CPSF6_HUMAN - dbPTM
CPSF6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CPSF6_HUMAN
UniProt AC Q16630
Protein Name Cleavage and polyadenylation specificity factor subunit 6 {ECO:0000305}
Gene Name CPSF6 {ECO:0000312|HGNC:HGNC:13871}
Organism Homo sapiens (Human).
Sequence Length 551
Subcellular Localization Nucleus . Nucleus, nucleoplasm . Nucleus speckle . Cytoplasm . Shuttles between the nucleus and the cytoplasm in a transcription- and XPO1/CRM1-independent manner, most probably in complex with the cleavage factor Im complex (CFIm) (PubMed:19864460).
Protein Description Component of the cleavage factor Im (CFIm) complex that functions as an activator of the pre-mRNA 3'-end cleavage and polyadenylation processing required for the maturation of pre-mRNA into functional mRNAs. [PubMed: 9659921]
Protein Sequence MADGVDHIDIYADVGEEFNQEAEYGGHDQIDLYDDVISPSANNGDAPEDRDYMDTLPPTVGDDVGKGAAPNVVYTYTGKRIALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANGQSKGFALVGVGSEASSKKLMDLLPKRELHGQNPVVTPCNKQFLSQFEMQSRKTTQSGQMSGEGKAGPPGGSSRAAFPQGGRGRGRFPGAVPGGDRFPGPAGPGGPPPPFPAGQTPPRPPLGPPGPPGPPGPPPPGQVLPPPLAGPPNRGDRPPPPVLFPGQPFGQPPLGPLPPGPPPPVPGYGPPPGPPPPQQGPPPPPGPFPPRPPGPLGPPLTLAPPPHLPGPPPGAPPPAPHVNPAFFPPPTNSGMPTSDSRGPPPTDPYGRPPPYDRGDYGPPGREMDTARTPLSEAEFEEIMNRNRAISSSAISRAVSDASAGDYGSAIETLVTAISLIKQSKVSADDRCKVLISSLQDCLHGIESKSYGSGSRRERSRERDHSRSREKSRRHKSRSRDRHDDYYRERSRERERHRDRDRDRDRERDREREYRHR
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
33PhosphorylationGHDQIDLYDDVISPS
CCCCCCCCCCCCCCC		13.3226074081
38PhosphorylationDLYDDVISPSANNGD
CCCCCCCCCCCCCCC		16.7926657352
40PhosphorylationYDDVISPSANNGDAP
CCCCCCCCCCCCCCC		36.5226074081
52PhosphorylationDAPEDRDYMDTLPPT
CCCCCCCCHHCCCCC		9.5923532336
55PhosphorylationEDRDYMDTLPPTVGD
CCCCCHHCCCCCCCC		25.3219664995
74PhosphorylationGAAPNVVYTYTGKRI
CCCCCEEEEECCCEE		6.9721945579
75PhosphorylationAAPNVVYTYTGKRIA
CCCCEEEEECCCEEE		11.7321945579
76PhosphorylationAPNVVYTYTGKRIAL
CCCEEEEECCCEEEE		8.8721945579
77PhosphorylationPNVVYTYTGKRIALY
CCEEEEECCCEEEEE		28.5521945579
79 (in isoform 3)Ubiquitination-32.6021890473
79 (in isoform 2)Ubiquitination-32.6021890473
79 (in isoform 1)Ubiquitination-32.6021890473
79UbiquitinationVVYTYTGKRIALYIG
EEEEECCCEEEEEEC		32.6027667366
79AcetylationVVYTYTGKRIALYIG
EEEEECCCEEEEEEC		32.6023954790
137PhosphorylationGVGSEASSKKLMDLL
ECCCHHHHHHHHHHH		40.6421712546
138MalonylationVGSEASSKKLMDLLP
CCCHHHHHHHHHHHC		47.6426320211
138AcetylationVGSEASSKKLMDLLP
CCCHHHHHHHHHHHC		47.6425953088
138UbiquitinationVGSEASSKKLMDLLP
CCCHHHHHHHHHHHC		47.6433845483
146UbiquitinationKLMDLLPKRELHGQN
HHHHHHCHHHHCCCC		59.4829967540
157PhosphorylationHGQNPVVTPCNKQFL
CCCCCCCCCCCHHHH		23.5130916345
161 (in isoform 1)Ubiquitination-49.4921890473
161 (in isoform 3)Ubiquitination-49.4921890473
161 (in isoform 2)Ubiquitination-49.4921890473
161AcetylationPVVTPCNKQFLSQFE
CCCCCCCHHHHHHHH		49.4925953088
161UbiquitinationPVVTPCNKQFLSQFE
CCCCCCCHHHHHHHH		49.4927667366
165PhosphorylationPCNKQFLSQFEMQSR
CCCHHHHHHHHHHCC		33.8317525332
169SulfoxidationQFLSQFEMQSRKTTQ
HHHHHHHHHCCCCCC		4.6521406390
174PhosphorylationFEMQSRKTTQSGQMS
HHHHCCCCCCCCCCC		29.0222210691
175PhosphorylationEMQSRKTTQSGQMSG
HHHCCCCCCCCCCCC		24.6322210691
177PhosphorylationQSRKTTQSGQMSGEG
HCCCCCCCCCCCCCC		28.9728111955
180SulfoxidationKTTQSGQMSGEGKAG
CCCCCCCCCCCCCCC		6.7530846556
181PhosphorylationTTQSGQMSGEGKAGP
CCCCCCCCCCCCCCC		26.2922210691
185 (in isoform 2)Ubiquitination-45.9621890473
185UbiquitinationGQMSGEGKAGPPGGS
CCCCCCCCCCCCCCC		45.9627667366
185AcetylationGQMSGEGKAGPPGGS
CCCCCCCCCCCCCCC		45.9625953088
185 (in isoform 1)Ubiquitination-45.9621890473
192PhosphorylationKAGPPGGSSRAAFPQ
CCCCCCCCCCCCCCC		23.6728111955
193PhosphorylationAGPPGGSSRAAFPQG
CCCCCCCCCCCCCCC		29.2528111955
194MethylationGPPGGSSRAAFPQGG
CCCCCCCCCCCCCCC		31.47-
202MethylationAAFPQGGRGRGRFPG
CCCCCCCCCCCCCCC		38.16-
204MethylationFPQGGRGRGRFPGAV
CCCCCCCCCCCCCCC		31.58-
206MethylationQGGRGRGRFPGAVPG
CCCCCCCCCCCCCCC		32.97-
258 (in isoform 2)Phosphorylation-12.2724117733
381PhosphorylationDSRGPPPTDPYGRPP
CCCCCCCCCCCCCCC		56.2128796482
384PhosphorylationGPPPTDPYGRPPPYD
CCCCCCCCCCCCCCC		28.6928796482
390PhosphorylationPYGRPPPYDRGDYGP
CCCCCCCCCCCCCCC		24.8528796482
392MethylationGRPPPYDRGDYGPPG
CCCCCCCCCCCCCCC		33.76-
395PhosphorylationPPYDRGDYGPPGREM
CCCCCCCCCCCCCCC		34.0628796482
404PhosphorylationPPGREMDTARTPLSE
CCCCCCCCCCCCCCH		19.4129255136
407PhosphorylationREMDTARTPLSEAEF
CCCCCCCCCCCHHHH		26.5629255136
410PhosphorylationDTARTPLSEAEFEEI
CCCCCCCCHHHHHHH		35.6423927012
418SulfoxidationEAEFEEIMNRNRAIS
HHHHHHHHHHCHHHC		4.3328183972
425PhosphorylationMNRNRAISSSAISRA
HHHCHHHCHHHHHHH		19.7718452278
426PhosphorylationNRNRAISSSAISRAV
HHCHHHCHHHHHHHH		20.0618452278
427PhosphorylationRNRAISSSAISRAVS
HCHHHCHHHHHHHHH		23.8818452278
430PhosphorylationAISSSAISRAVSDAS
HHCHHHHHHHHHCCC		17.5720860994
434PhosphorylationSAISRAVSDASAGDY
HHHHHHHHCCCCCCH		26.8621406692
437PhosphorylationSRAVSDASAGDYGSA
HHHHHCCCCCCHHHH		37.4621406692
441PhosphorylationSDASAGDYGSAIETL
HCCCCCCHHHHHHHH		16.4421406692
443PhosphorylationASAGDYGSAIETLVT
CCCCCHHHHHHHHHH		21.6121406692
447PhosphorylationDYGSAIETLVTAISL
CHHHHHHHHHHHHHH		22.0321406692
450PhosphorylationSAIETLVTAISLIKQ
HHHHHHHHHHHHHHH		22.7621406692
453PhosphorylationETLVTAISLIKQSKV
HHHHHHHHHHHHCCC		22.9024719451
456UbiquitinationVTAISLIKQSKVSAD
HHHHHHHHHCCCCHH		54.5433845483
459UbiquitinationISLIKQSKVSADDRC
HHHHHHCCCCHHHHH		37.40-
471PhosphorylationDRCKVLISSLQDCLH
HHHHHHHHHHHHHHH		22.3418452278
476GlutathionylationLISSLQDCLHGIESK
HHHHHHHHHHHHHCC		1.6322555962
482PhosphorylationDCLHGIESKSYGSGS
HHHHHHHCCCCCCCC		25.6126074081
483UbiquitinationCLHGIESKSYGSGSR
HHHHHHCCCCCCCCH		34.6021963094
484PhosphorylationLHGIESKSYGSGSRR
HHHHHCCCCCCCCHH		43.9626074081
485PhosphorylationHGIESKSYGSGSRRE
HHHHCCCCCCCCHHH		21.0326074081
487PhosphorylationIESKSYGSGSRRERS
HHCCCCCCCCHHHHH		25.9326074081
489PhosphorylationSKSYGSGSRRERSRE
CCCCCCCCHHHHHHH		29.8426074081
493UbiquitinationGSGSRRERSRERDHS
CCCCHHHHHHHHHHH		38.9233845483
494PhosphorylationSGSRRERSRERDHSR
CCCHHHHHHHHHHHH		33.4730916345
500PhosphorylationRSRERDHSRSREKSR
HHHHHHHHHHHHHHH		35.9230916345
502PhosphorylationRERDHSRSREKSRRH
HHHHHHHHHHHHHHH		48.0533259812
511PhosphorylationEKSRRHKSRSRDRHD
HHHHHHHHHHHHHHH		29.3930916345
513PhosphorylationSRRHKSRSRDRHDDY
HHHHHHHHHHHHHHH		45.7023401153
520PhosphorylationSRDRHDDYYRERSRE
HHHHHHHHHHHHHHH		15.5229449344
520UbiquitinationSRDRHDDYYRERSRE
HHHHHHHHHHHHHHH		15.5221963094
521PhosphorylationRDRHDDYYRERSRER
HHHHHHHHHHHHHHH		17.0029214152
525PhosphorylationDDYYRERSRERERHR
HHHHHHHHHHHHHHH		33.4730916345
539PhosphorylationRDRDRDRDRERDRER
HHHHHHHHHHHHHHH		62.1733259812
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
-KUbiquitinationE3 ubiquitin ligaseITCHQ96J02
PMID:16055720
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CPSF6_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 CPSF6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GIN1_HUMANGIN1physical
16189514
WWP1_HUMANWWP1physical
16189514
ARMC7_HUMANARMC7physical
16189514
KLH12_HUMANKLHL12physical
16189514
WWP2_HUMANWWP2physical
16189514
ITCH_HUMANITCHphysical
16055720
U2AF2_HUMANU2AF2physical
22939629
UBP2L_HUMANUBAP2Lphysical
22939629
NONO_HUMANNONOphysical
22939629
WBP11_HUMANWBP11physical
22939629
CPSF7_HUMANCPSF7physical
22939629
PUF60_HUMANPUF60physical
22939629
CSTF2_HUMANCSTF2physical
22939629
RPB9_HUMANPOLR2Iphysical
22939629
NUP88_HUMANNUP88physical
22939629
TCEA2_HUMANTCEA2physical
22939629
ZBT8B_HUMANZBTB8Bphysical
22939629
KC1A_HUMANCSNK1A1physical
22939629
SAFB1_HUMANSAFBphysical
22939629
MAX_HUMANMAXphysical
22939629
STRN_HUMANSTRNphysical
22939629
TBD2A_HUMANTBC1D2physical
22939629
TITIN_HUMANTTNphysical
22939629
NU107_HUMANNUP107physical
22939629
WWP1_HUMANWWP1physical
19447967
FXR2_HUMANFXR2physical
24778252
PPIL1_HUMANPPIL1physical
25416956
TOLIP_HUMANTOLLIPphysical
25416956
OTUB2_HUMANOTUB2physical
25416956
ARMC7_HUMANARMC7physical
25416956
CPSF5_HUMANNUDT21physical
26344197
PCF11_HUMANPCF11physical
26344197
SMRC1_HUMANSMARCC1physical
26344197
SMRC2_HUMANSMARCC2physical
26344197
P4R3A_HUMANSMEK1physical
26344197
CPSF7_HUMANCPSF7physical
28514442
ITCH_HUMANITCHphysical
28514442
WWP1_HUMANWWP1physical
28514442
RBBP6_HUMANRBBP6physical
28514442
CPSF5_HUMANNUDT21physical
28514442
TRAP1_HUMANTRAP1physical
27173435
SND1_HUMANSND1physical
27173435
GAG_HV1H2gagphysical
27107820
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 CPSF6_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-165, AND MASSSPECTROMETRY.
"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 THR-407, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory