FERM1_HUMAN - dbPTM
FERM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FERM1_HUMAN
UniProt AC Q9BQL6
Protein Name Fermitin family homolog 1
Gene Name FERMT1
Organism Homo sapiens (Human).
Sequence Length 677
Subcellular Localization Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell projection, ruffle membrane
Peripheral membrane protein
Cytoplasmic side. Constituent of focal adhesions. Localized at the basal aspect of skin keratinocytes, close to the cell membrane.
Protein Description Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites. May mediate TGF-beta 1 signaling in tumor progression..
Protein Sequence MLSSTDFTFASWELVVRVDHPNEEQQKDVTLRVSGDLHVGGVMLKLVEQINISQDWSDFALWWEQKHCWLLKTHWTLDKYGVQADAKLLFTPQHKMLRLRLPNLKMVRLRVSFSAVVFKAVSDICKILNIRRSEELSLLKPSGDYFKKKKKKDKNNKEPIIEDILNLESSPTASGSSVSPGLYSKTMTPIYDPINGTPASSTMTWFSDSPLTEQNCSILAFSQPPQSPEALADMYQPRSLVDKAKLNAGWLDSSRSLMEQGIQEDEQLLLRFKYYSFFDLNPKYDAVRINQLYEQARWAILLEEIDCTEEEMLIFAALQYHISKLSLSAETQDFAGESEVDEIEAALSNLEVTLEGGKADSLLEDITDIPKLADNLKLFRPKKLLPKAFKQYWFIFKDTSIAYFKNKELEQGEPLEKLNLRGCEVVPDVNVAGRKFGIKLLIPVADGMNEMYLRCDHENQYAQWMAACMLASKGKTMADSSYQPEVLNILSFLRMKNRNSASQVASSLENMDMNPECFVSPRCAKRHKSKQLAARILEAHQNVAQMPLVEAKLRFIQAWQSLPEFGLTYYLVRFKGSKKDDILGVSYNRLIKIDAATGIPVTTWRFTNIKQWNVNWETRQVVIEFDQNVFTAFTCLSADCKIVHEYIGGYIFLSTRSKDQNETLDEDLFHKLTGGQD
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
30PhosphorylationEEQQKDVTLRVSGDL
HHHHCCCEEEEECCE		20.9824719451
137PhosphorylationIRRSEELSLLKPSGD
CCCCHHHHCCCCCCC		34.6324719451
148AcetylationPSGDYFKKKKKKDKN
CCCCHHHHCCCCCCC		60.9824431609
169PhosphorylationEDILNLESSPTASGS
HHHHCCCCCCCCCCC		44.7930278072
170PhosphorylationDILNLESSPTASGSS
HHHCCCCCCCCCCCC		19.5230278072
172PhosphorylationLNLESSPTASGSSVS
HCCCCCCCCCCCCCC		35.0930278072
174PhosphorylationLESSPTASGSSVSPG
CCCCCCCCCCCCCCC		41.5130278072
176PhosphorylationSSPTASGSSVSPGLY
CCCCCCCCCCCCCCC		25.6825106551
177PhosphorylationSPTASGSSVSPGLYS
CCCCCCCCCCCCCCC		30.0926657352
179PhosphorylationTASGSSVSPGLYSKT
CCCCCCCCCCCCCCC		18.3928731282
183PhosphorylationSSVSPGLYSKTMTPI
CCCCCCCCCCCCCCC		17.6530206219
184PhosphorylationSVSPGLYSKTMTPIY
CCCCCCCCCCCCCCC		27.0530206219
191PhosphorylationSKTMTPIYDPINGTP
CCCCCCCCCCCCCCC		19.5022817900
274PhosphorylationQLLLRFKYYSFFDLN
HHHHHHEEEECCCCC		11.1321130716
275PhosphorylationLLLRFKYYSFFDLNP
HHHHHEEEECCCCCC		10.2921130716
361PhosphorylationLEGGKADSLLEDITD
ECCCCHHHHHHHHCC		39.4530266825
367PhosphorylationDSLLEDITDIPKLAD
HHHHHHHCCCHHHHH		39.9523186163
371UbiquitinationEDITDIPKLADNLKL
HHHCCCHHHHHHHHH		57.55-
392PhosphorylationLPKAFKQYWFIFKDT
CCHHHHHEEEEEECC		11.6822817900
399PhosphorylationYWFIFKDTSIAYFKN
EEEEEECCEEEEECC		23.7121082442
403PhosphorylationFKDTSIAYFKNKELE
EECCEEEEECCCCCC		17.2621082442
435AcetylationDVNVAGRKFGIKLLI
CCCCCCCEEEEEEEE		47.2011789985
452PhosphorylationADGMNEMYLRCDHEN
CCCCCCEEEECCCHH		5.70-
500PhosphorylationLRMKNRNSASQVASS
HHCCCCCCHHHHHHH		26.5127422710
502PhosphorylationMKNRNSASQVASSLE
CCCCCCHHHHHHHHH		25.6318669648
506PhosphorylationNSASQVASSLENMDM
CCHHHHHHHHHCCCC		36.2823090842
507PhosphorylationSASQVASSLENMDMN
CHHHHHHHHHCCCCC		29.9323090842
520PhosphorylationMNPECFVSPRCAKRH
CCHHHCCCHHHHHHH		6.0821712546
586PhosphorylationKDDILGVSYNRLIKI
CCCEEEEECCEEEEE		18.1921406692
587PhosphorylationDDILGVSYNRLIKID
CCEEEEECCEEEEEE		11.2521406692
592UbiquitinationVSYNRLIKIDAATGI
EECCEEEEEECCCCC		38.84-
597PhosphorylationLIKIDAATGIPVTTW
EEEEECCCCCCEEEE		37.0527174698
602PhosphorylationAATGIPVTTWRFTNI
CCCCCCEEEEEEECC		18.4527174698
603PhosphorylationATGIPVTTWRFTNIK
CCCCCEEEEEEECCE		18.1927174698
607PhosphorylationPVTTWRFTNIKQWNV
CEEEEEEECCEECCC		27.7127174698
618PhosphorylationQWNVNWETRQVVIEF
ECCCCEEEEEEEEEE		20.3027174698
657PhosphorylationYIFLSTRSKDQNETL
EEEEECCCCCCCCCC		40.4423312004
663PhosphorylationRSKDQNETLDEDLFH
CCCCCCCCCCHHHHH		47.2425159151
671UbiquitinationLDEDLFHKLTGGQD-
CCHHHHHHHHCCCC-		40.17-
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 FERM1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FERM1_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 FERM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CYBP_HUMANCACYBPphysical
26344197
RNH2B_HUMANRNASEH2Bphysical
26344197
SBDS_HUMANSBDSphysical
26344197
SKIV2_HUMANSKIV2Lphysical
26344197
ELOB_HUMANTCEB2physical
26344197
TTC37_HUMANTTC37physical
26344197
FERM2_HUMANFERMT2physical
28514442
URP2_HUMANFERMT3physical
28514442
MAGI3_HUMANMAGI3physical
28514442
ITPA_HUMANITPAphysical
28514442
SYTC2_HUMANTARSL2physical
28514442
Drug and Disease Associations
Kegg Disease
H00588 Kindler syndrome
OMIM Disease
173650Kindler syndrome (KINDS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FERM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-170 AND SER-179, ANDMASS SPECTROMETRY.

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