URP2_HUMAN - dbPTM
URP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID URP2_HUMAN
UniProt AC Q86UX7
Protein Name Fermitin family homolog 3
Gene Name FERMT3
Organism Homo sapiens (Human).
Sequence Length 667
Subcellular Localization Cell projection, podosome. Present in the F-actin surrounding ring structure of podosomes, which are specialized adhesion structures of hematopoietic cells..
Protein Description Plays a central role in cell adhesion in hematopoietic cells. [PubMed: 19234463]
Protein Sequence MAGMKTASGDYIDSSWELRVFVGEEDPEAESVTLRVTGESHIGGVLLKIVEQINRKQDWSDHAIWWEQKRQWLLQTHWTLDKYGILADARLFFGPQHRPVILRLPNRRALRLRASFSQPLFQAVAAICRLLSIRHPEELSLLRAPEKKEKKKKEKEPEEELYDLSKVVLAGGVAPALFRGMPAHFSDSAQTEACYHMLSRPQPPPDPLLLQRLPRPSSLSDKTQLHSRWLDSSRCLMQQGIKAGDALWLRFKYYSFFDLDPKTDPVRLTQLYEQARWDLLLEEIDCTEEEMMVFAALQYHINKLSQSGEVGEPAGTDPGLDDLDVALSNLEVKLEGSAPTDVLDSLTTIPELKDHLRIFRIPRRPRKLTLKGYRQHWVVFKETTLSYYKSQDEAPGDPIQQLNLKGCEVVPDVNVSGQKFCIKLLVPSPEGMSEIYLRCQDEQQYARWMAGCRLASKGRTMADSSYTSEVQAILAFLSLQRTGSGGPGNHPHGPDASAEGLNPYGLVAPRFQRKFKAKQLTPRILEAHQNVAQLSLAEAQLRFIQAWQSLPDFGISYVMVRFKGSRKDEILGIANNRLIRIDLAVGDVVKTWRFSNMRQWNVNWDIRQVAIEFDEHINVAFSCVSASCRIVHEYIGGYIFLSTRERARGEELDEDLFLQLTGGHEAF
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
5Acetylation---MAGMKTASGDYI
---CCCCCCCCCCCC		39.7725953088
5Ubiquitination---MAGMKTASGDYI
---CCCCCCCCCCCC		39.77-
6Phosphorylation--MAGMKTASGDYID
--CCCCCCCCCCCCC		19.7028122231
8PhosphorylationMAGMKTASGDYIDSS
CCCCCCCCCCCCCCC		37.1120058876
11PhosphorylationMKTASGDYIDSSWEL
CCCCCCCCCCCCEEE		15.3421082442
14PhosphorylationASGDYIDSSWELRVF
CCCCCCCCCEEEEEE		28.0023403867
15PhosphorylationSGDYIDSSWELRVFV
CCCCCCCCEEEEEEE		22.3323403867
31PhosphorylationEEDPEAESVTLRVTG
CCCCCCCEEEEEEEC		27.7028060719
33PhosphorylationDPEAESVTLRVTGES
CCCCCEEEEEEECCC		20.3728060719
42UbiquitinationRVTGESHIGGVLLKI
EEECCCCHHHHHHHH		7.7624816145
56UbiquitinationIVEQINRKQDWSDHA
HHHHHHCCCCCCCHH		48.3929967540
60PhosphorylationINRKQDWSDHAIWWE
HHCCCCCCCHHHHHH		28.0128270605
69UbiquitinationHAIWWEQKRQWLLQT
HHHHHHHHHHHHHHH		34.7329967540
69AcetylationHAIWWEQKRQWLLQT
HHHHHHHHHHHHHHH		34.7326822725
115PhosphorylationRALRLRASFSQPLFQ
HHHHHHHHCCHHHHH		20.9928450419
117PhosphorylationLRLRASFSQPLFQAV
HHHHHHCCHHHHHHH		28.5228450419
132PhosphorylationAAICRLLSIRHPEEL
HHHHHHHCCCCHHHH		23.3626546556
155UbiquitinationKEKKKKEKEPEEELY
HHHHHCCCCCHHHHH		83.73-
162PhosphorylationKEPEEELYDLSKVVL
CCCHHHHHHHHHHHH		20.3728796482
165PhosphorylationEEELYDLSKVVLAGG
HHHHHHHHHHHHHCC		22.1028796482
166UbiquitinationEELYDLSKVVLAGGV
HHHHHHHHHHHHCCH		43.5929967540
173UbiquitinationKVVLAGGVAPALFRG
HHHHHCCHHHHHHCC		5.8822505724
188PhosphorylationMPAHFSDSAQTEACY
CCCCCCCCHHHHHHH		22.5222210691
191PhosphorylationHFSDSAQTEACYHML
CCCCCHHHHHHHHHH		25.8522210691
195PhosphorylationSAQTEACYHMLSRPQ
CHHHHHHHHHHHCCC		9.4122210691
199PhosphorylationEACYHMLSRPQPPPD
HHHHHHHHCCCCCCC		34.0522210691
217PhosphorylationLQRLPRPSSLSDKTQ
HHCCCCCCCCCCCHH		45.2328450419
218PhosphorylationQRLPRPSSLSDKTQL
HCCCCCCCCCCCHHH		34.2828450419
220PhosphorylationLPRPSSLSDKTQLHS
CCCCCCCCCCHHHHH		38.7228450419
222UbiquitinationRPSSLSDKTQLHSRW
CCCCCCCCHHHHHHH		34.4925015289
235UbiquitinationRWLDSSRCLMQQGIK
HHHHHHHHHHHHCCC		3.9222505724
239UbiquitinationSSRCLMQQGIKAGDA
HHHHHHHHCCCCCCE		41.4322505724
242UbiquitinationCLMQQGIKAGDALWL
HHHHHCCCCCCEEEE		53.81-
243UbiquitinationLMQQGIKAGDALWLR
HHHHCCCCCCEEEEE		21.1222505724
252UbiquitinationDALWLRFKYYSFFDL
CEEEEEEEEEEECCC		36.52-
263PhosphorylationFFDLDPKTDPVRLTQ
ECCCCCCCCCCHHHH		51.4222210691
287PhosphorylationLLEEIDCTEEEMMVF
HHHHCCCCHHHHHHH		42.5622210691
299PhosphorylationMVFAALQYHINKLSQ
HHHHHHHHHHHHHHC		12.9122210691
316PhosphorylationEVGEPAGTDPGLDDL
CCCCCCCCCCCCCHH		40.9228060719
328PhosphorylationDDLDVALSNLEVKLE
CHHHHHHHCCEEEEE		29.6328060719
334UbiquitinationLSNLEVKLEGSAPTD
HHCCEEEEECCCCCH		12.4524816145
337PhosphorylationLEVKLEGSAPTDVLD
CEEEEECCCCCHHHH		23.0026657352
338UbiquitinationEVKLEGSAPTDVLDS
EEEEECCCCCHHHHH		23.1324816145
340PhosphorylationKLEGSAPTDVLDSLT
EEECCCCCHHHHHHC		38.1629255136
345PhosphorylationAPTDVLDSLTTIPEL
CCCHHHHHHCCCHHH		24.3726657352
347PhosphorylationTDVLDSLTTIPELKD
CHHHHHHCCCHHHHH		26.9926074081
348PhosphorylationDVLDSLTTIPELKDH
HHHHHHCCCHHHHHH		39.5726074081
353UbiquitinationLTTIPELKDHLRIFR
HCCCHHHHHHEEEEE		41.2522505724
365 (in isoform 2)Phosphorylation-38.75-
369PhosphorylationPRRPRKLTLKGYRQH
CCCCCCEECCCCHHE		29.4723401153
371MethylationRPRKLTLKGYRQHWV
CCCCEECCCCHHEEE		48.9772611923
371UbiquitinationRPRKLTLKGYRQHWV
CCCCEECCCCHHEEE		48.9729967540
373PhosphorylationRKLTLKGYRQHWVVF
CCEECCCCHHEEEEE		12.9123312004
383UbiquitinationHWVVFKETTLSYYKS
EEEEEEEEEHHHHCC		33.3624816145
383PhosphorylationHWVVFKETTLSYYKS
EEEEEEEEEHHHHCC		33.3628060719
384PhosphorylationWVVFKETTLSYYKSQ
EEEEEEEEHHHHCCC		18.1328060719
385UbiquitinationVVFKETTLSYYKSQD
EEEEEEEHHHHCCCC		3.9629967540
386PhosphorylationVFKETTLSYYKSQDE
EEEEEEHHHHCCCCC		25.0728060719
387UbiquitinationFKETTLSYYKSQDEA
EEEEEHHHHCCCCCC		20.3024816145
387PhosphorylationFKETTLSYYKSQDEA
EEEEEHHHHCCCCCC		20.3028060719
388PhosphorylationKETTLSYYKSQDEAP
EEEEHHHHCCCCCCC		10.7828060719
389UbiquitinationETTLSYYKSQDEAPG
EEEHHHHCCCCCCCC		33.1529967540
390PhosphorylationTTLSYYKSQDEAPGD
EEHHHHCCCCCCCCC		27.0928060719
401UbiquitinationAPGDPIQQLNLKGCE
CCCCCCCCCCCCCCE		32.7929967540
405UbiquitinationPIQQLNLKGCEVVPD
CCCCCCCCCCEECCC		61.5129967540
406UbiquitinationIQQLNLKGCEVVPDV
CCCCCCCCCEECCCC		18.9121890473
410UbiquitinationNLKGCEVVPDVNVSG
CCCCCEECCCCCCCC		1.2421890473
415UbiquitinationEVVPDVNVSGQKFCI
EECCCCCCCCCEEEE		7.3622505724
416PhosphorylationVVPDVNVSGQKFCIK
ECCCCCCCCCEEEEE		30.2429970186
419UbiquitinationDVNVSGQKFCIKLLV
CCCCCCCEEEEEEEE		45.8122505724
419AcetylationDVNVSGQKFCIKLLV
CCCCCCCEEEEEEEE		45.8123749302
423UbiquitinationSGQKFCIKLLVPSPE
CCCEEEEEEEECCCC		36.6322505724
428PhosphorylationCIKLLVPSPEGMSEI
EEEEEECCCCCCCEE		28.2728060719
436PhosphorylationPEGMSEIYLRCQDEQ
CCCCCEEEHEECCHH		5.5322817900
445PhosphorylationRCQDEQQYARWMAGC
EECCHHHHHHHHHHC		9.6028176486
478PhosphorylationQAILAFLSLQRTGSG
HHHHHHHHCCCCCCC		18.9224719451
482PhosphorylationAFLSLQRTGSGGPGN
HHHHCCCCCCCCCCC		23.8023401153
484PhosphorylationLSLQRTGSGGPGNHP
HHCCCCCCCCCCCCC		39.7123401153
497PhosphorylationHPHGPDASAEGLNPY
CCCCCCCCCCCCCCC		33.9428464451
504PhosphorylationSAEGLNPYGLVAPRF
CCCCCCCCCCCCHHH		23.2427155012
514UbiquitinationVAPRFQRKFKAKQLT
CCHHHHHHHHHHHCC		40.2024816145
516MethylationPRFQRKFKAKQLTPR
HHHHHHHHHHHCCHH		58.68116253085
518UbiquitinationFQRKFKAKQLTPRIL
HHHHHHHHHCCHHHH		46.5624816145
563UbiquitinationSYVMVRFKGSRKDEI
EEEEEEECCCCCHHE		45.4724816145
567UbiquitinationVRFKGSRKDEILGIA
EEECCCCCHHEEEEE		62.5024816145
586UbiquitinationIRIDLAVGDVVKTWR
EEEEEECCHHEEEEE		19.1821890473
586 (in isoform 2)Ubiquitination-19.1821890473
590UbiquitinationLAVGDVVKTWRFSNM
EECCHHEEEEECCCC		42.0722817900
590AcetylationLAVGDVVKTWRFSNM
EECCHHEEEEECCCC		42.0726822725
590 (in isoform 1)Ubiquitination-42.0721890473
591PhosphorylationAVGDVVKTWRFSNMR
ECCHHEEEEECCCCC		15.4028450419
595PhosphorylationVVKTWRFSNMRQWNV
HEEEEECCCCCCCCC		22.5727067055
622PhosphorylationEHINVAFSCVSASCR
CCHHHHHHHHHHHHH		12.13-
625PhosphorylationNVAFSCVSASCRIVH
HHHHHHHHHHHHHHH		20.84-
642PhosphorylationIGGYIFLSTRERARG
HCCEEEEEHHHHHCC		18.05-
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 URP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of URP2_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 URP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
PARVB_HUMANPARVBphysical
26344197
NCBP1_HUMANNCBP1physical
26496610
PRDX1_HUMANPRDX1physical
26496610
RBBP5_HUMANRBBP5physical
26496610
STXB1_HUMANSTXBP1physical
26496610
PKP4_HUMANPKP4physical
26496610
TAF1B_HUMANTAF1Bphysical
26496610
COX5A_HUMANCOX5Aphysical
26496610
IF4E2_HUMANEIF4E2physical
26496610
KEAP1_HUMANKEAP1physical
26496610
UBP15_HUMANUSP15physical
26496610
PDCD6_HUMANPDCD6physical
26496610
MINT_HUMANSPENphysical
26496610
U520_HUMANSNRNP200physical
26496610
UH1BL_HUMANUHRF1BP1Lphysical
26496610
RT27_HUMANMRPS27physical
26496610
PRDX5_HUMANPRDX5physical
26496610
KANL2_HUMANKANSL2physical
26496610
KLHL7_HUMANKLHL7physical
26496610
SNIP1_HUMANSNIP1physical
26496610
TB10A_HUMANTBC1D10Aphysical
26496610
UIF_HUMANFYTTD1physical
26496610
PDIP3_HUMANPOLDIP3physical
26496610
ALKB2_HUMANALKBH2physical
26496610
ZCH18_HUMANZC3H18physical
26496610
IPP_HUMANIPPphysical
28514442
FERM2_HUMANFERMT2physical
28514442
ITB3_HUMANITGB3physical
25609252
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612840Leukocyte adhesion deficiency 3 (LAD3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of URP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND TYR-11, AND MASSSPECTROMETRY.
"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 TYR-11 AND TYR-504, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-504, AND MASSSPECTROMETRY.

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