FAF1_HUMAN - dbPTM
FAF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FAF1_HUMAN
UniProt AC Q9UNN5
Protein Name FAS-associated factor 1
Gene Name FAF1
Organism Homo sapiens (Human).
Sequence Length 650
Subcellular Localization Nucleus .
Protein Description Ubiquitin-binding protein. [PubMed: 19722279 Required for the progression of DNA replication forks by targeting DNA replication licensing factor CDT1 for degradation]
Protein Sequence MASNMDREMILADFQACTGIENIDEAITLLEQNNWDLVAAINGVIPQENGILQSEYGGETIPGPAFNPASHPASAPTSSSSSAFRPVMPSRQIVERQPRMLDFRVEYRDRNVDVVLEDTCTVGEIKQILENELQIPVSKMLLKGWKTGDVEDSTVLKSLHLPKNNSLYVLTPDLPPPSSSSHAGALQESLNQNFMLIITHREVQREYNLNFSGSSTIQEVKRNVYDLTSIPVRHQLWEGWPTSATDDSMCLAESGLSYPCHRLTVGRRSSPAQTREQSEEQITDVHMVSDSDGDDFEDATEFGVDDGEVFGMASSALRKSPMMPENAENEGDALLQFTAEFSSRYGDCHPVFFIGSLEAAFQEAFYVKARDRKLLAIYLHHDESVLTNVFCSQMLCAESIVSYLSQNFITWAWDLTKDSNRARFLTMCNRHFGSVVAQTIRTQKTDQFPLFLIIMGKRSSNEVLNVIQGNTTVDELMMRLMAAMEIFTAQQQEDIKDEDEREARENVKREQDEAYRLSLEADRAKREAHEREMAEQFRLEQIRKEQEEEREAIRLSLEQALPPEPKEENAEPVSKLRIRTPSGEFLERRFLASNKLQIVFDFVASKGFPWDEYKLLSTFPRRDVTQLDPNKSLLEVKLFPQETLFLEAKE
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
30UbiquitinationIDEAITLLEQNNWDL
HHHHHHHHHHCCHHH
4.8123000965
34UbiquitinationITLLEQNNWDLVAAI
HHHHHHCCHHHHHHH
33.0821890473
37UbiquitinationLEQNNWDLVAAINGV
HHHCCHHHHHHHCCC
1.8223000965
48UbiquitinationINGVIPQENGILQSE
HCCCCCCCCCCEEEC
52.6623000965
54UbiquitinationQENGILQSEYGGETI
CCCCCEEECCCCCCC
29.3723000965
70O-linked_GlycosylationGPAFNPASHPASAPT
CCCCCCCCCCCCCCC
31.1223301498
80O-linked_GlycosylationASAPTSSSSSAFRPV
CCCCCCCCCCCCCCC
28.2523301498
112UbiquitinationVEYRDRNVDVVLEDT
EEECCCCCCEEEECC
6.5221890473
120GlutathionylationDVVLEDTCTVGEIKQ
CEEEECCCCHHHHHH
4.4922555962
138PhosphorylationNELQIPVSKMLLKGW
CCCCCCHHHHHHCCC
13.6430622161
139 (in isoform 1)Ubiquitination-33.5321890473
139 (in isoform 2)Ubiquitination-33.5321890473
139UbiquitinationELQIPVSKMLLKGWK
CCCCCHHHHHHCCCC
33.5321890473
139UbiquitinationELQIPVSKMLLKGWK
CCCCCHHHHHHCCCC
33.5323000965
143 (in isoform 1)Ubiquitination-59.7821890473
143 (in isoform 2)Ubiquitination-59.7821890473
143UbiquitinationPVSKMLLKGWKTGDV
CHHHHHHCCCCCCCC
59.7823000965
143UbiquitinationPVSKMLLKGWKTGDV
CHHHHHHCCCCCCCC
59.7821890473
143AcetylationPVSKMLLKGWKTGDV
CHHHHHHCCCCCCCC
59.7825953088
146UbiquitinationKMLLKGWKTGDVEDS
HHHHCCCCCCCCCCC
51.8321890473
146UbiquitinationKMLLKGWKTGDVEDS
HHHHCCCCCCCCCCC
51.8323000965
146AcetylationKMLLKGWKTGDVEDS
HHHHCCCCCCCCCCC
51.8319819239
146 (in isoform 1)Ubiquitination-51.8321890473
146 (in isoform 2)Ubiquitination-51.8321890473
147PhosphorylationMLLKGWKTGDVEDST
HHHCCCCCCCCCCCC
31.9120068231
153PhosphorylationKTGDVEDSTVLKSLH
CCCCCCCCCCCEEEE
13.6020068231
154PhosphorylationTGDVEDSTVLKSLHL
CCCCCCCCCCEEEEC
42.0320068231
157 (in isoform 1)Ubiquitination-46.7821890473
157MalonylationVEDSTVLKSLHLPKN
CCCCCCCEEEECCCC
46.7826320211
157AcetylationVEDSTVLKSLHLPKN
CCCCCCCEEEECCCC
46.7825953088
157UbiquitinationVEDSTVLKSLHLPKN
CCCCCCCEEEECCCC
46.7823000965
157UbiquitinationVEDSTVLKSLHLPKN
CCCCCCCEEEECCCC
46.7821890473
157 (in isoform 2)Ubiquitination-46.7821890473
163UbiquitinationLKSLHLPKNNSLYVL
CEEEECCCCCEEEEE
75.1123000965
207PhosphorylationHREVQREYNLNFSGS
EHHHHHHHCCCCCCC
27.4329083192
212PhosphorylationREYNLNFSGSSTIQE
HHHCCCCCCCHHHHH
36.3725693802
214PhosphorylationYNLNFSGSSTIQEVK
HCCCCCCCHHHHHHH
24.1025693802
215PhosphorylationNLNFSGSSTIQEVKR
CCCCCCCHHHHHHHH
32.8125693802
216PhosphorylationLNFSGSSTIQEVKRN
CCCCCCHHHHHHHHH
28.5125693802
221 (in isoform 1)Ubiquitination-37.1921890473
221UbiquitinationSSTIQEVKRNVYDLT
CHHHHHHHHHHCCCC
37.1921890473
221UbiquitinationSSTIQEVKRNVYDLT
CHHHHHHHHHHCCCC
37.1921963094
225PhosphorylationQEVKRNVYDLTSIPV
HHHHHHHCCCCCCCC
14.5828152594
264PhosphorylationSYPCHRLTVGRRSSP
CCCCEEECCCCCCCC
22.3721712546
269PhosphorylationRLTVGRRSSPAQTRE
EECCCCCCCCCHHHH
39.0320068231
270PhosphorylationLTVGRRSSPAQTREQ
ECCCCCCCCCHHHHC
23.5728176443
274PhosphorylationRRSSPAQTREQSEEQ
CCCCCCHHHHCCHHH
37.9820068231
289PhosphorylationITDVHMVSDSDGDDF
CCEEEEEECCCCCCH
24.6711713579
291PhosphorylationDVHMVSDSDGDDFED
EEEEEECCCCCCHHH
35.6711713579
292 (in isoform 2)Ubiquitination-70.3221890473
305 (in isoform 2)Ubiquitination-59.5921890473
314PhosphorylationGEVFGMASSALRKSP
HHHEEECCHHHHCCC
13.7826074081
315PhosphorylationEVFGMASSALRKSPM
HHEEECCHHHHCCCC
23.0626074081
319UbiquitinationMASSALRKSPMMPEN
ECCHHHHCCCCCCCC
60.81-
320PhosphorylationASSALRKSPMMPENA
CCHHHHCCCCCCCCC
16.1730278072
335UbiquitinationENEGDALLQFTAEFS
CCCCCHHHHHHHHHH
4.1622817900
342PhosphorylationLQFTAEFSSRYGDCH
HHHHHHHHHHHCCCE
12.86-
343PhosphorylationQFTAEFSSRYGDCHP
HHHHHHHHHHCCCEE
34.54-
348UbiquitinationFSSRYGDCHPVFFIG
HHHHHCCCEEEEEEE
3.2022053931
434PhosphorylationMCNRHFGSVVAQTIR
HHHHHHHHHHHHHHH
16.6924043423
439PhosphorylationFGSVVAQTIRTQKTD
HHHHHHHHHHCCCCC
11.5924043423
442PhosphorylationVVAQTIRTQKTDQFP
HHHHHHHCCCCCCCC
30.4824043423
444 (in isoform 1)Ubiquitination-54.1521890473
444UbiquitinationAQTIRTQKTDQFPLF
HHHHHCCCCCCCCEE
54.1521906983
445PhosphorylationQTIRTQKTDQFPLFL
HHHHCCCCCCCCEEE
25.8024043423
457UbiquitinationLFLIIMGKRSSNEVL
EEEEEEECCCHHHHH
31.5520639865
457 (in isoform 1)Ubiquitination-31.5521890473
496UbiquitinationAQQQEDIKDEDEREA
HHHHHHCCCHHHHHH
68.3429901268
508SumoylationREARENVKREQDEAY
HHHHHHHHHHHHHHH
62.90-
518PhosphorylationQDEAYRLSLEADRAK
HHHHHHHHHHHHHHH
18.3728555341
544UbiquitinationFRLEQIRKEQEEERE
HCHHHHHHHHHHHHH
66.43-
556PhosphorylationEREAIRLSLEQALPP
HHHHHHHHHHHHCCC
21.7325159151
566UbiquitinationQALPPEPKEENAEPV
HHCCCCCCCCCCCCC
75.8124816145
575UbiquitinationENAEPVSKLRIRTPS
CCCCCCCCCEEECCC
41.8629901268
580PhosphorylationVSKLRIRTPSGEFLE
CCCCEEECCCHHHHH
21.3123401153
582PhosphorylationKLRIRTPSGEFLERR
CCEEECCCHHHHHHH
50.7919664994
631UbiquitinationVTQLDPNKSLLEVKL
CCCCCCCCCCEEEEE
48.1229967540
637UbiquitinationNKSLLEVKLFPQETL
CCCCEEEEECCCCCE
34.7332015554

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
289SPhosphorylationKinaseAURKAO14965
GPS
289SPhosphorylationKinaseCSNK2A1P68400
GPS
289SPhosphorylationKinaseCK2-FAMILY-GPS
289SPhosphorylationKinaseCK2_GROUP-PhosphoELM
291SPhosphorylationKinaseAURKAO14965
GPS
291SPhosphorylationKinaseCSNK2A1P68400
GPS
291SPhosphorylationKinaseCK2-FAMILY-GPS
291SPhosphorylationKinaseCK2_GROUP-PhosphoELM
556SPhosphorylationKinaseIKKEQ14164
PSP
582SPhosphorylationKinaseAKT1P31749
PSP
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:23307929

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FAF1_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 FAF1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
21411632
TERA_HUMANVCPphysical
18775313
NPL4_HUMANNPLOC4physical
18775313
UFD1_HUMANUFD1Lphysical
18775313
CUL1_HUMANCUL1physical
18775313
CUL2_HUMANCUL2physical
18775313
CUL3_HUMANCUL3physical
18775313
UBR1_HUMANUBR1physical
18775313
HIF1A_HUMANHIF1Aphysical
18775313
PPB1_HUMANALPPphysical
18775313
VCIP1_HUMANVCPIP1physical
18775313
SKP1_HUMANSKP1physical
18775313
FBW1B_HUMANFBXW11physical
18775313
KLH22_HUMANKLHL22physical
18775313
KBTB7_HUMANKBTBD7physical
18775313
WDR26_HUMANWDR26physical
18775313
AMFR_HUMANAMFRphysical
18775313
UBR2_HUMANUBR2physical
18775313
UBR4_HUMANUBR4physical
18775313
PJA2_HUMANPJA2physical
18775313
NPL4_HUMANNPLOC4physical
21914798
TERA_HUMANVCPphysical
21914798
UFD1_HUMANUFD1Lphysical
21914798
FBW1A_HUMANBTRCphysical
22730322
CUL1_HUMANCUL1physical
22730322
SKP1_HUMANSKP1physical
22730322
TNR6_HUMANFASphysical
10462485
TERA_HUMANVCPphysical
15743842
UBC_HUMANUBCphysical
15743842
HSP74_HUMANHSPA4physical
22876279
TERA_HUMANVCPphysical
21645854
UBC_HUMANUBCphysical
19722279
TF65_HUMANRELAphysical
14600157
HSP7C_HUMANHSPA8physical
15596450
HSP74_HUMANHSPA4physical
15596450
FADD_HUMANFADDphysical
12702723
IKKB_HUMANIKBKBphysical
17684021
NLRP3_HUMANNLRP3physical
17046979
TERA_HUMANVCPphysical
22350894
TERA_HUMANVCPphysical
23293021
UBC_HUMANUBCphysical
23293021
HSP74_HUMANHSPA4physical
23293021
NPL4_HUMANNPLOC4physical
23293021
UFD1_HUMANUFD1Lphysical
23293021
CARM1_HUMANCARM1physical
22863883
SYCC_HUMANCARSphysical
22863883
NXP20_HUMANFAM114A1physical
22863883
SYFB_HUMANFARSBphysical
22863883
PUR2_HUMANGARTphysical
22863883
HIRP3_HUMANHIRIP3physical
22863883
HSP74_HUMANHSPA4physical
22863883
HS105_HUMANHSPH1physical
22863883
ILK_HUMANILKphysical
22863883
PLOD2_HUMANPLOD2physical
22863883
PPM1G_HUMANPPM1Gphysical
22863883
2A5G_HUMANPPP2R5Cphysical
22863883
ANM3_HUMANPRMT3physical
22863883
PUF60_HUMANPUF60physical
22863883
RANB3_HUMANRANBP3physical
22863883
RL24_HUMANRPL24physical
22863883
SAMH1_HUMANSAMHD1physical
22863883
SC23A_HUMANSEC23Aphysical
22863883
SET_HUMANSETphysical
22863883
SF01_HUMANSF1physical
22863883
SWP70_HUMANSWAP70physical
22863883
TLN1_HUMANTLN1physical
22863883
RO60_HUMANTROVE2physical
22863883
UGPA_HUMANUGP2physical
22863883
XPO7_HUMANXPO7physical
22863883
VAPA_HUMANVAPAphysical
24885147
VAPB_HUMANVAPBphysical
24885147
TERA_HUMANVCPphysical
24885147
UBC_HUMANUBCphysical
24885147
UBL4A_HUMANUBL4Aphysical
24885147
ASNA_HUMANASNA1physical
24885147
GET4_HUMANGET4physical
24885147
BAG6_HUMANBAG6physical
24885147
RPN2_HUMANRPN2physical
24885147
OST48_HUMANDDOSTphysical
24885147
FAF1_HUMANFAF1physical
23720822
UBC_HUMANUBCphysical
18775313
CTNB1_HUMANCTNNB1physical
22730322
UBC_HUMANUBCphysical
22876279
CDT1_HUMANCDT1physical
26842564
TERA_HUMANVCPphysical
26842564
CTNB1_HUMANCTNNB1physical
26456834
IPO5_HUMANIPO5physical
26811330
WDR24_HUMANWDR24physical
26389662
YTHD1_HUMANYTHDF1physical
26389662
RAE1L_HUMANRAE1physical
26389662
VAPA_HUMANVAPAphysical
26389662
TERA_HUMANVCPphysical
26389662
NPL4_HUMANNPLOC4physical
26389662
UFD1_HUMANUFD1Lphysical
26389662
BACD3_HUMANKCTD10physical
26389662
VAPB_HUMANVAPBphysical
26389662
YTHD3_HUMANYTHDF3physical
26389662
WDR59_HUMANWDR59physical
26389662
MMAB_HUMANMMABphysical
26389662
NUP98_HUMANNUP98physical
26389662
MYCB2_HUMANMYCBP2physical
26389662
UBP11_HUMANUSP11physical
26389662
ASPC1_HUMANASPSCR1physical
26389662
HSP72_HUMANHSPA2physical
26389662
MIO_HUMANMIOSphysical
26389662
UBXN6_HUMANUBXN6physical
26389662
BTBD9_HUMANBTBD9physical
26389662
BACD1_HUMANKCTD13physical
26389662
BACD2_HUMANTNFAIP1physical
26389662
UBXN7_HUMANUBXN7physical
26389662
CASP8_HUMANCASP8physical
28414080
TF65_HUMANRELAphysical
28414080

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 FAF1_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-320 AND SER-582, ANDMASS 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-320, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-225, AND MASSSPECTROMETRY.

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