FMN2_HUMAN - dbPTM
FMN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FMN2_HUMAN
UniProt AC Q9NZ56
Protein Name Formin-2
Gene Name FMN2
Organism Homo sapiens (Human).
Sequence Length 1722
Subcellular Localization Cytoplasm, cytoskeleton. Cytoplasm, perinuclear region. Cytoplasm, cytosol. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasm, cell cortex. Nucleus, nucleol
Protein Description Required for asymmetric spindle positioning, asymmetric oocyte division and polar body extrusion during female germ cell meiosis (By similarity). Actin-binding protein that is involved in actin cytoskeleton assembly and reorganization. Acts as an actin nucleation factor and promotes assembly of actin filaments together with SPIRE1 and SPIRE2. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Plays a role in responses to DNA damage, cellular stress and hypoxia by protecting CDKN1A against degradation, and thereby plays a role in stress-induced cell cycle arrest. Protects cells against apoptosis by protecting CDKN1A against degradation..
Protein Sequence MGNQDGKLKRSAGDALHEGGGGAEDALGPRDVEATKKGSGGKKALGKHGKGGGGGGGGGESGKKKSKSDSRASVFSNLRIRKNLSKGKGAGGSREDVLDSQALQTGELDSAHSLLTKTPDLSLSADEAGLSDTECADPFEVTGPGGPGPAEARVGGRPIAEDVETAAGAQDGQRTSSGSDTDIYSFHSATEQEDLLSDIQQAIRLQQQQQQQLQLQLQQQQQQQQLQGAEEPAAPPTAVSPQPGAFLGLDRFLLGPSGGAGEAPGSPDTEQALSALSDLPESLAAEPREPQQPPSPGGLPVSEAPSLPAAQPAAKDSPSSTAFPFPEAGPGEEAAGAPVRGAGDTDEEGEEDAFEDAPRGSPGEEWAPEVGEDAPQRLGEEPEEEAQGPDAPAAASLPGSPAPSQRCFKPYPLITPCYIKTTTRQLSSPNHSPSQSPNQSPRIKRRPEPSLSRGSRTALASVAAPAKKHRADGGLAAGLSRSADWTEELGARTPRVGGSAHLLERGVASDSGGGVSPALAAKASGAPAAADGFQNVFTGRTLLEKLFSQQENGPPEEAEKFCSRIIAMGLLLPFSDCFREPCNQNAQTNAASFDQDQLYTWAAVSQPTHSLDYSEGQFPRRVPSMGPPSKPPDEEHRLEDAETESQSAVSETPQKRSDAVQKEVVDMKSEGQATVIQQLEQTIEDLRTKIAELERQYPALDTEVASGHQGLENGVTASGDVCLEALRLEEKEVRHHRILEAKSIQTSPTEEGGVLTLPPVDGLPGRPPCPPGAESGPQTKFCSEISLIVSPRRISVQLDSHQPTQSISQPPPPPSLLWSAGQGQPGSQPPHSISTEFQTSHEHSVSSAFKNSCNIPSPPPLPCTESSSSMPGLGMVPPPPPPLPGMTVPTLPSTAIPQPPPLQGTEMLPPPPPPLPGAGIPPPPPLPGAGILPLPPLPGAGIPPPPPLPGAAIPPPPPLPGAGIPLPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGVGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPRVGIPPPPPLPGAGIPPPPPLPGAGIPPPPPLPGVGIPPPPPLPGVGIPPPPPLPGAGIPPPPPLPGMGIPPAPAPPLPPPGTGIPPPPLLPVSGPPLLPQVGSSTLPTPQVCGFLPPPLPSGLFGLGMNQDKGSRKQPIEPCRPMKPLYWTRIQLHSKRDSSTSLIWEKIEEPSIDCHEFEELFSKTAVKERKKPISDTISKTKAKQVVKLLSNKRSQAVGILMSSLHLDMKDIQHAVVNLDNSVVDLETLQALYENRAQSDELEKIEKHGRSSKDKENAKSLDKPEQFLYELSLIPNFSERVFCILFQSTFSESICSIRRKLELLQKLCETLKNGPGVMQVLGLVLAFGNYMNGGNKTRGQADGFGLDILPKLKDVKSSDNSRSLLSYIVSYYLRNFDEDAGKEQCLFPLPEPQDLFQASQMKFEDFQKDLRKLKKDLKACEVEAGKVYQVSSKEHMQPFKENMEQFIIQAKIDQEAEENSLTETHKCFLETTAYFFMKPKLGEKEVSPNAFFSIWHEFSSDFKDFWKKENKLLLQERVKEAEEVCRQKKGKSLYKIKPRHDSGIKAKISMKT
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
73PhosphorylationSKSDSRASVFSNLRI
CCCCCCHHHHHHHHH		23.68-
76PhosphorylationDSRASVFSNLRIRKN
CCCHHHHHHHHHHHC		32.57-
93PhosphorylationKGKGAGGSREDVLDS
CCCCCCCCHHHHHCH		31.4220363803
100PhosphorylationSREDVLDSQALQTGE
CHHHHHCHHHHHHCC		17.1225307156
105PhosphorylationLDSQALQTGELDSAH
HCHHHHHHCCCCHHH		33.2127732954
110PhosphorylationLQTGELDSAHSLLTK
HHHCCCCHHHHHHHC		40.2720363803
113PhosphorylationGELDSAHSLLTKTPD
CCCCHHHHHHHCCCC		25.4520363803
116PhosphorylationDSAHSLLTKTPDLSL
CHHHHHHHCCCCCCC		37.8620363803
118PhosphorylationAHSLLTKTPDLSLSA
HHHHHHCCCCCCCCC		19.4629449344
122PhosphorylationLTKTPDLSLSADEAG
HHCCCCCCCCCCCCC		27.8829449344
124PhosphorylationKTPDLSLSADEAGLS
CCCCCCCCCCCCCCC		30.2329449344
131PhosphorylationSADEAGLSDTECADP
CCCCCCCCCCCCCCC		41.3828348404
133PhosphorylationDEAGLSDTECADPFE
CCCCCCCCCCCCCCE		29.5928348404
175PhosphorylationGAQDGQRTSSGSDTD
CCCCCCCCCCCCCCC		21.2527732954
176PhosphorylationAQDGQRTSSGSDTDI
CCCCCCCCCCCCCCC		34.5927732954
177PhosphorylationQDGQRTSSGSDTDIY
CCCCCCCCCCCCCCE		41.5227732954
179PhosphorylationGQRTSSGSDTDIYSF
CCCCCCCCCCCCEEC		39.0127732954
181PhosphorylationRTSSGSDTDIYSFHS
CCCCCCCCCCEECCC		26.4527732954
184PhosphorylationSGSDTDIYSFHSATE
CCCCCCCEECCCCHH		14.2225884760
185PhosphorylationGSDTDIYSFHSATEQ
CCCCCCEECCCCHHH		19.4727732954
188PhosphorylationTDIYSFHSATEQEDL
CCCEECCCCHHHHHH		34.5727732954
190PhosphorylationIYSFHSATEQEDLLS
CEECCCCHHHHHHHH		41.0127732954
197PhosphorylationTEQEDLLSDIQQAIR
HHHHHHHHHHHHHHH		39.7127732954
266PhosphorylationGAGEAPGSPDTEQAL
CCCCCCCCCCHHHHH		20.6728348404
269PhosphorylationEAPGSPDTEQALSAL
CCCCCCCHHHHHHHH		33.1228348404
274PhosphorylationPDTEQALSALSDLPE
CCHHHHHHHHHCCCH		30.1326657352
295PhosphorylationREPQQPPSPGGLPVS
CCCCCCCCCCCCCCH		42.7429255136
302PhosphorylationSPGGLPVSEAPSLPA
CCCCCCCHHCCCCCC		26.5429255136
306PhosphorylationLPVSEAPSLPAAQPA
CCCHHCCCCCCCCCC		54.7727732954
317PhosphorylationAQPAAKDSPSSTAFP
CCCCCCCCCCCCCCC		26.4427732954
319PhosphorylationPAAKDSPSSTAFPFP
CCCCCCCCCCCCCCC		44.2527732954
320PhosphorylationAAKDSPSSTAFPFPE
CCCCCCCCCCCCCCC		27.4327732954
321PhosphorylationAKDSPSSTAFPFPEA
CCCCCCCCCCCCCCC		36.3327732954
345PhosphorylationPVRGAGDTDEEGEED
CCCCCCCCCCCCCCC		44.3829255136
361PhosphorylationFEDAPRGSPGEEWAP
CCCCCCCCCCCCCCC		30.8921082442
396PhosphorylationPDAPAAASLPGSPAP
CCCCHHHCCCCCCCC		30.3017525332
400PhosphorylationAAASLPGSPAPSQRC
HHHCCCCCCCCCCCC		18.8917525332
404PhosphorylationLPGSPAPSQRCFKPY
CCCCCCCCCCCCCCC		32.1517525332
421PhosphorylationITPCYIKTTTRQLSS
ECCEEEEECCCCCCC		24.6829514088
422PhosphorylationTPCYIKTTTRQLSSP
CCEEEEECCCCCCCC		18.2529514088
423PhosphorylationPCYIKTTTRQLSSPN
CEEEEECCCCCCCCC		22.9629514088
427PhosphorylationKTTTRQLSSPNHSPS
EECCCCCCCCCCCCC		35.1022199227
428PhosphorylationTTTRQLSSPNHSPSQ
ECCCCCCCCCCCCCC		38.0129514088
432PhosphorylationQLSSPNHSPSQSPNQ
CCCCCCCCCCCCCCC		32.6520363803
434PhosphorylationSSPNHSPSQSPNQSP
CCCCCCCCCCCCCCC		46.4320363803
436PhosphorylationPNHSPSQSPNQSPRI
CCCCCCCCCCCCCCC		30.1020363803
440PhosphorylationPSQSPNQSPRIKRRP
CCCCCCCCCCCCCCC		23.8420363803
457PhosphorylationSLSRGSRTALASVAA
CCCCCCHHHHHHHHH		27.9326699800
461PhosphorylationGSRTALASVAAPAKK
CCHHHHHHHHHCCHH		17.0926699800
482PhosphorylationLAAGLSRSADWTEEL
CCCCCCCCCHHHHHH		27.4922617229
486PhosphorylationLSRSADWTEELGART
CCCCCHHHHHHCCCC		21.8222199227
493PhosphorylationTEELGARTPRVGGSA
HHHHCCCCCCCCCCH		18.2122199227
499PhosphorylationRTPRVGGSAHLLERG
CCCCCCCCHHHHHCC		13.4429255136
509PhosphorylationLLERGVASDSGGGVS
HHHCCCCCCCCCCCC		29.8722199227
511PhosphorylationERGVASDSGGGVSPA
HCCCCCCCCCCCCHH		36.5222199227
516PhosphorylationSDSGGGVSPALAAKA
CCCCCCCCHHHHHHH		14.0229255136
524PhosphorylationPALAAKASGAPAAAD
HHHHHHHHCCCCHHC		34.4827732954
539PhosphorylationGFQNVFTGRTLLEKL
CHHHHHCHHHHHHHH		14.7617525332
543PhosphorylationVFTGRTLLEKLFSQQ
HHCHHHHHHHHHHHC		5.5817525332
547PhosphorylationRTLLEKLFSQQENGP
HHHHHHHHHHCCCCC		10.3017525332
563PhosphorylationEEAEKFCSRIIAMGL
HHHHHHHHHHHHHHH		29.64-
575PhosphorylationMGLLLPFSDCFREPC
HHHHCCHHHHCCCCC		31.37-
624PhosphorylationQFPRRVPSMGPPSKP
CCCCCCCCCCCCCCC		33.2523898821
629PhosphorylationVPSMGPPSKPPDEEH
CCCCCCCCCCCCHHH		62.0123898821
743PhosphorylationHRILEAKSIQTSPTE
HHHEEEECCCCCCCC		27.2925332170
746PhosphorylationLEAKSIQTSPTEEGG
EEEECCCCCCCCCCC		34.7026471730
747PhosphorylationEAKSIQTSPTEEGGV
EEECCCCCCCCCCCE		17.2826471730
749PhosphorylationKSIQTSPTEEGGVLT
ECCCCCCCCCCCEEE		46.5726471730
756PhosphorylationTEEGGVLTLPPVDGL
CCCCCEEECCCCCCC		34.5126471730
783PhosphorylationGPQTKFCSEISLIVS
CCCCCCCCEEEEEEE		40.89-
786PhosphorylationTKFCSEISLIVSPRR
CCCCCEEEEEEECCE		14.16-
790PhosphorylationSEISLIVSPRRISVQ
CEEEEEEECCEEEEE		13.00-
867PhosphorylationPLPCTESSSSMPGLG
CCCCCCCCCCCCCCC		21.8724275569
868PhosphorylationLPCTESSSSMPGLGM
CCCCCCCCCCCCCCC		39.6824275569
1309PhosphorylationQLHSKRDSSTSLIWE
EEECCCCCCCCEEEE		39.2819664994
1312PhosphorylationSKRDSSTSLIWEKIE
CCCCCCCCEEEEECC		21.5819664994
1333PhosphorylationHEFEELFSKTAVKER
HHHHHHHHHHHHHHC		41.5424719451
1361PhosphorylationKQVVKLLSNKRSQAV
HHHHHHHHCCHHHHH		51.2221712546
1588MalonylationRKLKKDLKACEVEAG
HHHHHHHHHCCCCCC		62.2130639696
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 FMN2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FMN2_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 FMN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of FMN2_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616193Mental retardation, autosomal recessive 47 (MRT47)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FMN2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396; SER-400 ANDSER-404, AND MASS SPECTROMETRY.

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