CTIF_HUMAN - dbPTM
CTIF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CTIF_HUMAN
UniProt AC O43310
Protein Name CBP80/20-dependent translation initiation factor
Gene Name CTIF
Organism Homo sapiens (Human).
Sequence Length 598
Subcellular Localization Cytoplasm, perinuclear region .
Protein Description Specifically required for the pioneer round of mRNA translation mediated by the cap-binding complex (CBC), that takes place during or right after mRNA export via the nuclear pore complex (NPC). Acts via its interaction with the NCBP1/CBP80 component of the CBC complex and recruits the 40S small subunit of the ribosome via eIF3. In contrast, it is not involved in steady state translation, that takes place when the CBC complex is replaced by cytoplasmic cap-binding protein eIF4E. Also required for nonsense-mediated mRNA decay (NMD), the pioneer round of mRNA translation mediated by the cap-binding complex playing a central role in nonsense-mediated mRNA decay (NMD)..
Protein Sequence MENSSAASASSEAGSSRSQEIEELERFIDSYVLEYQVQGLLADKTEGDGESERTQSHISQWTADCSEPLDSSCSFSRGRAPPQQNGSKDNSLDMLGTDIWAANTFDSFSGATWDLQPEKLDFTQFHRKVRHTPKQPLPHIDREGCGKGKLEDGDGINLNDIEKVLPAWQGYHPMPHEVEIAHTKKLFRRRRNDRRRQQRPPGGNKPQQHGDHQPGSAKHNRDHQKSYQGGSAPHPSGRPTHHGYSQNRRWHHGNMKHPPGDKGEAGAHRNAKETMTIENPKLEDTAGDTGHSSLEAPRSPDTLAPVASERLPPQQSGGPEVETKRKDSILPERIGERPKITLLQSSKDRLRRRLKEKDEVAVETTTPQQNKMDKLIEILNSMRNNSSDVDTKLTTFMEEAQNSTNSEEMLGEIVRTIYQKAVSDRSFAFTAAKLCDKMALFMVEGTKFRSLLLNMLQKDFTVREELQQQDVERWLGFITFLCEVFGTMRSSTGEPFRVLVCPIYTCLRELLQSQDVKEDAVLCCSMELQSTGRLLEEQLPEMMTELLASARDKMLCPSESMLTRSLLLEVIELHANSWNPLTPPITQYYNRTIQKLTA
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
1Acetylation-------MENSSAAS
-------CCCCCHHH		11.2522814378
4Phosphorylation----MENSSAASASS
----CCCCCHHHHCC		14.1927251275
5Phosphorylation---MENSSAASASSE
---CCCCCHHHHCCC		39.1628450419
8PhosphorylationMENSSAASASSEAGS
CCCCCHHHHCCCCCC		28.5328450419
10PhosphorylationNSSAASASSEAGSSR
CCCHHHHCCCCCCCC		26.6428450419
11PhosphorylationSSAASASSEAGSSRS
CCHHHHCCCCCCCCH		31.0528450419
15PhosphorylationSASSEAGSSRSQEIE
HHCCCCCCCCHHHHH		29.6228450419
16PhosphorylationASSEAGSSRSQEIEE
HCCCCCCCCHHHHHH		34.7328450419
18PhosphorylationSEAGSSRSQEIEELE
CCCCCCCHHHHHHHH		33.8323401153
35PhosphorylationIDSYVLEYQVQGLLA
HHHHHHHHHHHHHHC		15.1528796482
71PhosphorylationDCSEPLDSSCSFSRG
CCCCCCCCCCCCCCC		40.7128857561
72PhosphorylationCSEPLDSSCSFSRGR
CCCCCCCCCCCCCCC		17.2828857561
74PhosphorylationEPLDSSCSFSRGRAP
CCCCCCCCCCCCCCC		28.3623186163
123PhosphorylationQPEKLDFTQFHRKVR
CHHHCCHHHHHHHCC		29.9629978859
216PhosphorylationHGDHQPGSAKHNRDH
CCCCCCCCCCCCCCC		40.6128555341
226PhosphorylationHNRDHQKSYQGGSAP
CCCCCCHHCCCCCCC		19.00-
274PhosphorylationAHRNAKETMTIENPK
CCCCCCCCEEEECCC		20.9323186163
276PhosphorylationRNAKETMTIENPKLE
CCCCCCEEEECCCHH		32.3423186163
285PhosphorylationENPKLEDTAGDTGHS
ECCCHHCCCCCCCCC		24.1423403867
289PhosphorylationLEDTAGDTGHSSLEA
HHCCCCCCCCCCCCC		35.5623927012
292PhosphorylationTAGDTGHSSLEAPRS
CCCCCCCCCCCCCCC		37.6523927012
293PhosphorylationAGDTGHSSLEAPRSP
CCCCCCCCCCCCCCC		25.2623927012
299PhosphorylationSSLEAPRSPDTLAPV
CCCCCCCCCCCCCCH		26.5219664994
302PhosphorylationEAPRSPDTLAPVASE
CCCCCCCCCCCHHHC		28.3630266825
308PhosphorylationDTLAPVASERLPPQQ
CCCCCHHHCCCCCCC		24.3922167270
328PhosphorylationVETKRKDSILPERIG
CCCCCCCCCCHHHCC		29.1228102081
364PhosphorylationKDEVAVETTTPQQNK
HCCHHEECCCCCCCH		29.3922210691
365PhosphorylationDEVAVETTTPQQNKM
CCHHEECCCCCCCHH		23.9922210691
366PhosphorylationEVAVETTTPQQNKMD
CHHEECCCCCCCHHH		26.9021815630
458AcetylationLLLNMLQKDFTVREE
HHHHHHHCCCCHHHH		51.347976049
544PhosphorylationEQLPEMMTELLASAR
HHHHHHHHHHHHHHH		23.3629888752
549PhosphorylationMMTELLASARDKMLC
HHHHHHHHHHHHCCC		24.6529888752
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 CTIF_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CTIF_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 CTIF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CTIF_HUMAN !!
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 CTIF_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-16 AND SER-18, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-16 AND SER-18, AND MASS SPECTROMETRY.
"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-18, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASSSPECTROMETRY.

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