FIGL1_HUMAN - dbPTM
FIGL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FIGL1_HUMAN
UniProt AC Q6PIW4
Protein Name Fidgetin-like protein 1
Gene Name FIGNL1
Organism Homo sapiens (Human).
Sequence Length 674
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, perinuclear region . Together with RAD51 and a subset of H2A histone proteins, redistributed in discrete nuclear DNA damage-induced foci after ionizing radiation (IR) treatment (PubMed:23754376).
Protein Description Involved in DNA double-strand break (DBS) repair via homologous recombination (HR). Recruited at DSB sites independently of BRCA2, RAD51 and RAD51 paralogs in a H2AX-dependent manner. May regulate osteoblast proliferation and differentiation. [PubMed: 23754376 May play a role in the control of male meiosis dynamic (By similarity]
Protein Sequence MQTSSSRSVHLSEWQKNYFAITSGICTGPKADAYRAQILRIQYAWANSEISQVCATKLFKKYAEKYSAIIDSDNVESGLNNYAENILTLAGSQQTDSDKWQSGLSINNVFKMSSVQKMMQAGKKFKDSLLEPALASVVIHKEATVFDLPKFSVCGSSQESDSLPNSAHDRDRTQDFPESNRLKLLQNAQPPMVTNTARTCPTFSAPVGESATAKFHVTPLFGNVKKENHSSAKENIGLNVFLSNQSCFPAACENPQRKSFYGSGTIDALSNPILNKACSKTEDNGPKEDSSLPTFKTAKEQLWVDQQKKYHQPQRASGSSYGGVKKSLGASRSRGILGKFVPPIPKQDGGEQNGGMQCKPYGAGPTEPAHPVDERLKNLEPKMIELIMNEIMDHGPPVNWEDIAGVEFAKATIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEKMVRALFAVARCQQPAVIFIDEIDSLLSQRGDGEHESSRRIKTEFLVQLDGATTSSEDRILVVGATNRPQEIDEAARRRLVKRLYIPLPEASARKQIVINLMSKEQCCLSEEEIEQIVQQSDAFSGADMTQLCREASLGPIRSLQTADIATITPDQVRPIAYIDFENAFRTVRPSVSPKDLELYENWNKTFGCGK
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
3Phosphorylation-----MQTSSSRSVH
-----CCCCCCCCCC		29.3129888752
4Phosphorylation----MQTSSSRSVHL
----CCCCCCCCCCH		14.9329888752
5Phosphorylation---MQTSSSRSVHLS
---CCCCCCCCCCHH		32.9129888752
6Phosphorylation--MQTSSSRSVHLSE
--CCCCCCCCCCHHH		28.4829888752
8PhosphorylationMQTSSSRSVHLSEWQ
CCCCCCCCCCHHHHH		18.8129888752
12PhosphorylationSSRSVHLSEWQKNYF
CCCCCCHHHHHHHEE		23.1629888752
30UbiquitinationSGICTGPKADAYRAQ
CCCCCCCCHHHHHHH		61.31-
48PhosphorylationIQYAWANSEISQVCA
HHHHHCCCHHHHHHH		28.6728258704
56PhosphorylationEISQVCATKLFKKYA
HHHHHHHHHHHHHHH		24.1328258704
65UbiquitinationLFKKYAEKYSAIIDS
HHHHHHHHHCEEECC		36.01-
77PhosphorylationIDSDNVESGLNNYAE
ECCCCCCHHHHHHHH		44.2728102081
82PhosphorylationVESGLNNYAENILTL
CCHHHHHHHHHCHHH		17.7728102081
88PhosphorylationNYAENILTLAGSQQT
HHHHHCHHHCCCCCC		15.6828102081
92PhosphorylationNILTLAGSQQTDSDK
HCHHHCCCCCCCCCH		17.3228102081
95PhosphorylationTLAGSQQTDSDKWQS
HHCCCCCCCCCHHHC		29.8128102081
117UbiquitinationFKMSSVQKMMQAGKK
HHHHHHHHHHHCCHH		33.90-
117AcetylationFKMSSVQKMMQAGKK
HHHHHHHHHHHCCHH		33.9061147
123AcetylationQKMMQAGKKFKDSLL
HHHHHCCHHHHHHHH		59.0490581
124UbiquitinationKMMQAGKKFKDSLLE
HHHHCCHHHHHHHHH		57.64-
126UbiquitinationMQAGKKFKDSLLEPA
HHCCHHHHHHHHHHH		56.11-
126MethylationMQAGKKFKDSLLEPA
HHCCHHHHHHHHHHH		56.11-
141UbiquitinationLASVVIHKEATVFDL
CHHHEECCCCEEECC		37.61-
144PhosphorylationVVIHKEATVFDLPKF
HEECCCCEEECCCCC		23.8525954137
147 (in isoform 2)Ubiquitination-58.6921890473
150UbiquitinationATVFDLPKFSVCGSS
CEEECCCCCEECCCC		58.53-
150SumoylationATVFDLPKFSVCGSS
CEEECCCCCEECCCC		58.53-
152PhosphorylationVFDLPKFSVCGSSQE
EECCCCCEECCCCCC		23.7127251275
156PhosphorylationPKFSVCGSSQESDSL
CCCEECCCCCCCCCC		24.5823663014
157PhosphorylationKFSVCGSSQESDSLP
CCEECCCCCCCCCCC		24.2117525332
160PhosphorylationVCGSSQESDSLPNSA
ECCCCCCCCCCCCCC		25.5123663014
162PhosphorylationGSSQESDSLPNSAHD
CCCCCCCCCCCCCCC		55.8123663014
166PhosphorylationESDSLPNSAHDRDRT
CCCCCCCCCCCCCCC		25.6623312004
183UbiquitinationFPESNRLKLLQNAQP
CCHHHHHHHHHHCCC		43.87-
192SulfoxidationLQNAQPPMVTNTART
HHHCCCCCEEECCCC		8.0521406390
214UbiquitinationVGESATAKFHVTPLF
CCCCCCEEEEEECCC		31.48-
218PhosphorylationATAKFHVTPLFGNVK
CCEEEEEECCCCCCC		13.0025159151
225SumoylationTPLFGNVKKENHSSA
ECCCCCCCCCCCCCH		59.3728112733
225UbiquitinationTPLFGNVKKENHSSA
ECCCCCCCCCCCCCH		59.37-
225SumoylationTPLFGNVKKENHSSA
ECCCCCCCCCCCCCH		59.37-
226UbiquitinationPLFGNVKKENHSSAK
CCCCCCCCCCCCCHH		60.51-
228AcetylationFGNVKKENHSSAKEN
CCCCCCCCCCCHHHH		49.5819608861
258SumoylationACENPQRKSFYGSGT
HCCCCCCCCCCCCCH		39.40-
258UbiquitinationACENPQRKSFYGSGT
HCCCCCCCCCCCCCH		39.4021890473
258 (in isoform 1)Ubiquitination-39.4021890473
258SumoylationACENPQRKSFYGSGT
HCCCCCCCCCCCCCH		39.40-
259PhosphorylationCENPQRKSFYGSGTI
CCCCCCCCCCCCCHH		26.3725159151
261PhosphorylationNPQRKSFYGSGTIDA
CCCCCCCCCCCHHHH		19.9221712546
263PhosphorylationQRKSFYGSGTIDALS
CCCCCCCCCHHHHHC		22.7623186163
265PhosphorylationKSFYGSGTIDALSNP
CCCCCCCHHHHHCCH		19.8523186163
270PhosphorylationSGTIDALSNPILNKA
CCHHHHHCCHHHHHH		42.1323879269
276UbiquitinationLSNPILNKACSKTED
HCCHHHHHHHCCCCC		47.53-
279PhosphorylationPILNKACSKTEDNGP
HHHHHHHCCCCCCCC		47.6923879269
287UbiquitinationKTEDNGPKEDSSLPT
CCCCCCCCCCCCCCC		75.46-
291PhosphorylationNGPKEDSSLPTFKTA
CCCCCCCCCCCHHHH		51.1728555341
296MethylationDSSLPTFKTAKEQLW
CCCCCCHHHHHHHHH		50.48-
296UbiquitinationDSSLPTFKTAKEQLW
CCCCCCHHHHHHHHH		50.48-
297PhosphorylationSSLPTFKTAKEQLWV
CCCCCHHHHHHHHHH		38.4822817900
299UbiquitinationLPTFKTAKEQLWVDQ
CCCHHHHHHHHHHHH		51.75-
308UbiquitinationQLWVDQQKKYHQPQR
HHHHHHHHHCCCCCC		50.06-
309UbiquitinationLWVDQQKKYHQPQRA
HHHHHHHHCCCCCCC		43.56-
317PhosphorylationYHQPQRASGSSYGGV
CCCCCCCCCCCCCHH		41.2028555341
319PhosphorylationQPQRASGSSYGGVKK
CCCCCCCCCCCHHHH		20.2128674419
325UbiquitinationGSSYGGVKKSLGASR
CCCCCHHHHHCCCCC		39.66-
339AcetylationRSRGILGKFVPPIPK
CCCCCCCCCCCCCCC		39.4819608861
339SumoylationRSRGILGKFVPPIPK
CCCCCCCCCCCCCCC		39.4819608861
339SumoylationRSRGILGKFVPPIPK
CCCCCCCCCCCCCCC		39.48-
359UbiquitinationQNGGMQCKPYGAGPT
CCCCCCCCCCCCCCC		25.12-
359AcetylationQNGGMQCKPYGAGPT
CCCCCCCCCCCCCCC		25.1226051181
377UbiquitinationHPVDERLKNLEPKMI
CCHHHHHHCCCHHHH		66.75-
445PhosphorylationLLFGPPGTGKTLIGK
EEECCCCCCHHHHHH		41.08-
447UbiquitinationFGPPGTGKTLIGKCI
ECCCCCCHHHHHHHH		39.74-
456PhosphorylationLIGKCIASQSGATFF
HHHHHHHCCCCCEEE		12.6426434552
458PhosphorylationGKCIASQSGATFFSI
HHHHHCCCCCEEEEE		28.0926434552
468PhosphorylationTFFSISASSLTSKWV
EEEEEEHHHHCCCCC		21.06-
507PhosphorylationDEIDSLLSQRGDGEH
CCHHHHHHHCCCCCC		24.1124719451
564PhosphorylationRRLVKRLYIPLPEAS
HHHHHHHCCCCCHHH		12.4321406692
571PhosphorylationYIPLPEASARKQIVI
CCCCCHHHHHHHHHH		27.2621406692
658UbiquitinationVRPSVSPKDLELYEN
CCCCCCHHHHHHHHH		68.39-
668UbiquitinationELYENWNKTFGCGK-
HHHHHHHHHCCCCC-		36.52-
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 FIGL1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FIGL1_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 FIGL1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HS71L_HUMANHSPA1Lphysical
22939629
KDM1A_HUMANKDM1Aphysical
23455924
CALD1_HUMANCALD1physical
26496610
T22D3_HUMANTSC22D3physical
26496610
CA112_HUMANC1orf112physical
26496610
THA11_HUMANTHAP11physical
26496610
TDRD3_HUMANTDRD3physical
26496610
RAD51_HUMANRAD51physical
28514442
POTEI_HUMANPOTEIphysical
28514442
VCIP1_HUMANVCPIP1physical
28514442
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 FIGL1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-339, AND MASS SPECTROMETRY.
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-157, AND MASSSPECTROMETRY.

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