RHG44_HUMAN - dbPTM
RHG44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RHG44_HUMAN
UniProt AC Q17R89
Protein Name Rho GTPase-activating protein 44
Gene Name ARHGAP44
Organism Homo sapiens (Human).
Sequence Length 818
Subcellular Localization Cell projection, dendritic spine. Recycling endosome. Cell junction, synapse. In CA1 hippocampal synapses, detected at both presynaptic and postsynaptic sites..
Protein Description GTPase-activating protein (GAP) that stimulates the GTPase activity of Rho-type GTPases. Thereby, controls Rho-type GTPases cycling between their active GTP-bound and inactive GDP-bound states. May act as a GAP for CDC42 and RAC1. Endosomal recycling protein which, in association with SHANK3, is involved in synaptic plasticity. Promotes GRIA1 exocytosis from recycling endosomes and spine morphological changes associated to long-term potentiation..
Protein Sequence MKKQFNRMRQLANQTVGRAEKTEVLSEDLLQVEKRLELVKQVSHSTHKKLTACLQGQQGAEADKRSKKLPLTTLAQCLMEGSAILGDDTLLGKMLKLCGETEDKLAQELIHFELQVERDVIEPLFLLAEVEIPNIQKQRKHLAKLVLDMDSSRTRWQQTSKSSGLSSSLQPAGAKADALREEMEEAANRVEICRDQLSADMYSFVAKEIDYANYFQTLIEVQAEYHRKSLTLLQAVLPQIKAQQEAWVEKPSFGKPLEEHLTISGREIAFPIEACVTMLLECGMQEEGLFRVAPSASKLKKLKAALDCCVVDVQEYSADPHAIAGALKSYLRELPEPLMTFELYDEWIQASNVQEQDKKLQALWNACEKLPKANHNNIRYLIKFLSKLSEYQDVNKMTPSNMAIVLGPNLLWPQAEGNITEMMTTVSLQIVGIIEPIIQHADWFFPGEIEFNITGNYGSPVHVNHNANYSSMPSPDMDPADRRQPEQARRPLSVATDNMMLEFYKKDGLRKIQSMGVRVMDTNWVARRGSSAGRKVSCAPPSMQPPAPPAELAAPLPSPLPEQPLDSPAAPALSPSGLGLQPGPERTSTTKSKELSPGSAQKGSPGSSQGTACAGTQPGAQPGAQPGASPSPSQPPADQSPHTLRKVSKKLAPIPPKVPFGQPGAMADQSAGQPSPVSLSPTPPSTPSPYGLSYPQGYSLASGQLSPAAAPPLASPSVFTSTLSKSRPTPKPRQRPTLPPPQPPTVNLSASSPQSTEAPMLDGMSPGESMSTDLVHFDIPSIHIELGSTLRLSPLEHMRRHSVTDKRDSEEESESTAL
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
3Methylation-----MKKQFNRMRQ
-----CHHHHHHHHH		59.84-
15PhosphorylationMRQLANQTVGRAEKT
HHHHHHHHCCCHHHH		25.4129214152
26PhosphorylationAEKTEVLSEDLLQVE
HHHHHHCCHHHHHHH		33.95-
162PhosphorylationRWQQTSKSSGLSSSL
HHHHHHHHCCCCCCC		29.4328450419
163PhosphorylationWQQTSKSSGLSSSLQ
HHHHHHHCCCCCCCC		47.7128450419
166PhosphorylationTSKSSGLSSSLQPAG
HHHHCCCCCCCCCCC		22.7728450419
167PhosphorylationSKSSGLSSSLQPAGA
HHHCCCCCCCCCCCH		39.8628450419
168PhosphorylationKSSGLSSSLQPAGAK
HHCCCCCCCCCCCHH		27.8728450419
493PhosphorylationEQARRPLSVATDNMM
HHHCCCCCHHCCCHH		16.6428450419
496PhosphorylationRRPLSVATDNMMLEF
CCCCCHHCCCHHEEH		26.2528122231
504PhosphorylationDNMMLEFYKKDGLRK
CCHHEEHHHHHCHHH		14.04-
514PhosphorylationDGLRKIQSMGVRVMD
HCHHHHHHCCEEEEC		22.4523403867
589PhosphorylationPGPERTSTTKSKELS
CCCCCCCCCCCCCCC		37.32-
590PhosphorylationGPERTSTTKSKELSP
CCCCCCCCCCCCCCC		32.84-
596PhosphorylationTTKSKELSPGSAQKG
CCCCCCCCCCCCCCC		28.4525849741
599PhosphorylationSKELSPGSAQKGSPG
CCCCCCCCCCCCCCC		30.8029449344
604PhosphorylationPGSAQKGSPGSSQGT
CCCCCCCCCCCCCCC		32.8823312004
607PhosphorylationAQKGSPGSSQGTACA
CCCCCCCCCCCCCCC		23.9123312004
608PhosphorylationQKGSPGSSQGTACAG
CCCCCCCCCCCCCCC		38.2523312004
611PhosphorylationSPGSSQGTACAGTQP
CCCCCCCCCCCCCCC		15.7823312004
616PhosphorylationQGTACAGTQPGAQPG
CCCCCCCCCCCCCCC		17.0523312004
629PhosphorylationPGAQPGASPSPSQPP
CCCCCCCCCCCCCCC		31.6527251275
631PhosphorylationAQPGASPSPSQPPAD
CCCCCCCCCCCCCCC		34.3927251275
633PhosphorylationPGASPSPSQPPADQS
CCCCCCCCCCCCCCC		60.7130576142
640PhosphorylationSQPPADQSPHTLRKV
CCCCCCCCHHHHHHH		21.1325849741
643PhosphorylationPADQSPHTLRKVSKK
CCCCCHHHHHHHHHH		31.4830242111
706PhosphorylationSLASGQLSPAAAPPL
CCCCCCCCCCCCCCC		12.4726657352
726PhosphorylationFTSTLSKSRPTPKPR
HHHCCCCCCCCCCCC		39.8729449344
729PhosphorylationTLSKSRPTPKPRQRP
CCCCCCCCCCCCCCC		42.7229449344
793PhosphorylationLGSTLRLSPLEHMRR
CCCCEECCHHHHHHH		22.4726074081
802PhosphorylationLEHMRRHSVTDKRDS
HHHHHHHCCCCCCCC		25.5424719451
804PhosphorylationHMRRHSVTDKRDSEE
HHHHHCCCCCCCCHH		38.5330624053
809PhosphorylationSVTDKRDSEEESEST
CCCCCCCCHHHHHHC		51.4428355574
813PhosphorylationKRDSEEESESTAL--
CCCCHHHHHHCCC--		39.8828450419
815PhosphorylationDSEEESESTAL----
CCHHHHHHCCC----		28.4128450419
816PhosphorylationSEEESESTAL-----
CHHHHHHCCC-----		28.1128450419
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 RHG44_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RHG44_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 RHG44_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDC42_HUMANCDC42physical
11431473
RAC1_HUMANRAC1physical
11431473
RHG17_HUMANARHGAP17physical
28514442
FBP1L_HUMANFNBP1Lphysical
28514442
3BP1_HUMANSH3BP1physical
28514442
SH3K1_HUMANSH3KBP1physical
28514442
CIP4_HUMANTRIP10physical
28514442
CD2AP_HUMANCD2APphysical
28514442
PP2BC_HUMANPPP3CCphysical
28514442
WDTC1_HUMANWDTC1physical
28514442
VP26A_HUMANVPS26Aphysical
28514442
NHRF2_HUMANSLC9A3R2physical
27173435
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 RHG44_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-514, AND MASSSPECTROMETRY.

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