GEMI4_HUMAN - dbPTM
GEMI4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GEMI4_HUMAN
UniProt AC P57678
Protein Name Gem-associated protein 4
Gene Name GEMIN4
Organism Homo sapiens (Human).
Sequence Length 1058
Subcellular Localization Cytoplasm. Nucleus. Nucleus, nucleolus. Nucleus, gem. Localized in subnuclear structures next to coiled bodies, called gems, which are highly enriched in spliceosomal snRNPs and in the nucleolus.
Protein Description The SMN complex plays a catalyst role in the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus..
Protein Sequence MDLGPLNICEEMTILHGGFLLAEQLFHPKALAELTKSDWERVGRPIVEALREISSAAAHSQPFAWKKKALIIIWAKVLQPHPVTPSDTETRWQEDLFFSVGNMIPTINHTILFELLKSLEASGLFIQLLMALPTTICHAELERFLEHVTVDTSAEDVAFFLDVWWEVMKHKGHPQDPLLSQFSAMAHKYLPALDEFPHPPKRLRSDPDACPTMPLLAMLLRGLTQIQSRILGPGRKCCALANLADMLTVFALTEDDPQEVSATVYLDKLATVISVWNSDTQNPYHQQALAEKVKEAERDVSLTSLAKLPSETIFVGCEFLHHLLREWGEELQAVLRSSQGTSYDSYRLCDSLTSFSQNATLYLNRTSLSKEDRQVVSELAECVRDFLRKTSTVLKNRALEDITASIAMAVIQQKMDRHMEVCYIFASEKKWAFSDEWVACLGSNRALFRQPDLVLRLLETVIDVSTADRAIPESQIRQVIHLILECYADLSLPGKNKVLAGILRSWGRKGLSEKLLAYVEGFQEDLNTTFNQLTQSASEQGLAKAVASVARLVIVHPEVTVKKMCSLAVVNLGTHKFLAQILTAFPALRFVEEQGPNSSATFMVSCLKETVWMKFSTPKEEKQFLELLNCLMSPVKPQGIPVAALLEPDEVLKEFVLPFLRLDVEEVDLSLRIFIQTLEANACREEYWLQTCSPFPLLFSLCQLLDRFSKYWQLPKEKRCLSLDRKDLAIHILELLCEIVSANAETFSPDVWIKSLSWLHRKLEQLDWTVGLRLKSFFEGHFKCEVPATLFEICKLSEDEWTSQAHPGYGAGTGLLAWMECCCVSSGISERMLSLLVVDVGNPEEVRLFSKGFLVALVQVMPWCSPQEWQRLHQLTRRLLEKQLLHVPYSLEYIQFVPLLNLKPFAQELQLSVLFLRTFQFLCSHSCRDWLPLEGWNHVVKLLCGSLTRLLDSVRAIQAAGPWVQGPEQDLTQEALFVYTQVFCHALHIMAMLHPEVCEPLYVLALETLTCYETLSKTNPSVSSLLQRAHEQRFLKSIAEGIGPEERRQTLLQKMSSF
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-------MDLGPLNI
-------CCCCCCCC		42.0719413330
13PhosphorylationLNICEEMTILHGGFL
CCCCCCCHHCCCCCH		24.5426503514
36UbiquitinationKALAELTKSDWERVG
HHHHHHCHHHHHHHC		60.0721890473
66AcetylationHSQPFAWKKKALIII
HCCCCCCHHHEEEEE		40.7526051181
66UbiquitinationHSQPFAWKKKALIII
HCCCCCCHHHEEEEE		40.7521890473
68AcetylationQPFAWKKKALIIIWA
CCCCCHHHEEEEEEE		44.7021466224
84PhosphorylationVLQPHPVTPSDTETR
HHCCCCCCCCCCCCC		22.8629255136
86PhosphorylationQPHPVTPSDTETRWQ
CCCCCCCCCCCCCCC		48.0429255136
88PhosphorylationHPVTPSDTETRWQED
CCCCCCCCCCCCCHH		43.5229255136
90PhosphorylationVTPSDTETRWQEDLF
CCCCCCCCCCCHHCE		39.0229255136
188UbiquitinationQFSAMAHKYLPALDE
HHHHHHHHHHHHHCC		38.66-
201UbiquitinationDEFPHPPKRLRSDPD
CCCCCCCCCCCCCCC		69.3921906983
205PhosphorylationHPPKRLRSDPDACPT
CCCCCCCCCCCCCCH		59.0722617229
210GlutathionylationLRSDPDACPTMPLLA
CCCCCCCCCHHHHHH		3.6222555962
212PhosphorylationSDPDACPTMPLLAML
CCCCCCCHHHHHHHH		31.16-
292AcetylationHQQALAEKVKEAERD
HHHHHHHHHHHHHHC		53.6626051181
292UbiquitinationHQQALAEKVKEAERD
HHHHHHHHHHHHHHC		53.6621890473
294UbiquitinationQALAEKVKEAERDVS
HHHHHHHHHHHHCCC		63.37-
301PhosphorylationKEAERDVSLTSLAKL
HHHHHCCCHHHHCCC		30.1621815630
303PhosphorylationAERDVSLTSLAKLPS
HHHCCCHHHHCCCCC		17.7523312004
304PhosphorylationERDVSLTSLAKLPSE
HHCCCHHHHCCCCCC		31.4620873877
341PhosphorylationVLRSSQGTSYDSYRL
HHHHCCCCCCCHHHC		19.2420860994
343PhosphorylationRSSQGTSYDSYRLCD
HHCCCCCCCHHHCHH		14.5620860994
345PhosphorylationSQGTSYDSYRLCDSL
CCCCCCCHHHCHHHC		12.1520860994
346PhosphorylationQGTSYDSYRLCDSLT
CCCCCCHHHCHHHCC		12.5220860994
351PhosphorylationDSYRLCDSLTSFSQN
CHHHCHHHCCHHCCC		32.3330622161
353PhosphorylationYRLCDSLTSFSQNAT
HHCHHHCCHHCCCCE		31.5130622161
354PhosphorylationRLCDSLTSFSQNATL
HCHHHCCHHCCCCEE		28.3525693802
370UbiquitinationLNRTSLSKEDRQVVS
ECCCCCCHHHHHHHH		69.7721906983
377PhosphorylationKEDRQVVSELAECVR
HHHHHHHHHHHHHHH		28.2126074081
389UbiquitinationCVRDFLRKTSTVLKN
HHHHHHHHHHHHHHH		49.31-
390PhosphorylationVRDFLRKTSTVLKNR
HHHHHHHHHHHHHHH		24.1726074081
391PhosphorylationRDFLRKTSTVLKNRA
HHHHHHHHHHHHHHH		21.3926074081
392PhosphorylationDFLRKTSTVLKNRAL
HHHHHHHHHHHHHHH		34.7826074081
3952-HydroxyisobutyrylationRKTSTVLKNRALEDI
HHHHHHHHHHHHHHH		39.80-
395UbiquitinationRKTSTVLKNRALEDI
HHHHHHHHHHHHHHH		39.80-
414UbiquitinationAMAVIQQKMDRHMEV
HHHHHHHHHHHHCEE		26.79-
429UbiquitinationCYIFASEKKWAFSDE
EEEEECCCCCCCCCC		51.63-
430UbiquitinationYIFASEKKWAFSDEW
EEEECCCCCCCCCCH		39.44-
497UbiquitinationLSLPGKNKVLAGILR
CCCCCCCHHHHHHHH		41.95-
536PhosphorylationTFNQLTQSASEQGLA
HHHHHHHHHHHHHHH		28.6430622161
538PhosphorylationNQLTQSASEQGLAKA
HHHHHHHHHHHHHHH		35.3830622161
619UbiquitinationWMKFSTPKEEKQFLE
HHHCCCCHHHHHHHH		77.81-
670PhosphorylationDVEEVDLSLRIFIQT
CHHHHHHHHHHHHHH		15.9024719451
716UbiquitinationSKYWQLPKEKRCLSL
HHHCCCCHHHCCCCC		81.89-
775UbiquitinationWTVGLRLKSFFEGHF
CHHHHHHHHHHCCCC		38.49-
850PhosphorylationPEEVRLFSKGFLVAL
HHHHHHHCCHHHHHH		36.1424719451
1018PhosphorylationCYETLSKTNPSVSSL
HHHHHHCCCCCHHHH		49.3220068231
1021PhosphorylationTLSKTNPSVSSLLQR
HHHCCCCCHHHHHHH		36.3830622161
1023PhosphorylationSKTNPSVSSLLQRAH
HCCCCCHHHHHHHHH		21.4330622161
1024PhosphorylationKTNPSVSSLLQRAHE
CCCCCHHHHHHHHHH		30.8320068231
1036UbiquitinationAHEQRFLKSIAEGIG
HHHHHHHHHHHHCCC		36.78-
1036AcetylationAHEQRFLKSIAEGIG
HHHHHHHHHHHHCCC		36.7826051181
1050PhosphorylationGPEERRQTLLQKMSS
CHHHHHHHHHHHHHC		27.85-
1054UbiquitinationRRQTLLQKMSSF---
HHHHHHHHHHCC---		40.49-
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 GEMI4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GEMI4_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 GEMI4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX20_HUMANDDX20physical
12668731
PP4C_HUMANPPP4Cphysical
12668731
PP4R2_HUMANPPP4R2physical
12668731
LEG1_HUMANLGALS1physical
11522829
LEG3_HUMANLGALS3physical
11522829
DDX20_HUMANDDX20physical
10725331
AGO2_HUMANAGO2physical
11914277
CACO2_HUMANCALCOCO2physical
12869526
CACO2_HUMANCALCOCO2physical
23143396
HDA11_HUMANHDAC11physical
23752268
SMN_HUMANSMN1physical
23752268
DDX20_HUMANDDX20physical
23752268
GEMI4_HUMANGEMIN4physical
23752268
DICER_HUMANDICER1physical
23752268
MORC4_HUMANMORC4physical
21988832
SQSTM_HUMANSQSTM1physical
21988832
SPY1_HUMANSPRY1physical
21988832
PIAS3_HUMANPIAS3physical
21988832
SRRT_HUMANSRRTphysical
21988832
GLYR1_HUMANGLYR1physical
21988832
NUFP1_HUMANNUFIP1physical
26275778
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 GEMI4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-205, AND MASSSPECTROMETRY.

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