CSTF2_HUMAN - dbPTM
CSTF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSTF2_HUMAN
UniProt AC P33240
Protein Name Cleavage stimulation factor subunit 2
Gene Name CSTF2
Organism Homo sapiens (Human).
Sequence Length 577
Subcellular Localization Nucleus . Localized with DDX1 in cleavage bodies.
Protein Description One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs (By similarity)..
Protein Sequence MAGLTVRDPAVDRSLRSVFVGNIPYEATEEQLKDIFSEVGPVVSFRLVYDRETGKPKGYGFCEYQDQETALSAMRNLNGREFSGRALRVDNAASEKNKEELKSLGTGAPVIESPYGETISPEDAPESISKAVASLPPEQMFELMKQMKLCVQNSPQEARNMLLQNPQLAYALLQAQVVMRIVDPEIALKILHRQTNIPTLIAGNPQPVHGAGPGSGSNVSMNQQNPQAPQAQSLGGMHVNGAPPLMQASMQGGVPAPGQMPAAVTGPGPGSLAPGGGMQAQVGMPGSGPVSMERGQVPMQDPRAAMQRGSLPANVPTPRGLLGDAPNDPRGGTLLSVTGEVEPRGYLGPPHQGPPMHHVPGHESRGPPPHELRGGPLPEPRPLMAEPRGPMLDQRGPPLDGRGGRDPRGIDARGMEARAMEARGLDARGLEARAMEARAMEARAMEARAMEARAMEVRGMEARGMDTRGPVPGPRGPIPSGMQGPSPINMGAVVPQGSRQVPVMQGTGMQGASIQGGSQPGGFSPGQNQVTPQDHEKAALIMQVLQLTADQIAMLPPEQRQSILILKEQIQKSTGAP
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
2Acetylation------MAGLTVRDP
------CCCCEECCH		23.00-
14PhosphorylationRDPAVDRSLRSVFVG
CCHHHCHHHHHEEEC		24.5423186163
44PhosphorylationSEVGPVVSFRLVYDR
HHHCCEEEEEEEEEC		12.6024719451
57AcetylationDRETGKPKGYGFCEY
ECCCCCCCEECCCCC		69.1526051181
96UbiquitinationVDNAASEKNKEELKS
CCCHHHHHCHHHHHH		71.47-
96AcetylationVDNAASEKNKEELKS
CCCHHHHHCHHHHHH		71.4725953088
103PhosphorylationKNKEELKSLGTGAPV
HCHHHHHHCCCCCCE		44.6627732954
106PhosphorylationEELKSLGTGAPVIES
HHHHHCCCCCCEEEC		35.1530624053
113PhosphorylationTGAPVIESPYGETIS
CCCCEEECCCCCCCC		16.5827273156
115PhosphorylationAPVIESPYGETISPE
CCEEECCCCCCCCHH		36.5525884760
118PhosphorylationIESPYGETISPEDAP
EECCCCCCCCHHHCC		23.5325159151
120PhosphorylationSPYGETISPEDAPES
CCCCCCCCHHHCCHH		29.6525159151
127PhosphorylationSPEDAPESISKAVAS
CHHHCCHHHHHHHHC		30.9727732954
129PhosphorylationEDAPESISKAVASLP
HHCCHHHHHHHHCCC		24.6827732954
130UbiquitinationDAPESISKAVASLPP
HCCHHHHHHHHCCCH		45.25-
145UbiquitinationEQMFELMKQMKLCVQ
HHHHHHHHHHHHHHH		60.92-
148UbiquitinationFELMKQMKLCVQNSP
HHHHHHHHHHHHCCH		35.92-
148AcetylationFELMKQMKLCVQNSP
HHHHHHHHHHHHCCH		35.9226051181
150GlutathionylationLMKQMKLCVQNSPQE
HHHHHHHHHHCCHHH		2.1722555962
154PhosphorylationMKLCVQNSPQEARNM
HHHHHHCCHHHHHHH		15.7425159151
189UbiquitinationVDPEIALKILHRQTN
CCHHHHHHHHHHHCC		33.9120972266
189AcetylationVDPEIALKILHRQTN
CCHHHHHHHHHHHCC		33.9125953088
189SumoylationVDPEIALKILHRQTN
CCHHHHHHHHHHHCC		33.9128112733
189 (in isoform 1)Ubiquitination-33.9121890473
189 (in isoform 2)Ubiquitination-33.9121890473
299SulfoxidationMERGQVPMQDPRAAM
CCCCCCCCCCHHHHH		8.0921406390
303MethylationQVPMQDPRAAMQRGS
CCCCCCHHHHHHHCC		43.18-
308MethylationDPRAAMQRGSLPANV
CHHHHHHHCCCCCCC		24.4724129315
310PhosphorylationRAAMQRGSLPANVPT
HHHHHHCCCCCCCCC		33.1125159151
317PhosphorylationSLPANVPTPRGLLGD
CCCCCCCCCCCCCCC		22.7229396449
319MethylationPANVPTPRGLLGDAP
CCCCCCCCCCCCCCC		51.36-
330MethylationGDAPNDPRGGTLLSV
CCCCCCCCCCCEEEE		60.06-
333PhosphorylationPNDPRGGTLLSVTGE
CCCCCCCCEEEEECE		27.6120860994
336PhosphorylationPRGGTLLSVTGEVEP
CCCCCEEEEECEECC		22.2720860994
338PhosphorylationGGTLLSVTGEVEPRG
CCCEEEEECEECCCC		25.0120860994
344MethylationVTGEVEPRGYLGPPH
EECEECCCCCCCCCC		32.65-
364PhosphorylationHHVPGHESRGPPPHE
CCCCCCCCCCCCCCC		36.5430257219
365MethylationHVPGHESRGPPPHEL
CCCCCCCCCCCCCCC		59.66-
373MethylationGPPPHELRGGPLPEP
CCCCCCCCCCCCCCC		45.07-
381MethylationGGPLPEPRPLMAEPR
CCCCCCCCCCCCCCC		35.01-
388MethylationRPLMAEPRGPMLDQR
CCCCCCCCCCCCCCC		54.04-
402MethylationRGPPLDGRGGRDPRG
CCCCCCCCCCCCCCC		44.02-
405MethylationPLDGRGGRDPRGIDA
CCCCCCCCCCCCCCC		54.29-
423MethylationEARAMEARGLDARGL
HHHHHHHCCCCHHHH		32.66-
428MethylationEARGLDARGLEARAM
HHCCCCHHHHHHHHH		50.31-
458MethylationEARAMEVRGMEARGM
HHHHHHHHCHHHCCC		25.99-
463MethylationEVRGMEARGMDTRGP
HHHCHHHCCCCCCCC		27.88-
468MethylationEARGMDTRGPVPGPR
HHCCCCCCCCCCCCC		43.0624129315
468DimethylationEARGMDTRGPVPGPR
HHCCCCCCCCCCCCC		43.06-
475MethylationRGPVPGPRGPIPSGM
CCCCCCCCCCCCCCC		70.2324129315
475DimethylationRGPVPGPRGPIPSGM
CCCCCCCCCCCCCCC		70.23-
480PhosphorylationGPRGPIPSGMQGPSP
CCCCCCCCCCCCCCC		47.8420068231
486PhosphorylationPSGMQGPSPINMGAV
CCCCCCCCCCCCCCC		45.2820068231
498PhosphorylationGAVVPQGSRQVPVMQ
CCCCCCCCCCCEEEE		17.8120068231
499MethylationAVVPQGSRQVPVMQG
CCCCCCCCCCEEEEC		48.63-
507PhosphorylationQVPVMQGTGMQGASI
CCEEEECCCCCCCCC		16.7629255136
513PhosphorylationGTGMQGASIQGGSQP
CCCCCCCCCCCCCCC		23.4429255136
518PhosphorylationGASIQGGSQPGGFSP
CCCCCCCCCCCCCCC		39.7717525332
524PhosphorylationGSQPGGFSPGQNQVT
CCCCCCCCCCCCCCC		31.2529255136
531PhosphorylationSPGQNQVTPQDHEKA
CCCCCCCCCCHHHHH		12.8829255136
555 (in isoform 2)Ubiquitination-4.7721890473
562PhosphorylationLPPEQRQSILILKEQ
CCHHHHHHHHHHHHH		22.8821406692
5672-HydroxyisobutyrylationRQSILILKEQIQKST
HHHHHHHHHHHHHHH		40.35-
567AcetylationRQSILILKEQIQKST
HHHHHHHHHHHHHHH		40.3526051181
567UbiquitinationRQSILILKEQIQKST
HHHHHHHHHHHHHHH		40.35-
572 (in isoform 1)Ubiquitination-52.1721890473
572UbiquitinationILKEQIQKSTGAP--
HHHHHHHHHHCCC--		52.17-
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 CSTF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSTF2_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 CSTF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCP4_HUMANSUB1physical
11389848
UBQL1_HUMANUBQLN1physical
16189514
ECH1_HUMANECH1physical
16169070
FEZ1_HUMANFEZ1physical
16169070
KAT5_HUMANKAT5physical
16169070
ELP1_HUMANIKBKAPphysical
16169070
MIC60_HUMANIMMTphysical
16169070
BAG6_HUMANBAG6physical
16169070
ERG28_HUMANC14orf1physical
16169070
CHD3_HUMANCHD3physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
CE126_HUMANKIAA1377physical
16169070
SYMPK_HUMANSYMPKphysical
10669729
CSTF3_HUMANCSTF3physical
10669729
CSTF1_HUMANCSTF1physical
10669729
CPSF1_HUMANCPSF1physical
10669729
CPSF2_HUMANCPSF2physical
10669729
CDC73_HUMANCDC73physical
19136632
A4_HUMANAPPphysical
21832049
CSTF3_HUMANCSTF3physical
22939629
DDX1_HUMANDDX1physical
22939629
MAX_HUMANMAXphysical
22939629
IF4B_HUMANEIF4Bphysical
22939629
NU153_HUMANNUP153physical
22939629
DDB1_HUMANDDB1physical
22939629
PARN_HUMANPARNphysical
20379136
BARD1_HUMANBARD1physical
20379136
BABA1_HUMANBABAM1physical
22863883
CDN2A_HUMANCDKN2Aphysical
22863883
ARF_HUMANCDKN2Aphysical
22863883
GET4_HUMANGET4physical
22863883
MAP4_HUMANMAP4physical
22863883
LSM8_HUMANLSM8physical
22863883
HGS_HUMANHGSphysical
25416956
TFG_HUMANTFGphysical
25416956
CREST_HUMANSS18L1physical
25416956
SPAG8_HUMANSPAG8physical
25416956
UBQL1_HUMANUBQLN1physical
25416956
ZN341_HUMANZNF341physical
25416956
CD2AP_HUMANCD2APphysical
26344197
CHM2A_HUMANCHMP2Aphysical
26344197
CSTF1_HUMANCSTF1physical
26344197
CSTFT_HUMANCSTF2Tphysical
26344197
CSTF3_HUMANCSTF3physical
26344197
DD19B_HUMANDDX19Bphysical
26344197
K1143_HUMANKIAA1143physical
26344197
PAPOB_HUMANPAPOLBphysical
26344197
PCF11_HUMANPCF11physical
26344197
SH3K1_HUMANSH3KBP1physical
26344197
TTC27_HUMANTTC27physical
26344197
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 CSTF2_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 ALA-2, AND MASS SPECTROMETRY.
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-524, 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-154 AND SER-524, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518 AND SER-524, ANDMASS SPECTROMETRY.

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