LARP7_HUMAN - dbPTM
LARP7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LARP7_HUMAN
UniProt AC Q4G0J3
Protein Name La-related protein 7
Gene Name LARP7
Organism Homo sapiens (Human).
Sequence Length 582
Subcellular Localization Nucleus, nucleoplasm .
Protein Description Negative transcriptional regulator of polymerase II genes, acting by means of the 7SK RNP system. Within the 7SK RNP complex, the positive transcription elongation factor b (P-TEFb) is sequestered in an inactive form, preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation..
Protein Sequence METESGNQEKVMEEESTEKKKEVEKKKRSRVKQVLADIAKQVDFWFGDANLHKDRFLREQIEKSRDGYVDISLLVSFNKMKKLTTDGKLIARALRSSAVVELDLEGTRIRRKKPLGERPKDEDERTVYVELLPKNVNHSWIERVFGKCGNVVYISIPHYKSTGDPKGFAFVEFETKEQAAKAIEFLNNPPEEAPRKPGIFPKTVKNKPIPALRVVEEKKKKKKKKGRMKKEDNIQAKEENMDTSNTSISKMKRSRPTSEGSDIESTEPQKQCSKKKKKRDRVEASSLPEVRTGKRKRSSSEDAESLAPRSKVKKIIQKDIIKEASEASKENRDIEISTEEEKDTGDLKDSSLLKTKRKHKKKHKERHKMGEEVIPLRVLSKSEWMDLKKEYLALQKASMASLKKTISQIKSESEMETDSGVPQNTGMKNEKTANREECRTQEKVNATGPQFVSGVIVKIISTEPLPGRKQVRDTLAAISEVLYVDLLEGDTECHARFKTPEDAQAVINAYTEINKKHCWKLEILSGDHEQRYWQKILVDRQAKLNQPREKKRGTEKLITKAEKIRLAKTQQASKHIRFSEYD
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
1Acetylation-------METESGNQ
-------CCCCCCCH		15.0522814378
3Phosphorylation-----METESGNQEK
-----CCCCCCCHHH		33.8729116813
5Phosphorylation---METESGNQEKVM
---CCCCCCCHHHHC		50.9229116813
10 (in isoform 3)Phosphorylation-36.8029116813
16PhosphorylationEKVMEEESTEKKKEV
HHHCCHHHHHHHHHH		45.1829116813
17PhosphorylationKVMEEESTEKKKEVE
HHCCHHHHHHHHHHH		55.9229116813
23PhosphorylationSTEKKKEVEKKKRSR
HHHHHHHHHHHHHHH		21.0027251275
68PhosphorylationIEKSRDGYVDISLLV
HHHCCCCCCEEEEEE		10.1529083192
72PhosphorylationRDGYVDISLLVSFNK
CCCCCEEEEEEECHH		15.9329083192
76PhosphorylationVDISLLVSFNKMKKL
CEEEEEEECHHCCCC		24.0729083192
84O-linked_GlycosylationFNKMKKLTTDGKLIA
CHHCCCCCCCHHHHH		31.5530379171
84PhosphorylationFNKMKKLTTDGKLIA
CHHCCCCCCCHHHHH		31.55-
85PhosphorylationNKMKKLTTDGKLIAR
HHCCCCCCCHHHHHH		53.87-
88AcetylationKKLTTDGKLIARALR
CCCCCCHHHHHHHHH		39.2627452117
96PhosphorylationLIARALRSSAVVELD
HHHHHHHCCCEEEEE		24.4123312004
97PhosphorylationIARALRSSAVVELDL
HHHHHHCCCEEEEEC		20.7423312004
107PhosphorylationVELDLEGTRIRRKKP
EEEECCCCEEEECCC		17.3423312004
120UbiquitinationKPLGERPKDEDERTV
CCCCCCCCCCCCCEE		78.8324816145
127UbiquitinationKDEDERTVYVELLPK
CCCCCCEEEEEECCC		6.7124816145
128PhosphorylationDEDERTVYVELLPKN
CCCCCEEEEEECCCC		6.39-
139PhosphorylationLPKNVNHSWIERVFG
CCCCCCHHHHHHHHC		25.2524719451
147AcetylationWIERVFGKCGNVVYI
HHHHHHCCCCCEEEE		27.7526051181
171UbiquitinationDPKGFAFVEFETKEQ
CCCCEEEEEEECHHH		8.0532015554
220PhosphorylationRVVEEKKKKKKKKGR
HHHHHHHHHHHCCCC		79.4933259812
229AcetylationKKKKGRMKKEDNIQA
HHCCCCCCHHHHHHH		52.217711307
237SumoylationKEDNIQAKEENMDTS
HHHHHHHHHHCCCCC		49.5428112733
243PhosphorylationAKEENMDTSNTSISK
HHHHCCCCCCCHHHH		17.0725159151
244PhosphorylationKEENMDTSNTSISKM
HHHCCCCCCCHHHHH		33.5725159151
246PhosphorylationENMDTSNTSISKMKR
HCCCCCCCHHHHHHH		27.4925159151
247PhosphorylationNMDTSNTSISKMKRS
CCCCCCCHHHHHHHC		29.1725159151
249PhosphorylationDTSNTSISKMKRSRP
CCCCCHHHHHHHCCC		26.8528450419
249UbiquitinationDTSNTSISKMKRSRP
CCCCCHHHHHHHCCC		26.8532015554
250UbiquitinationTSNTSISKMKRSRPT
CCCCHHHHHHHCCCC		46.9332015554
253PhosphorylationTSISKMKRSRPTSEG
CHHHHHHHCCCCCCC		34.1127251275
254PhosphorylationSISKMKRSRPTSEGS
HHHHHHHCCCCCCCC		36.7725159151
257PhosphorylationKMKRSRPTSEGSDIE
HHHHCCCCCCCCCCC		38.0029255136
257UbiquitinationKMKRSRPTSEGSDIE
HHHHCCCCCCCCCCC		38.0032015554
258PhosphorylationMKRSRPTSEGSDIES
HHHCCCCCCCCCCCC		42.5129255136
259PhosphorylationKRSRPTSEGSDIEST
HHCCCCCCCCCCCCC		66.2632645325
261PhosphorylationSRPTSEGSDIESTEP
CCCCCCCCCCCCCCC		31.2229255136
265PhosphorylationSEGSDIESTEPQKQC
CCCCCCCCCCCHHHH		38.1022167270
266PhosphorylationEGSDIESTEPQKQCS
CCCCCCCCCCHHHHC		38.6022167270
268PhosphorylationSDIESTEPQKQCSKK
CCCCCCCCHHHHCCC		46.9227251275
269UbiquitinationDIESTEPQKQCSKKK
CCCCCCCHHHHCCCC		42.0732015554
270UbiquitinationIESTEPQKQCSKKKK
CCCCCCHHHHCCCCH		65.08-
273PhosphorylationTEPQKQCSKKKKKRD
CCCHHHHCCCCHHHH		45.0423927012
275UbiquitinationPQKQCSKKKKKRDRV
CHHHHCCCCHHHHHH		54.2333845483
285PhosphorylationKRDRVEASSLPEVRT
HHHHHHHHCCCCHHC		20.9229255136
286PhosphorylationRDRVEASSLPEVRTG
HHHHHHHCCCCHHCC		55.8029255136
292PhosphorylationSSLPEVRTGKRKRSS
HCCCCHHCCCCCCCC		52.8328555341
293PhosphorylationSLPEVRTGKRKRSSS
CCCCHHCCCCCCCCH		19.7327251275
298PhosphorylationRTGKRKRSSSEDAES
HCCCCCCCCHHHHHH		41.0529255136
299PhosphorylationTGKRKRSSSEDAESL
CCCCCCCCHHHHHHH		41.6029255136
300PhosphorylationGKRKRSSSEDAESLA
CCCCCCCHHHHHHHC		40.5229255136
305PhosphorylationSSSEDAESLAPRSKV
CCHHHHHHHCCHHHH		31.3929255136
306PhosphorylationSSEDAESLAPRSKVK
CHHHHHHHCCHHHHH		5.9933259812
307PhosphorylationSEDAESLAPRSKVKK
HHHHHHHCCHHHHHH		13.5127251275
310PhosphorylationAESLAPRSKVKKIIQ
HHHHCCHHHHHHHHH		40.5222210691
318AcetylationKVKKIIQKDIIKEAS
HHHHHHHHHHHHHHH		40.2523954790
325AcetylationKDIIKEASEASKENR
HHHHHHHHHHHHHHC		34.4819608861
337PhosphorylationENRDIEISTEEEKDT
HHCCCCCCCCCCCCC		19.5829255136
338PhosphorylationNRDIEISTEEEKDTG
HCCCCCCCCCCCCCC		53.7529255136
344PhosphorylationSTEEEKDTGDLKDSS
CCCCCCCCCCCCCCH		43.6029255136
345PhosphorylationTEEEKDTGDLKDSSL
CCCCCCCCCCCCCHH		48.6832645325
347UbiquitinationEEKDTGDLKDSSLLK
CCCCCCCCCCCHHHH		7.6032015554
348UbiquitinationEKDTGDLKDSSLLKT
CCCCCCCCCCHHHHH		61.3732015554
350PhosphorylationDTGDLKDSSLLKTKR
CCCCCCCCHHHHHHH		22.6930266825
351PhosphorylationTGDLKDSSLLKTKRK
CCCCCCCHHHHHHHH		48.1030266825
353UbiquitinationDLKDSSLLKTKRKHK
CCCCCHHHHHHHHHH		7.7633845483
354AcetylationLKDSSLLKTKRKHKK
CCCCHHHHHHHHHHH		58.2419818023
354UbiquitinationLKDSSLLKTKRKHKK
CCCCHHHHHHHHHHH		58.2433845483
355UbiquitinationKDSSLLKTKRKHKKK
CCCHHHHHHHHHHHH		35.7332015554
358PhosphorylationSLLKTKRKHKKKHKE
HHHHHHHHHHHHHHH		62.4227251275
360UbiquitinationLKTKRKHKKKHKERH
HHHHHHHHHHHHHHH		67.5632015554
361UbiquitinationKTKRKHKKKHKERHK
HHHHHHHHHHHHHHC		60.8833845483
366UbiquitinationHKKKHKERHKMGEEV
HHHHHHHHHCCCCCC		39.2633845483
367UbiquitinationKKKHKERHKMGEEVI
HHHHHHHHCCCCCCC		26.0833845483
391PhosphorylationWMDLKKEYLALQKAS
HCHHHHHHHHHHHHH		13.2223532336
398PhosphorylationYLALQKASMASLKKT
HHHHHHHHHHHHHHH		23.1623532336
405PhosphorylationSMASLKKTISQIKSE
HHHHHHHHHHHHHCH		25.0329496963
407PhosphorylationASLKKTISQIKSESE
HHHHHHHHHHHCHHH		30.9629496963
410SumoylationKKTISQIKSESEMET
HHHHHHHHCHHHHCC		40.3028112733
411PhosphorylationKTISQIKSESEMETD
HHHHHHHCHHHHCCC		48.2425159151
413PhosphorylationISQIKSESEMETDSG
HHHHHCHHHHCCCCC		49.7025159151
417PhosphorylationKSESEMETDSGVPQN
HCHHHHCCCCCCCCC		33.8720068231
418PhosphorylationSESEMETDSGVPQNT
CHHHHCCCCCCCCCC		30.0427251275
419PhosphorylationESEMETDSGVPQNTG
HHHHCCCCCCCCCCC		49.4630576142
425PhosphorylationDSGVPQNTGMKNEKT
CCCCCCCCCCCCHHH		33.1520068231
428AcetylationVPQNTGMKNEKTANR
CCCCCCCCCHHHCCH		64.4023954790
431AcetylationNTGMKNEKTANREEC
CCCCCCHHHCCHHHH		63.4325953088
436UbiquitinationNEKTANREECRTQEK
CHHHCCHHHHHHHHH		62.3432015554
447PhosphorylationTQEKVNATGPQFVSG
HHHHHHCCCCCEECE		44.16-
453PhosphorylationATGPQFVSGVIVKII
CCCCCEECEEEEEEE		28.73-
461PhosphorylationGVIVKIISTEPLPGR
EEEEEEEECCCCCCC		30.14-
462PhosphorylationVIVKIISTEPLPGRK
EEEEEEECCCCCCCH		31.08-
514UbiquitinationINAYTEINKKHCWKL
HHHHHHHCHHHEEEE		40.8832015554
515AcetylationNAYTEINKKHCWKLE
HHHHHHCHHHEEEEE		49.9425953088
515UbiquitinationNAYTEINKKHCWKLE
HHHHHHCHHHEEEEE		49.9432015554
522UbiquitinationKKHCWKLEILSGDHE
HHHEEEEEEECCCHH		37.8532015554
527UbiquitinationKLEILSGDHEQRYWQ
EEEEECCCHHHHHHH		38.4832015554
528UbiquitinationLEILSGDHEQRYWQK
EEEECCCHHHHHHHH		36.2932015554
554PhosphorylationPREKKRGTEKLITKA
CHHHHCCHHHHHHHH		33.7020068231
574AcetylationAKTQQASKHIRFSEY
HHHHHHHHCCCCCCC		46.1719608861
579PhosphorylationASKHIRFSEYD----
HHHCCCCCCCC----		25.9524247654
581AcetylationKHIRFSEYD------
HCCCCCCCC------		26.2519608861
581PhosphorylationKHIRFSEYD------
HCCCCCCCC------		26.2527251275
586PhosphorylationSEYD-----------
CCCC-----------		27251275
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 LARP7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LARP7_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 LARP7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
RS16_HUMANRPS16physical
18483487
CDK9_HUMANCDK9physical
18483487
HEXI1_HUMANHEXIM1physical
18483487
CCNT1_HUMANCCNT1physical
18483487
MEPCE_HUMANMEPCEphysical
18483487
ROA1_HUMANHNRNPA1physical
18483487
JMJD6_HUMANJMJD6physical
23455924
CDK9_HUMANCDK9physical
24367103
CCNT1_HUMANCCNT1physical
24367103
AFF1_HUMANAFF1physical
24367103
HEXI1_HUMANHEXIM1physical
24367103
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615071Alazami syndrome (ALAZS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LARP7_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-574, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-337 AND THR-338, ANDMASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND MASSSPECTROMETRY.
"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-254; THR-257; SER-258;SER-261; SER-265 AND SER-300, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-338, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-257; SER-258; SER-261;SER-273; SER-337 AND THR-338, AND MASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-337 AND THR-338, ANDMASS SPECTROMETRY.

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