F169A_HUMAN - dbPTM
F169A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID F169A_HUMAN
UniProt AC Q9Y6X4
Protein Name Soluble lamin-associated protein of 75 kDa
Gene Name FAM169A
Organism Homo sapiens (Human).
Sequence Length 670
Subcellular Localization Nucleus envelope . Nucleus inner membrane
Peripheral membrane protein
Nucleoplasmic side . Enriched at the nuclear lamina.
Protein Description
Protein Sequence MAFPVDMLENCSHEELENSAEDYMSDLRCGDPENPECFSLLNITIPISLSNVGFVPLYGGDQTQKILALFAPEDSLTAVALYLADQWWAIDDIVKTSVPSREGLKQVSTLGERVVLYVLNRIIYRKQEMERNEIPFLCHSSTDYAKILWKKGEAIGFYSVKPTGSICASFLTQSYQLPVLDTMFLRKKYRGKDFGLHMLEDFVDSFTEDALGLRYPLSSLMYTACKQYFEKYPGDHELLWEVEGVGHWYQRIPVTRALQREALKILALSQNEPKRPMSGEYGPASVPEYEARTEDNQSSEMQLTIDSLKDAFASTSEGHDKTSVSTHTRSGNLKRPKIGKRFQDSEFSSSQGEDEKTSQTSLTASINKLESTARPSESSEEFLEEEPEQRGIEFEDESSDRDARPALETQPQQEKQDGEKESELEPMNGEIMDDSLKTSLITEEEDSTSEVLDEELKLQPFNSSEDSTNLVPLVVESSKPPEVDAPDKTPRIPDSEMLMDEGTSDEKGHMEEKLSLLPRKKAHLGSSDNVATMSNEERSDGGFPNSVIAEFSEEPVSENLSPNTTSSLEDQGEEGVSEPQETSTALPQSSLIEVELEDVPFSQNAGQKNQSEEQSEASSEQLDQFTQSAEKAVDSSSEEIEVEVPVVDRRNLRRKAKGHKGPAKKKAKLT
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
44UbiquitinationCFSLLNITIPISLSN
HHHCCEEEEEEEHHH		21.4532015554
117PhosphorylationLGERVVLYVLNRIIY
HHHHHHHHHHHHHHH		7.41-
127UbiquitinationNRIIYRKQEMERNEI
HHHHHHHHHHHHCCC		46.3932015554
139UbiquitinationNEIPFLCHSSTDYAK
CCCCCEEECCCCHHH		27.2533845483
140PhosphorylationEIPFLCHSSTDYAKI
CCCCEEECCCCHHHH		33.6629083192
140UbiquitinationEIPFLCHSSTDYAKI
CCCCEEECCCCHHHH		33.6621890473
141PhosphorylationIPFLCHSSTDYAKIL
CCCEEECCCCHHHHH		11.1329083192
142PhosphorylationPFLCHSSTDYAKILW
CCEEECCCCHHHHHH		35.7229083192
144PhosphorylationLCHSSTDYAKILWKK
EEECCCCHHHHHHHC		15.1929083192
145UbiquitinationCHSSTDYAKILWKKG
EECCCCHHHHHHHCC		8.6722817900
189PhosphorylationTMFLRKKYRGKDFGL
HHHHCHHHCCCCCCH		27.8622798277
202UbiquitinationGLHMLEDFVDSFTED
CHHHHHHHHHHCCHH		4.8621890473
207UbiquitinationEDFVDSFTEDALGLR
HHHHHHCCHHHHCCC		36.5922817900
215PhosphorylationEDALGLRYPLSSLMY
HHHHCCCCCHHHHHH		17.36-
223UbiquitinationPLSSLMYTACKQYFE
CHHHHHHHHHHHHHH		16.1822817900
226UbiquitinationSLMYTACKQYFEKYP
HHHHHHHHHHHHHCC		45.6422817900
226 (in isoform 1)Ubiquitination-45.6421890473
231UbiquitinationACKQYFEKYPGDHEL
HHHHHHHHCCCCCEE		47.0122817900
235UbiquitinationYFEKYPGDHELLWEV
HHHHCCCCCEEEEEE		27.8133845483
278PhosphorylationNEPKRPMSGEYGPAS
CCCCCCCCCCCCCCC		31.0228348404
281PhosphorylationKRPMSGEYGPASVPE
CCCCCCCCCCCCCCC		31.7530108239
285PhosphorylationSGEYGPASVPEYEAR
CCCCCCCCCCCCEEC		41.1429978859
285UbiquitinationSGEYGPASVPEYEAR
CCCCCCCCCCCCEEC		41.1422817900
289PhosphorylationGPASVPEYEARTEDN
CCCCCCCCEECCCCC		14.6027732954
293PhosphorylationVPEYEARTEDNQSSE
CCCCEECCCCCCCCE		55.5323879269
298PhosphorylationARTEDNQSSEMQLTI
ECCCCCCCCEEEEEH		34.2222817901
299PhosphorylationRTEDNQSSEMQLTID
CCCCCCCCEEEEEHH		27.5928348404
309 (in isoform 1)Ubiquitination-51.4621890473
309UbiquitinationQLTIDSLKDAFASTS
EEEHHHHHHHHHHCC		51.4622817900
321UbiquitinationSTSEGHDKTSVSTHT
HCCCCCCCCCCCCCC		36.7033845483
323PhosphorylationSEGHDKTSVSTHTRS
CCCCCCCCCCCCCCC		21.5823312004
325PhosphorylationGHDKTSVSTHTRSGN
CCCCCCCCCCCCCCC		17.7828348404
326PhosphorylationHDKTSVSTHTRSGNL
CCCCCCCCCCCCCCC		25.7228348404
330PhosphorylationSVSTHTRSGNLKRPK
CCCCCCCCCCCCCCC		32.9428985074
345PhosphorylationIGKRFQDSEFSSSQG
CCCHHCCCCCCCCCC		29.7421406692
348PhosphorylationRFQDSEFSSSQGEDE
HHCCCCCCCCCCCCC		25.6529116813
349PhosphorylationFQDSEFSSSQGEDEK
HCCCCCCCCCCCCCC		31.8129116813
350PhosphorylationQDSEFSSSQGEDEKT
CCCCCCCCCCCCCCC		40.7925693802
357PhosphorylationSQGEDEKTSQTSLTA
CCCCCCCCCCHHHHH		24.8229116813
358PhosphorylationQGEDEKTSQTSLTAS
CCCCCCCCCHHHHHH		42.3929116813
360PhosphorylationEDEKTSQTSLTASIN
CCCCCCCHHHHHHHH		26.0227282143
361PhosphorylationDEKTSQTSLTASINK
CCCCCCHHHHHHHHH		18.9823312004
363PhosphorylationKTSQTSLTASINKLE
CCCCHHHHHHHHHHH		20.3725693802
365PhosphorylationSQTSLTASINKLEST
CCHHHHHHHHHHHHC		22.8129743597
371PhosphorylationASINKLESTARPSES
HHHHHHHHCCCCCCC		37.4923401153
372PhosphorylationSINKLESTARPSESS
HHHHHHHCCCCCCCH		19.8123401153
376PhosphorylationLESTARPSESSEEFL
HHHCCCCCCCHHHHH		44.5523927012
378PhosphorylationSTARPSESSEEFLEE
HCCCCCCCHHHHHHH		47.6023927012
379PhosphorylationTARPSESSEEFLEEE
CCCCCCCHHHHHHHC		36.7723927012
398PhosphorylationGIEFEDESSDRDARP
CCCCCCCCCCCCCHH		50.2723401153
399PhosphorylationIEFEDESSDRDARPA
CCCCCCCCCCCCHHH		34.3230266825
409PhosphorylationDARPALETQPQQEKQ
CCHHHHHCCCHHHCC		46.5326657352
422PhosphorylationKQDGEKESELEPMNG
CCCCCCCCCCCCCCC		59.5627174698
435PhosphorylationNGEIMDDSLKTSLIT
CCCCCCCHHHHCCCC		27.7429978859
437PhosphorylationEIMDDSLKTSLITEE
CCCCCHHHHCCCCCC		39.7733259812
438PhosphorylationIMDDSLKTSLITEEE
CCCCHHHHCCCCCCC		33.7728450419
439PhosphorylationMDDSLKTSLITEEED
CCCHHHHCCCCCCCC		19.0428450419
442PhosphorylationSLKTSLITEEEDSTS
HHHHCCCCCCCCCHH		42.5130278072
447PhosphorylationLITEEEDSTSEVLDE
CCCCCCCCHHHHCCH		36.7930278072
448PhosphorylationITEEEDSTSEVLDEE
CCCCCCCHHHHCCHH		41.0330278072
449PhosphorylationTEEEDSTSEVLDEEL
CCCCCCHHHHCCHHH		29.6519664994
463PhosphorylationLKLQPFNSSEDSTNL
HCCCCCCCCCCCCCC		35.1727732954
464PhosphorylationKLQPFNSSEDSTNLV
CCCCCCCCCCCCCCE		46.6727732954
467PhosphorylationPFNSSEDSTNLVPLV
CCCCCCCCCCCEEEE		18.3630266825
468PhosphorylationFNSSEDSTNLVPLVV
CCCCCCCCCCEEEEE		44.9130266825
477PhosphorylationLVPLVVESSKPPEVD
CEEEEEECCCCCCCC		31.8630266825
478PhosphorylationVPLVVESSKPPEVDA
EEEEEECCCCCCCCC		35.3630266825
489PhosphorylationEVDAPDKTPRIPDSE
CCCCCCCCCCCCCHH		25.7730266825
495PhosphorylationKTPRIPDSEMLMDEG
CCCCCCCHHHCCCCC		21.3930108239
503PhosphorylationEMLMDEGTSDEKGHM
HHCCCCCCCCCCCCH		30.8430108239
504PhosphorylationMLMDEGTSDEKGHME
HCCCCCCCCCCCCHH		55.4130108239
515PhosphorylationGHMEEKLSLLPRKKA
CCHHHHHHCCCCCCC		38.64-
526PhosphorylationRKKAHLGSSDNVATM
CCCCCCCCCCCEEEC		40.6623927012
527PhosphorylationKKAHLGSSDNVATMS
CCCCCCCCCCEEECC		31.2623927012
532PhosphorylationGSSDNVATMSNEERS
CCCCCEEECCHHHHC		19.4925850435
533SulfoxidationSSDNVATMSNEERSD
CCCCEEECCHHHHCC		2.6721406390
533PhosphorylationSSDNVATMSNEERSD
CCCCEEECCHHHHCC		2.6733259812
534PhosphorylationSDNVATMSNEERSDG
CCCEEECCHHHHCCC		36.4123927012
611PhosphorylationNAGQKNQSEEQSEAS
CCCCCCCCHHHHHHH		53.1222617229
615PhosphorylationKNQSEEQSEASSEQL
CCCCHHHHHHHHHHH		38.1122617229
618PhosphorylationSEEQSEASSEQLDQF
CHHHHHHHHHHHHHH		30.2923401153
619PhosphorylationEEQSEASSEQLDQFT
HHHHHHHHHHHHHHH		36.0922617229
626PhosphorylationSEQLDQFTQSAEKAV
HHHHHHHHHHHHHHH		18.9130108239
628PhosphorylationQLDQFTQSAEKAVDS
HHHHHHHHHHHHHCC		35.0227732954
635PhosphorylationSAEKAVDSSSEEIEV
HHHHHHCCCCCCEEE		29.2119664994
636PhosphorylationAEKAVDSSSEEIEVE
HHHHHCCCCCCEEEE		36.9928176443
637PhosphorylationEKAVDSSSEEIEVEV
HHHHCCCCCCEEEEE		43.1119664994
657AcetylationRNLRRKAKGHKGPAK
HHHHHHHCCCCCCCC		65.6611307441
664AcetylationKGHKGPAKKKAKLT-
CCCCCCCCHHCCCC-		58.9211307449
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 F169A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of F169A_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 F169A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of F169A_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 F169A_HUMAN

loading...

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-449, 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-447; SER-619; SER-635;SER-636 AND SER-637, AND MASS SPECTROMETRY.

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