FHOD3_HUMAN - dbPTM
FHOD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FHOD3_HUMAN
UniProt AC Q2V2M9
Protein Name FH1/FH2 domain-containing protein 3
Gene Name FHOD3
Organism Homo sapiens (Human).
Sequence Length 1422
Subcellular Localization Cytoplasm, cytoskeleton . Main part of the protein localizes to actin fibers and the remaining part displays filamentous staining..
Isoform 4: Cytoplasm, myofibril, sarcomere, Z line. Threonine phosphorylation in isoform 4-specific sequence TDT
Protein Description Actin-organizing protein that may cause stress fiber formation together with cell elongation (By similarity). Isoform 4 may play a role in actin filament polymerization in cardiomyocytes..
Protein Sequence MATLACRVQFLDDTDPFNSTNFPEPSRPPLFTFREDLALGTQLAGVHRLLQAPHKLDDCTLQLSHNGAYLDLEATLAEQRDELEGFQDDAGRGKKHSIILRTQLSVRVHACIEKLYNSSGRDLRRALFSLKQIFQDDKDLVHEFVVAEGLTCLIKVGAEADQNYQNYILRALGQIMLYVDGMNGVINRNETIQWLYTLIGSKFRLVVKTALKLLLVFVEYSESNAPLLIQAVTAVDTKRGVKPWSNIMEILEEKDGVDTELLVYAMTLVNKTLSGLPDQDTFYDVVDCLEELGIAAVSQRHLNKKGTDLDLVEQLNIYEVALRHEDGDETTEPPPSGCRDRRRASVCSSGGGEHRGLDRRRSRRHSVQSIKSTLSAPTSPCSQSAPSFKPNQVRDLREKYSNFGNNSYHSSRPSSGSSVPTTPTSSVSPPQEARLERSSPSGLLTSSFRQHQESLAAERERRRQEREERLQRIEREERNKFRYKYLEQLAAEEHEKELRSRSVSRGRADLSLDLTSPAAPACLAPLSHSPSSSDSQEALTVSASSPGTPHHPQASAGDPEPESEAEPEAEAGAGQVADEAGQDIASAHEGAETEVEQALEQEPEERASLSEKERQNEGVNERDNCSASSVSSSSSTLEREEKEDKLSRDRTTGLWPAGVQDAGVNGQCGDILTNKRFMLDMLYAHNRKSPDDEEKGDGEAGRTQQEAEAVASLATRISTLQANSQTQDESVRRVDVGCLDNRGSVKAFAEKFNSGDLGRGSISPDAEPNDKVPETAPVQPKTESDYIWDQLMANPRELRIQDMDFTDLGEEDDIDVLDVDLGHREAPGPPPPPPPTFLGLPPPPPPPLLDSIPPPPVPGNLLVPPPPVFNAPQGLGWSQVPRGQPTFTKKKKTIRLFWNEVRPFDWPCKNNRRCREFLWSKLEPIKVDTSRLEHLFESKSKELSVSKKTAADGKRQEIIVLDSKRSNAINIGLTVLPPPRTIKIAILNFDEYALNKEGIEKILTMIPTDEEKQKIQEAQLANPEIPLGSAEQFLLTLSSISELSARLHLWAFKMDYETTEKEVAEPLLDLKEGIDQLENNKTLGFILSTLLAIGNFLNGTNAKAFELSYLEKVPEVKDTVHKQSLLHHVCTMVVENFPDSSDLYSEIGAITRSAKVDFDQLQDNLCQMERRCKASWDHLKAIAKHEMKPVLKQRMSEFLKDCAERIIILKIVHRRIINRFHSFLLFMGHPPYAIREVNINKFCRIISEFALEYRTTRERVLQQKQKRANHRERNKTRGKMITDSGKFSGSSPAPPSQPQGLSYAEDAAEHENMKAVLKTSSPSVEDATPALGVRTRSRASRGSTSSWTMGTDDSPNVTDDAADEIMDRIVKSATQVPSQRVVPRERKRSRANRKSLRRTLKSGLTPEEARALGLVGTSELQL
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
129PhosphorylationDLRRALFSLKQIFQD
HHHHHHHHHHHHHCC		35.1924719451
191PhosphorylationGVINRNETIQWLYTL
CCCCHHHHHHHHHHH		23.2425003641
196PhosphorylationNETIQWLYTLIGSKF
HHHHHHHHHHHCCCH		9.1325003641
345PhosphorylationCRDRRRASVCSSGGG
CCCCCCCEECCCCCC		23.1128857561
348PhosphorylationRRRASVCSSGGGEHR
CCCCEECCCCCCCCC		29.8427251275
349PhosphorylationRRASVCSSGGGEHRG
CCCEECCCCCCCCCC		36.01-
366PhosphorylationRRRSRRHSVQSIKST
HHHHHHHHHHHHHHH		21.7529743597
372PhosphorylationHSVQSIKSTLSAPTS
HHHHHHHHHHCCCCC		32.6730108239
373PhosphorylationSVQSIKSTLSAPTSP
HHHHHHHHHCCCCCC		21.5230108239
375PhosphorylationQSIKSTLSAPTSPCS
HHHHHHHCCCCCCCC		32.0823927012
378PhosphorylationKSTLSAPTSPCSQSA
HHHHCCCCCCCCCCC		45.0423927012
379PhosphorylationSTLSAPTSPCSQSAP
HHHCCCCCCCCCCCC		23.8923927012
382PhosphorylationSAPTSPCSQSAPSFK
CCCCCCCCCCCCCCC		30.4730108239
384PhosphorylationPTSPCSQSAPSFKPN
CCCCCCCCCCCCCHH		26.3430108239
387PhosphorylationPCSQSAPSFKPNQVR
CCCCCCCCCCHHHHH		45.6927251275
411PhosphorylationGNNSYHSSRPSSGSS
CCCCCCCCCCCCCCC		34.59-
422PhosphorylationSGSSVPTTPTSSVSP
CCCCCCCCCCCCCCC		20.64-
426PhosphorylationVPTTPTSSVSPPQEA
CCCCCCCCCCCCHHH		29.14-
438PhosphorylationQEARLERSSPSGLLT
HHHHHHHCCCCCCCC		36.9128857561
439PhosphorylationEARLERSSPSGLLTS
HHHHHHCCCCCCCCH		29.3428857561
441PhosphorylationRLERSSPSGLLTSSF
HHHHCCCCCCCCHHH		43.98-
445PhosphorylationSSPSGLLTSSFRQHQ
CCCCCCCCHHHHHHH		27.6328857561
446PhosphorylationSPSGLLTSSFRQHQE
CCCCCCCHHHHHHHH		27.7028857561
447PhosphorylationPSGLLTSSFRQHQES
CCCCCCHHHHHHHHH		21.1528857561
500O-linked_GlycosylationEHEKELRSRSVSRGR
HHHHHHHHCCHHCCC		41.3430379171
608PhosphorylationQEPEERASLSEKERQ
HCHHHHHCCCHHHHH		38.3528102081
626PhosphorylationVNERDNCSASSVSSS
CCCCCCCCHHHCCCC		37.1229083192
628PhosphorylationERDNCSASSVSSSSS
CCCCCCHHHCCCCCC		18.2529083192
629PhosphorylationRDNCSASSVSSSSST
CCCCCHHHCCCCCCH		26.2429083192
631PhosphorylationNCSASSVSSSSSTLE
CCCHHHCCCCCCHHC		26.8429083192
632PhosphorylationCSASSVSSSSSTLER
CCHHHCCCCCCHHCH		31.8929083192
633PhosphorylationSASSVSSSSSTLERE
CHHHCCCCCCHHCHH		22.3229083192
634PhosphorylationASSVSSSSSTLEREE
HHHCCCCCCHHCHHH		29.3229083192
635PhosphorylationSSVSSSSSTLEREEK
HHCCCCCCHHCHHHH		38.6729083192
636PhosphorylationSVSSSSSTLEREEKE
HCCCCCCHHCHHHHH		34.2929083192
724PhosphorylationISTLQANSQTQDESV
HHHHHHCCCCCCCCC		37.3126714015
761PhosphorylationSGDLGRGSISPDAEP
CCCCCCCCCCCCCCC		20.6630108239
763PhosphorylationDLGRGSISPDAEPND
CCCCCCCCCCCCCCC		20.5828355574
775PhosphorylationPNDKVPETAPVQPKT
CCCCCCCCCCCCCCC		30.14-
778PhosphorylationKVPETAPVQPKTESD
CCCCCCCCCCCCHHH		16.4427251275
780PhosphorylationPETAPVQPKTESDYI
CCCCCCCCCCHHHHH		45.8527251275
893PhosphorylationTFTKKKKTIRLFWNE
CCCCCCCEEEEECCC		21.87-
944PhosphorylationESKSKELSVSKKTAA
HHCCCCCCCCCEECC		25.9924719451
949PhosphorylationELSVSKKTAADGKRQ
CCCCCCEECCCCCCC		30.7128634120
992PhosphorylationAILNFDEYALNKEGI
EEEECHHHHCCHHHH		20.4527811184
1117AcetylationLEKVPEVKDTVHKQS
HCCCCCCCCHHHHHH		46.127683701
1196PhosphorylationPVLKQRMSEFLKDCA
HHHHHHHHHHHHHHH		27.64-
1276PhosphorylationNHRERNKTRGKMITD
HHHHHHHHCCCCCCC		48.48-
1279AcetylationERNKTRGKMITDSGK
HHHHHCCCCCCCCCC		24.6820167786
1286AcetylationKMITDSGKFSGSSPA
CCCCCCCCCCCCCCC		40.0720167786
1290PhosphorylationDSGKFSGSSPAPPSQ
CCCCCCCCCCCCCCC		31.7619276368
1296PhosphorylationGSSPAPPSQPQGLSY
CCCCCCCCCCCCCCH		54.13-
1302PhosphorylationPSQPQGLSYAEDAAE
CCCCCCCCHHHHHHH		29.1719276368
1318AcetylationENMKAVLKTSSPSVE
HHHHHHHHCCCCCHH		39.5020167786
1319PhosphorylationNMKAVLKTSSPSVED
HHHHHHHCCCCCHHH		30.2128857561
1320PhosphorylationMKAVLKTSSPSVEDA
HHHHHHCCCCCHHHC		38.3728857561
1321PhosphorylationKAVLKTSSPSVEDAT
HHHHHCCCCCHHHCC		26.8228857561
1343PhosphorylationRSRASRGSTSSWTMG
CCCCCCCCCCCCCCC		24.8124043423
1344PhosphorylationSRASRGSTSSWTMGT
CCCCCCCCCCCCCCC		29.6024043423
1345PhosphorylationRASRGSTSSWTMGTD
CCCCCCCCCCCCCCC		26.1024043423
1346PhosphorylationASRGSTSSWTMGTDD
CCCCCCCCCCCCCCC		27.0124043423
1348PhosphorylationRGSTSSWTMGTDDSP
CCCCCCCCCCCCCCC		13.9924043423
1351PhosphorylationTSSWTMGTDDSPNVT
CCCCCCCCCCCCCCC		26.3024043423
1354PhosphorylationWTMGTDDSPNVTDDA
CCCCCCCCCCCCHHH		22.6024043423
1358PhosphorylationTDDSPNVTDDAADEI
CCCCCCCCHHHHHHH		34.5024043423
1395PhosphorylationRSRANRKSLRRTLKS
HHHHHHHHHHHHHHC		24.7029514088
1399PhosphorylationNRKSLRRTLKSGLTP
HHHHHHHHHHCCCCH		31.9129514088
1402PhosphorylationSLRRTLKSGLTPEEA
HHHHHHHCCCCHHHH		41.9918785766
1405PhosphorylationRTLKSGLTPEEARAL
HHHHCCCCHHHHHHH		31.9818785766
1474 (in isoform 4)Phosphorylation-21149568
1476 (in isoform 4)Phosphorylation-26437602
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 FHOD3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
1474TPhosphorylation

21149568
1476TPhosphorylation

21149568
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 FHOD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SQSTM_HUMANSQSTM1physical
21149568
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 FHOD3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-375; THR-378 ANDSER-379, AND MASS SPECTROMETRY.

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