANALS2CR11physical
25416956
ZMAT2_HUMANZMAT2physical
25416956
CF206_HUMANC6orf165physical
25416956
CC116_HUMANCCDC116physical
25416956
PPR18_HUMANPPP1R18physical
25416956
THAP8_HUMANTHAP8physical
25416956
TXLNA_HUMANTXLNAphysical
25416956
FA13C_HUMANFAM13Cphysical
25416956
KANL1_HUMANKANSL1physical
25416956
CE57L_HUMANCEP57L1physical
25416956
K2C6C_HUMANKRT6Cphysical
25416956
PAXB1_HUMANPAXBP1physical
26344197
PRPF3_HUMANPRPF3physical
26344197
PRP4_HUMANPRPF4physical
26344197
SNUT1_HUMANSART1physical
26344197
KANL1_HUMANKANSL1physical
21516116
IL16_HUMANIL16physical
21516116
K1C20_HUMANKRT20physical
21516116
MET17_HUMANMETTL17physical
21516116
PP16A_HUMANPPP1R16Aphysical
21516116
UBP7_HUMANUSP7physical
26460617
MDM2_HUMANMDM2physical
26460617
P53_HUMANTP53physical
26460617
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TFP11_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59; SER-98; SER-210 ANDTYR-162, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98 AND SER-210, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, AND MASSSPECTROMETRY.

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