SSF1_HUMAN - dbPTM
SSF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SSF1_HUMAN
UniProt AC Q9NQ55
Protein Name Suppressor of SWI4 1 homolog
Gene Name PPAN
Organism Homo sapiens (Human).
Sequence Length 473
Subcellular Localization Nucleus, nucleolus .
Protein Description May have a role in cell growth..
Protein Sequence MGQSGRSRHQKRARAQAQLRNLEAYAANPHSFVFTRGCTGRNIRQLSLDVRRVMEPLTASRLQVRKKNSLKDCVAVAGPLGVTHFLILSKTETNVYFKLMRLPGGPTLTFQVKKYSLVRDVVSSLRRHRMHEQQFAHPPLLVLNSFGPHGMHVKLMATMFQNLFPSINVHKVNLNTIKRCLLIDYNPDSQELDFRHYSIKVVPVGASRGMKKLLQEKFPNMSRLQDISELLATGAGLSESEAEPDGDHNITELPQAVAGRGNMRAQQSAVRLTEIGPRMTLQLIKVQEGVGEGKVMFHSFVSKTEEELQAILEAKEKKLRLKAQRQAQQAQNVQRKQEQREAHRKKSLEGMKKARVGGSDEEASGIPSRTASLELGEDDDEQEDDDIEYFCQAVGEAPSEDLFPEAKQKRLAKSPGRKRKRWEMDRGRGRLCDQKFPKTKDKSQGAQARRGPRGASRDGGRGRGRGRPGKRVA
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
25PhosphorylationQLRNLEAYAANPHSF
HHHCHHHHHCCCCCE		9.2528152594
31PhosphorylationAYAANPHSFVFTRGC
HHHCCCCCEEEECCC		25.1028152594
35PhosphorylationNPHSFVFTRGCTGRN
CCCCEEEECCCCCCC		22.3528152594
36MethylationPHSFVFTRGCTGRNI
CCCEEEECCCCCCCH		27.07115917877
39PhosphorylationFVFTRGCTGRNIRQL
EEEECCCCCCCHHHH		41.8420860994
41MethylationFTRGCTGRNIRQLSL
EECCCCCCCHHHHCC		19.76115917881
45UbiquitinationCTGRNIRQLSLDVRR
CCCCCHHHHCCHHHH		31.4421890473
54SulfoxidationSLDVRRVMEPLTASR
CCHHHHHHCHHHHHH		4.1021406390
98UbiquitinationTETNVYFKLMRLPGG
CCCCEEEEEEECCCC		24.5621890473
98 (in isoform 2)Ubiquitination-24.5621890473
98AcetylationTETNVYFKLMRLPGG
CCCCEEEEEEECCCC		24.5626051181
98 (in isoform 1)Ubiquitination-24.5621890473
98UbiquitinationTETNVYFKLMRLPGG
CCCCEEEEEEECCCC		24.5621890473
123PhosphorylationSLVRDVVSSLRRHRM
HHHHHHHHHHHHHHH		24.4124719451
124PhosphorylationLVRDVVSSLRRHRMH
HHHHHHHHHHHHHHH		17.8124719451
158UbiquitinationMHVKLMATMFQNLFP
HHHHHHHHHHHHHCC		12.4523000965
159UbiquitinationHVKLMATMFQNLFPS
HHHHHHHHHHHHCCC		2.0621890473
164UbiquitinationATMFQNLFPSINVHK
HHHHHHHCCCCCEEE		6.1423000965
178UbiquitinationKVNLNTIKRCLLIDY
ECCHHHCCCEEEEEC		34.71-
178AcetylationKVNLNTIKRCLLIDY
ECCHHHCCCEEEEEC		34.7126051181
198PhosphorylationELDFRHYSIKVVPVG
CCCCCEEEEEEEECC		15.1424719451
200UbiquitinationDFRHYSIKVVPVGAS
CCCEEEEEEEECCCC		31.10-
210UbiquitinationPVGASRGMKKLLQEK
ECCCCHHHHHHHHHH		3.1723000965
211UbiquitinationVGASRGMKKLLQEKF
CCCCHHHHHHHHHHC		42.9921890473
212UbiquitinationGASRGMKKLLQEKFP
CCCHHHHHHHHHHCC		45.6023000965
212 (in isoform 1)Ubiquitination-45.6021890473
212 (in isoform 2)Ubiquitination-45.6021890473
212UbiquitinationGASRGMKKLLQEKFP
CCCHHHHHHHHHHCC		45.6021890473
216UbiquitinationGMKKLLQEKFPNMSR
HHHHHHHHHCCCCHH		57.5423000965
217 (in isoform 2)Ubiquitination-53.8421890473
217UbiquitinationMKKLLQEKFPNMSRL
HHHHHHHHCCCCHHH		53.8421890473
217 (in isoform 1)Ubiquitination-53.8421890473
217AcetylationMKKLLQEKFPNMSRL
HHHHHHHHCCCCHHH		53.8426051181
217UbiquitinationMKKLLQEKFPNMSRL
HHHHHHHHCCCCHHH		53.8423000965
228PhosphorylationMSRLQDISELLATGA
CHHHHHHHHHHHHCC		30.4030278072
233PhosphorylationDISELLATGAGLSES
HHHHHHHHCCCCCHH		27.7726503892
238PhosphorylationLATGAGLSESEAEPD
HHHCCCCCHHHCCCC		37.8525159151
240PhosphorylationTGAGLSESEAEPDGD
HCCCCCHHHCCCCCC		38.4430175587
241UbiquitinationGAGLSESEAEPDGDH
CCCCCHHHCCCCCCC		53.6629967540
251PhosphorylationPDGDHNITELPQAVA
CCCCCCCCHHCHHHH		36.4721955146
262UbiquitinationQAVAGRGNMRAQQSA
HHHHCCCCHHHHHHC		18.5329967540
268PhosphorylationGNMRAQQSAVRLTEI
CCHHHHHHCHHHHCC		19.36-
278MethylationRLTEIGPRMTLQLIK
HHHCCCCCCEEEEEE		26.04115917873
293UbiquitinationVQEGVGEGKVMFHSF
EECCCCCCEEEEEEC		23.1729967540
294UbiquitinationQEGVGEGKVMFHSFV
ECCCCCCEEEEEECC		26.6529967540
300UbiquitinationGKVMFHSFVSKTEEE
CEEEEEECCCCCHHH		5.5924816145
306PhosphorylationSFVSKTEEELQAILE
ECCCCCHHHHHHHHH		70.0532142685
314UbiquitinationELQAILEAKEKKLRL
HHHHHHHHHHHHHHH		23.1229967540
315UbiquitinationLQAILEAKEKKLRLK
HHHHHHHHHHHHHHH		61.7729967540
315AcetylationLQAILEAKEKKLRLK
HHHHHHHHHHHHHHH		61.7726051181
317UbiquitinationAILEAKEKKLRLKAQ
HHHHHHHHHHHHHHH		57.30-
347PhosphorylationREAHRKKSLEGMKKA
HHHHHHHHHHHHHHH		34.3921815630
352UbiquitinationKKSLEGMKKARVGGS
HHHHHHHHHHCCCCC		54.8824816145
352AcetylationKKSLEGMKKARVGGS
HHHHHHHHHHCCCCC		54.8825953088
353UbiquitinationKSLEGMKKARVGGSD
HHHHHHHHHCCCCCH		32.3124816145
358PhosphorylationMKKARVGGSDEEASG
HHHHCCCCCHHHHCC		29.1232142685
359PhosphorylationKKARVGGSDEEASGI
HHHCCCCCHHHHCCC		35.6019664994
364PhosphorylationGGSDEEASGIPSRTA
CCCHHHHCCCCCCCE		40.3022167270
368PhosphorylationEEASGIPSRTASLEL
HHHCCCCCCCEEEEC		40.1022167270
370PhosphorylationASGIPSRTASLELGE
HCCCCCCCEEEECCC		25.5718669648
372PhosphorylationGIPSRTASLELGEDD
CCCCCCEEEECCCCC		23.0526074081
382UbiquitinationLGEDDDEQEDDDIEY
CCCCCCCCCCCCHHH		67.4333845483
387UbiquitinationDEQEDDDIEYFCQAV
CCCCCCCHHHHHHHH		6.2624816145
399PhosphorylationQAVGEAPSEDLFPEA
HHHCCCCHHHCCHHH		51.2827499020
414PhosphorylationKQKRLAKSPGRKRKR
HHHHHHCCCCCCHHH		27.2924732914
426MethylationRKRWEMDRGRGRLCD
HHHCCCCCCCCCCCC		35.0854563439
428MethylationRWEMDRGRGRLCDQK
HCCCCCCCCCCCCCC		28.1431341467
430MethylationEMDRGRGRLCDQKFP
CCCCCCCCCCCCCCC		30.68115917885
434UbiquitinationGRGRLCDQKFPKTKD
CCCCCCCCCCCCCCC		48.5733845483
435UbiquitinationRGRLCDQKFPKTKDK
CCCCCCCCCCCCCCH		50.8433845483
435AcetylationRGRLCDQKFPKTKDK
CCCCCCCCCCCCCCH		50.8425825284
438AcetylationLCDQKFPKTKDKSQG
CCCCCCCCCCCHHHH		71.93-
439UbiquitinationCDQKFPKTKDKSQGA
CCCCCCCCCCHHHHC		44.7224816145
440UbiquitinationDQKFPKTKDKSQGAQ
CCCCCCCCCHHHHCH		70.1024816145
453MethylationAQARRGPRGASRDGG
CHHHCCCCCCCCCCC		57.0154563443
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 SSF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SSF1_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 SSF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
YBOX2_HUMANYBX2physical
28514442
H12_HUMANHIST1H1Cphysical
28514442
DIEXF_HUMANDIEXFphysical
28514442
ZCHC7_HUMANZCCHC7physical
28514442
PK1IP_HUMANPAK1IP1physical
28514442
ZN496_HUMANZNF496physical
28514442
PAPD5_HUMANPAPD5physical
28514442
ZN184_HUMANZNF184physical
28514442
Z354A_HUMANZNF354Aphysical
28514442
RRP15_HUMANRRP15physical
28514442
I20L2_HUMANISG20L2physical
28514442
ZNF16_HUMANZNF16physical
28514442
ZN317_HUMANZNF317physical
28514442
RT35_HUMANMRPS35physical
28514442
GZF1_HUMANGZF1physical
28514442
REXO4_HUMANREXO4physical
28514442
ZBT24_HUMANZBTB24physical
28514442
DDX56_HUMANDDX56physical
28514442
RRP8_HUMANRRP8physical
28514442
RL37A_HUMANRPL37Aphysical
28514442
ZN644_HUMANZNF644physical
28514442
NOG2_HUMANGNL2physical
28514442
RB_HUMANRB1physical
28514442
PRD10_HUMANPRDM10physical
28514442
PPM1G_HUMANPPM1Gphysical
28514442
STAU2_HUMANSTAU2physical
28514442
ZNF22_HUMANZNF22physical
28514442
ZN770_HUMANZNF770physical
28514442
LARP1_HUMANLARP1physical
28514442
RLP24_HUMANRSL24D1physical
28514442
ZFP62_HUMANZFP62physical
28514442
U3IP2_HUMANRRP9physical
28514442
NOG1_HUMANGTPBP4physical
28514442
KNOP1_HUMANKNOP1physical
28514442
DDX24_HUMANDDX24physical
28514442
DKC1_HUMANDKC1physical
28514442
RS3A_HUMANRPS3Aphysical
28514442
STAU1_HUMANSTAU1physical
28514442
BRX1_HUMANBRIX1physical
28514442
GLYR1_HUMANGLYR1physical
28514442
KRR1_HUMANKRR1physical
28514442
ZN771_HUMANZNF771physical
28514442
DHX30_HUMANDHX30physical
28514442
RM13_HUMANMRPL13physical
28514442
RT31_HUMANMRPS31physical
28514442
TCF25_HUMANTCF25physical
28514442
PUM3_HUMANKIAA0020physical
28514442
NVL_HUMANNVLphysical
28514442
RL3_HUMANRPL3physical
28514442
RL26L_HUMANRPL26L1physical
28514442
YBOX3_HUMANYBX3physical
28514442
DDX27_HUMANDDX27physical
28514442
NOL10_HUMANNOL10physical
28514442
ZSC25_HUMANZSCAN25physical
28514442
IF2B3_HUMANIGF2BP3physical
28514442
STRBP_HUMANSTRBPphysical
28514442
NMNA1_HUMANNMNAT1physical
28514442
SF3B1_HUMANSF3B1physical
28514442
NUFP1_HUMANNUFIP1physical
28514442
RT23_HUMANMRPS23physical
28514442
UBR5_HUMANUBR5physical
28514442
RENT1_HUMANUPF1physical
28514442
RS13_HUMANRPS13physical
28514442
NGRN_HUMANNGRNphysical
28514442
ZN574_HUMANZNF574physical
28514442
RM03_HUMANMRPL3physical
28514442
MOV10_HUMANMOV10physical
28514442
TRBP2_HUMANTARBP2physical
28514442
DDX54_HUMANDDX54physical
28514442
MDM2_HUMANMDM2physical
28514442
GNL3_HUMANGNL3physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SSF1_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-238; SER-240 ANDSER-359, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASSSPECTROMETRY.
"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-359, 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-238; SER-240 ANDSER-359, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, 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 SER-238; SER-240 ANDSER-359, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359; SER-364 ANDSER-372, AND MASS SPECTROMETRY.
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline.";
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
Electrophoresis 28:2027-2034(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASSSPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, 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-238; SER-240 ANDSER-359, AND MASS SPECTROMETRY.
"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-359, AND MASSSPECTROMETRY.

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