GIMA4_HUMAN - dbPTM
GIMA4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GIMA4_HUMAN
UniProt AC Q9NUV9
Protein Name GTPase IMAP family member 4
Gene Name GIMAP4
Organism Homo sapiens (Human).
Sequence Length 329
Subcellular Localization Cytoplasm, cytosol .
Protein Description May play a role in regulating lymphocyte apoptosis (By similarity). Exhibits intrisinic GTPase activity. Shows a higher affinity for GDP over GTP (about 12-fold higher), and binding shows an absolute requirement for magnesium..
Protein Sequence MAAQYGSMSFNPSTPGASYGPGRQEPRNSQLRIVLVGKTGAGKSATGNSILGRKVFHSGTAAKSITKKCEKRSSSWKETELVVVDTPGIFDTEVPNAETSKEIIRCILLTSPGPHALLLVVPLGRYTEEEHKATEKILKMFGERARSFMILIFTRKDDLGDTNLHDYLREAPEDIQDLMDIFGDRYCALNNKATGAEQEAQRAQLLGLIQRVVRENKEGCYTNRMYQRAEEEIQKQTQAMQELHRVELEREKARIREEYEEKIRKLEDKVEQEKRKKQMEKKLAEQEAHYAVRQQRARTEVESKDGILELIMTALQIASFILLRLFAED
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
5Phosphorylation---MAAQYGSMSFNP
---CCCCCCCCCCCC		13.3628857561
7Phosphorylation-MAAQYGSMSFNPST
-CCCCCCCCCCCCCC		13.3028857561
9PhosphorylationAAQYGSMSFNPSTPG
CCCCCCCCCCCCCCC		24.4628857561
13PhosphorylationGSMSFNPSTPGASYG
CCCCCCCCCCCCCCC		48.6223401153
14PhosphorylationSMSFNPSTPGASYGP
CCCCCCCCCCCCCCC		27.3128857561
19PhosphorylationPSTPGASYGPGRQEP
CCCCCCCCCCCCCCC		27.14-
38UbiquitinationLRIVLVGKTGAGKSA
EEEEEEECCCCCCCC		35.98-
39PhosphorylationRIVLVGKTGAGKSAT
EEEEEECCCCCCCCC		26.7424905233
43UbiquitinationVGKTGAGKSATGNSI
EECCCCCCCCCCCCC		36.06-
49PhosphorylationGKSATGNSILGRKVF
CCCCCCCCCCCCHHC		22.1223401153
54UbiquitinationGNSILGRKVFHSGTA
CCCCCCCHHCCCCCH		47.67-
58PhosphorylationLGRKVFHSGTAAKSI
CCCHHCCCCCHHHHH		26.7823312004
60PhosphorylationRKVFHSGTAAKSITK
CHHCCCCCHHHHHHH		26.8523312004
63AcetylationFHSGTAAKSITKKCE
CCCCCHHHHHHHHHH		39.6725953088
63UbiquitinationFHSGTAAKSITKKCE
CCCCCHHHHHHHHHH		39.67-
67AcetylationTAAKSITKKCEKRSS
CHHHHHHHHHHHCCC		54.48130439
71AcetylationSITKKCEKRSSSWKE
HHHHHHHHCCCCCCC		68.03130443
77UbiquitinationEKRSSSWKETELVVV
HHCCCCCCCCEEEEE		57.62-
111PhosphorylationIRCILLTSPGPHALL
HHHHHHCCCCCCEEE		28.0330576142
134PhosphorylationTEEEHKATEKILKMF
CHHHHHHHHHHHHHH		42.48-
147PhosphorylationMFGERARSFMILIFT
HHHHHHHCEEEEEEE		20.4127732954
179SulfoxidationPEDIQDLMDIFGDRY
CHHHHHHHHHHHHHH		5.1021406390
192UbiquitinationRYCALNNKATGAEQE
HHHHHCCCCCCHHHH		46.37-
217UbiquitinationQRVVRENKEGCYTNR
HHHHHHCCCCCCHHH		51.21-
226PhosphorylationGCYTNRMYQRAEEEI
CCCHHHHHHHHHHHH		7.51-
235UbiquitinationRAEEEIQKQTQAMQE
HHHHHHHHHHHHHHH		62.06-
237PhosphorylationEEEIQKQTQAMQELH
HHHHHHHHHHHHHHH		25.90-
252UbiquitinationRVELEREKARIREEY
HHHHHHHHHHHHHHH		49.54-
259PhosphorylationKARIREEYEEKIRKL
HHHHHHHHHHHHHHH		25.3325839225
262AcetylationIREEYEEKIRKLEDK
HHHHHHHHHHHHHHH		35.5523749302
262UbiquitinationIREEYEEKIRKLEDK
HHHHHHHHHHHHHHH		35.5519608861
269AcetylationKIRKLEDKVEQEKRK
HHHHHHHHHHHHHHH		37.9919828523
282UbiquitinationRKKQMEKKLAEQEAH
HHHHHHHHHHHHHHH		39.35-
290PhosphorylationLAEQEAHYAVRQQRA
HHHHHHHHHHHHHHH		17.5329978859
290NitrationLAEQEAHYAVRQQRA
HHHHHHHHHHHHHHH		17.53-
303PhosphorylationRARTEVESKDGILEL
HHHCHHHCCHHHHHH		41.0224719451
313PhosphorylationGILELIMTALQIASF
HHHHHHHHHHHHHHH		19.7524719451
319PhosphorylationMTALQIASFILLRLF
HHHHHHHHHHHHHHH		17.9124719451
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 GIMA4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GIMA4_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 GIMA4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
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 GIMA4_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-262, AND MASS SPECTROMETRY.

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