STRBP_HUMAN - dbPTM
STRBP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STRBP_HUMAN
UniProt AC Q96SI9
Protein Name Spermatid perinuclear RNA-binding protein
Gene Name STRBP
Organism Homo sapiens (Human).
Sequence Length 672
Subcellular Localization Cytoplasm. Microtubule-associated that localizes to the manchette in developing spermatids..
Protein Description Involved in spermatogenesis and sperm function. Plays a role in regulation of cell growth. Binds to double-stranded DNA and RNA. Binds most efficiently to poly(I:C) RNA than to poly(dI:dC) DNA. Binds also to single-stranded poly(G) RNA. Binds non-specifically to the mRNA PRM1 3'-UTR and adenovirus VA RNA (By similarity)..
Protein Sequence MRSIRSFANDDRHVMVKHSTIYPSPEELEAVQNMVSTVECALKHVSDWLDETNKGTKTEGETEVKKDEAGENYSKDQGGRTLCGVMRIGLVAKGLLIKDDMDLELVLMCKDKPTETLLNTVKDNLPIQIQKLTEEKYQVEQCVNEASIIIRNTKEPTLTLKVILTSPLIRDELEKKDGENVSMKDPPDLLDRQKCLNALASLRHAKWFQARANGLKSCVIVLRILRDLCNRVPTWAPLKGWPLELICEKSIGTCNRPLGAGEALRRVMECLASGILLPGGPGLHDPCERDPTDALSYMTIQQKEDITHSAQHALRLSAFGQIYKVLEMDPLPSSKPFQKYSWSVTDKEGAGSSALKRPFEDGLGDDKDPNKKMKRNLRKILDSKAIDLMNALMRLNQIRPGLQYKLLSQSGPVHAPVFTMSVDVDGTTYEASGPSKKTAKLHVAVKVLQAMGYPTGFDADIECMSSDEKSDNESKNETVSSNSSNNTGNSTTETSSTLEVRTQGPILTASGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFRGAGPNKKVAKASAALAALEKLFSGPNAANNKKKKIIPQAKGVVNTAVSAAVQAVRGRGRGTLTRGAFVGATAAPGYIAPGYGTPYGYSTAAPAYGLPKRMVLLPVMKFPTYPVPHYSFF
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-----MRSIRSFAND
-----CCCHHHHCCC		22.5125404012
5 (in isoform 2)Phosphorylation-27.2822210691
6 (in isoform 2)Phosphorylation-27.3422210691
6Phosphorylation--MRSIRSFANDDRH
--CCCHHHHCCCCCE		27.3425404012
38 (in isoform 2)Phosphorylation-4.4122210691
42 (in isoform 2)Phosphorylation-6.2722210691
65AcetylationTEGETEVKKDEAGEN
CCCCEEEECCCCCCC		48.5526051181
73PhosphorylationKDEAGENYSKDQGGR
CCCCCCCCCCCCCCC		16.8820068231
74PhosphorylationDEAGENYSKDQGGRT
CCCCCCCCCCCCCCE		41.1420068231
81PhosphorylationSKDQGGRTLCGVMRI
CCCCCCCEECHHHHH		29.6720068231
112AcetylationLVLMCKDKPTETLLN
EEEEECCCCCHHHHH		39.0625953088
122UbiquitinationETLLNTVKDNLPIQI
HHHHHHHHHCCCCCH		38.57-
165PhosphorylationLTLKVILTSPLIRDE
EEEEEEECCHHHHHH		19.7121406692
166PhosphorylationTLKVILTSPLIRDEL
EEEEEECCHHHHHHH		17.7924719451
182PhosphorylationKKDGENVSMKDPPDL
HCCCCCCCCCCCCCC		31.5328555341
183SulfoxidationKDGENVSMKDPPDLL
CCCCCCCCCCCCCCC		5.0621406390
192AcetylationDPPDLLDRQKCLNAL
CCCCCCCHHHHHHHH		37.5219608861
201PhosphorylationKCLNALASLRHAKWF
HHHHHHHHHHHHHHH		27.1324719451
206UbiquitinationLASLRHAKWFQARAN
HHHHHHHHHHHHHHC		42.2719608861
206AcetylationLASLRHAKWFQARAN
HHHHHHHHHHHHHHC		42.2719608861
216MalonylationQARANGLKSCVIVLR
HHHHCCHHHHHHHHH		43.1126320211
216UbiquitinationQARANGLKSCVIVLR
HHHHCCHHHHHHHHH		43.11-
216AcetylationQARANGLKSCVIVLR
HHHHCCHHHHHHHHH		43.1125953088
273PhosphorylationRVMECLASGILLPGG
HHHHHHHHCCCCCCC		17.2621130716
325 (in isoform 2)Ubiquitination-2.8421890473
335AcetylationMDPLPSSKPFQKYSW
CCCCCCCCCCCCCEE		54.9426051181
335UbiquitinationMDPLPSSKPFQKYSW
CCCCCCCCCCCCCEE		54.94-
339UbiquitinationPSSKPFQKYSWSVTD
CCCCCCCCCEEEECC		41.4521890473
339 (in isoform 1)Ubiquitination-41.4521890473
341PhosphorylationSKPFQKYSWSVTDKE
CCCCCCCEEEECCCC		21.6521815630
343PhosphorylationPFQKYSWSVTDKEGA
CCCCCEEEECCCCCC		14.8121815630
345PhosphorylationQKYSWSVTDKEGAGS
CCCEEEECCCCCCCC		35.5223186163
347UbiquitinationYSWSVTDKEGAGSSA
CEEEECCCCCCCCCC		49.00-
367AcetylationEDGLGDDKDPNKKMK
CCCCCCCCCCCHHHH		78.7226051181
371AcetylationGDDKDPNKKMKRNLR
CCCCCCCHHHHHHHH		60.6826051181
384UbiquitinationLRKILDSKAIDLMNA
HHHHHHHHHHHHHHH		49.37-
405MethylationIRPGLQYKLLSQSGP
CCCCHHHHHHHCCCC		29.95-
408PhosphorylationGLQYKLLSQSGPVHA
CHHHHHHHCCCCCCC		32.5128111955
410PhosphorylationQYKLLSQSGPVHAPV
HHHHHHCCCCCCCCE		41.5128111955
427PhosphorylationMSVDVDGTTYEASGP
EEEECCCCEEEECCC		23.0328111955
428PhosphorylationSVDVDGTTYEASGPS
EEECCCCEEEECCCC		25.5428111955
429PhosphorylationVDVDGTTYEASGPSK
EECCCCEEEECCCCH		14.8828111955
432PhosphorylationDGTTYEASGPSKKTA
CCCEEEECCCCHHHC		39.0228111955
435PhosphorylationTYEASGPSKKTAKLH
EEEECCCCHHHCHHH		50.7628111955
440UbiquitinationGPSKKTAKLHVAVKV
CCCHHHCHHHHHHHH		44.34-
453PhosphorylationKVLQAMGYPTGFDAD
HHHHHCCCCCCCCCC		5.6423663014
455PhosphorylationLQAMGYPTGFDADIE
HHHCCCCCCCCCCEE		41.8323663014
465PhosphorylationDADIECMSSDEKSDN
CCCEEECCCCCCCCC		46.4225159151
466PhosphorylationADIECMSSDEKSDNE
CCEEECCCCCCCCCC		23.9425159151
470PhosphorylationCMSSDEKSDNESKNE
ECCCCCCCCCCCCCC		43.5522617229
474PhosphorylationDEKSDNESKNETVSS
CCCCCCCCCCCCCCC		47.2222617229
478PhosphorylationDNESKNETVSSNSSN
CCCCCCCCCCCCCCC		34.7728450419
480PhosphorylationESKNETVSSNSSNNT
CCCCCCCCCCCCCCC		31.0828450419
481PhosphorylationSKNETVSSNSSNNTG
CCCCCCCCCCCCCCC		36.0728450419
483PhosphorylationNETVSSNSSNNTGNS
CCCCCCCCCCCCCCC		36.0725627689
484PhosphorylationETVSSNSSNNTGNST
CCCCCCCCCCCCCCC		38.0525627689
487PhosphorylationSSNSSNNTGNSTTET
CCCCCCCCCCCCCCC		41.8325627689
492PhosphorylationNNTGNSTTETSSTLE
CCCCCCCCCCCCEEE		36.7727251275
494PhosphorylationTGNSTTETSSTLEVR
CCCCCCCCCCEEEEE		26.3627251275
495PhosphorylationGNSTTETSSTLEVRT
CCCCCCCCCEEEEEE		18.3327251275
496PhosphorylationNSTTETSSTLEVRTQ
CCCCCCCCEEEEEEC		44.4227251275
497PhosphorylationSTTETSSTLEVRTQG
CCCCCCCEEEEEECC		27.0627251275
508PhosphorylationRTQGPILTASGKNPV
EECCCEEEECCCCCC		21.3522985185
510PhosphorylationQGPILTASGKNPVME
CCCEEEECCCCCCCH		45.1025627689
512 (in isoform 2)Ubiquitination-56.4321890473
526 (in isoform 1)Ubiquitination-39.2321890473
526UbiquitinationNEKRRGLKYELISET
HHHHCCCCEEEEECC		39.2321890473
527PhosphorylationEKRRGLKYELISETG
HHHCCCCEEEEECCC		22.4728152594
531PhosphorylationGLKYELISETGGSHD
CCCEEEEECCCCCCC		41.5528555341
533PhosphorylationKYELISETGGSHDKR
CEEEEECCCCCCCCE		39.8025159151
536PhosphorylationLISETGGSHDKRFVM
EEECCCCCCCCEEEE		29.8327251275
539UbiquitinationETGGSHDKRFVMEVE
CCCCCCCCEEEEEEE		42.17-
565PhosphorylationNKKVAKASAALAALE
CHHHHHHHHHHHHHH		17.2320068231
576PhosphorylationAALEKLFSGPNAANN
HHHHHHHCCCCCCCC		64.8725159151
608DimethylationSAAVQAVRGRGRGTL
HHHHHHHHCCCCCCC		31.91-
608MethylationSAAVQAVRGRGRGTL
HHHHHHHHCCCCCCC		31.9154559719
610MethylationAVQAVRGRGRGTLTR
HHHHHHCCCCCCCCC		22.5254559727
612MethylationQAVRGRGRGTLTRGA
HHHHCCCCCCCCCCC		33.3080702745
612Asymmetric dimethylarginineQAVRGRGRGTLTRGA
HHHHCCCCCCCCCCC		33.30-
614PhosphorylationVRGRGRGTLTRGAFV
HHCCCCCCCCCCCEE		24.4828787133
617MethylationRGRGTLTRGAFVGAT
CCCCCCCCCCEECCC		37.24115391841
617Asymmetric dimethylarginineRGRGTLTRGAFVGAT
CCCCCCCCCCEECCC		37.24-
634PhosphorylationPGYIAPGYGTPYGYS
CCEECCCCCCCCCCC		19.43-
652MethylationPAYGLPKRMVLLPVM
CCCCCCCCEEEEEEC		20.64115917985
669PhosphorylationPTYPVPHYSFF----
CCCCCCCCCCC----		10.9125159151
670PhosphorylationTYPVPHYSFF-----
CCCCCCCCCC-----		19.6925627689
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 STRBP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STRBP_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 STRBP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNRPR_HUMANHNRNPRphysical
28514442
ILF2_HUMANILF2physical
28514442
ELAV2_HUMANELAVL2physical
28514442
PUM2_HUMANPUM2physical
28514442
RT11_HUMANMRPS11physical
28514442
RT34_HUMANMRPS34physical
28514442
RALY_HUMANRALYphysical
28514442
STAU2_HUMANSTAU2physical
28514442
RT27_HUMANMRPS27physical
28514442
KLK6_HUMANKLK6physical
28514442
DICER_HUMANDICER1physical
28514442
TRBP2_HUMANTARBP2physical
28514442
RENT1_HUMANUPF1physical
28514442
NGRN_HUMANNGRNphysical
28514442
RT15_HUMANMRPS15physical
28514442
ROA1_HUMANHNRNPA1physical
28514442
RT09_HUMANMRPS9physical
28514442
PRKRA_HUMANPRKRAphysical
28514442
LARP1_HUMANLARP1physical
28514442
RU17_HUMANSNRNP70physical
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 STRBP_HUMAN

loading...

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-465; SER-466 ANDSER-470, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory