AP1G2_HUMAN - dbPTM
AP1G2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP1G2_HUMAN
UniProt AC O75843
Protein Name AP-1 complex subunit gamma-like 2
Gene Name AP1G2
Organism Homo sapiens (Human).
Sequence Length 785
Subcellular Localization Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasmic vesicle membrane
Peripheral membrane protein. Endosome membrane
Peripheral membrane protein. Mainly localized to perinuclear vesicular structures (PubMed:97337
Protein Description May function in protein sorting in late endosomes or multivesucular bodies (MVBs). Involved in MVB-assisted maturation of hepatitis B virus (HBV)..
Protein Sequence MVVPSLKLQDLIEEIRGAKTQAQEREVIQKECAHIRASFRDGDPVHRHRQLAKLLYVHMLGYPAHFGQMECLKLIASSRFTDKRVGYLGAMLLLDERHDAHLLITNSIKNDLSQGIQPVQGLALCTLSTMGSAEMCRDLAPEVEKLLLQPSPYVRKKAILTAVHMIRKVPELSSVFLPPCAQLLHERHHGILLGTITLITELCERSPAALRHFRKVVPQLVHILRTLVTMGYSTEHSISGVSDPFLQVQILRLLRILGRNHEESSETMNDLLAQVATNTDTSRNAGNAVLFETVLTIMDIRSAAGLRVLAVNILGRFLLNSDRNIRYVALTSLLRLVQSDHSAVQRHRPTVVECLRETDASLSRRALELSLALVNSSNVRAMMQELQAFLESCPPDLRADCASGILLAAERFAPTKRWHIDTILHVLTTAGTHVRDDAVANLTQLIGGAQELHAYSVRRLYNALAEDISQQPLVQVAAWCIGEYGDLLLAGNCEEIEPLQVDEEEVLALLEKVLQSHMSLPATRGYALTALMKLSTRLCGDNNRIRQVVSIYGSCLDVELQQRAVEYDTLFRKYDHMRAAILEKMPLVERDGPQADEEAKESKEAAQLSEAAPVPTEPQASQLLDLLDLLDGASGDVQHPPHLDPSPGGALVHLLDLPCVPPPPAPIPDLKVFEREGVQLNLSFIRPPENPALLLITITATNFSEGDVTHFICQAAVPKSLQLQLQAPSGNTVPARGGLPITQLFRILNPNKAPLRLKLRLTYDHFHQSVQEIFEVNNLPVESWQ
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
7Ubiquitination-MVVPSLKLQDLIEE
-CCCCCCCHHHHHHH		48.73-
19UbiquitinationIEEIRGAKTQAQERE
HHHHHCCCHHHHHHH		43.95-
20PhosphorylationEEIRGAKTQAQEREV
HHHHCCCHHHHHHHH		28.71961862217
30UbiquitinationQEREVIQKECAHIRA
HHHHHHHHHHHHHHH		43.57-
38PhosphorylationECAHIRASFRDGDPV
HHHHHHHHCCCCCCH		15.80113302787
62PhosphorylationLYVHMLGYPAHFGQM
HHHHHHCCCCHHCHH		8.0346164957
81PhosphorylationLIASSRFTDKRVGYL
HHHHCCCCCCCHHHH		39.2346164951
87PhosphorylationFTDKRVGYLGAMLLL
CCCCCHHHHHHHHHH		10.1022817900
145UbiquitinationDLAPEVEKLLLQPSP
HHHHHHHHHHCCCCH		50.0021890473
151PhosphorylationEKLLLQPSPYVRKKA
HHHHCCCCHHHHHHH		18.8628348404
156UbiquitinationQPSPYVRKKAILTAV
CCCHHHHHHHHHHHH		36.19-
157UbiquitinationPSPYVRKKAILTAVH
CCHHHHHHHHHHHHH		30.05-
168UbiquitinationTAVHMIRKVPELSSV
HHHHHHHHCCCHHHC		51.74-
173PhosphorylationIRKVPELSSVFLPPC
HHHCCCHHHCCCHHH		23.8546164921
174PhosphorylationRKVPELSSVFLPPCA
HHCCCHHHCCCHHHH		29.5246164927
215UbiquitinationAALRHFRKVVPQLVH
HHHHHHHHHHHHHHH		46.7921906983
296PhosphorylationVLFETVLTIMDIRSA
HEEEEEHHHHHHHHH		15.2124719451
332PhosphorylationIRYVALTSLLRLVQS
HHHHHHHHHHHHHHC		26.6824719451
339PhosphorylationSLLRLVQSDHSAVQR
HHHHHHHCCHHHHHH		29.7921406692
342PhosphorylationRLVQSDHSAVQRHRP
HHHHCCHHHHHHCCC		34.8221406692
358PhosphorylationVVECLRETDASLSRR
HHHHHHHCCCHHHHH		30.3646164945
361PhosphorylationCLRETDASLSRRALE
HHHHCCCHHHHHHHH		29.6827174698
363PhosphorylationRETDASLSRRALELS
HHCCCHHHHHHHHHH		19.7527174698
376PhosphorylationLSLALVNSSNVRAMM
HHHHHHCCHHHHHHH		18.7946164933
516PhosphorylationLLEKVLQSHMSLPAT
HHHHHHHHCCCCCCH		19.5946164939
519PhosphorylationKVLQSHMSLPATRGY
HHHHHCCCCCCHHHH		26.2768714243
523PhosphorylationSHMSLPATRGYALTA
HCCCCCCHHHHHHHH		23.7668714249
526PhosphorylationSLPATRGYALTALMK
CCCCHHHHHHHHHHH		8.6421964256
529PhosphorylationATRGYALTALMKLST
CHHHHHHHHHHHHHH		15.0121964256
533UbiquitinationYALTALMKLSTRLCG
HHHHHHHHHHHHHHC		39.89-
567PhosphorylationLQQRAVEYDTLFRKY
HHHHHHHHHHHHHHH		13.9728796482
569PhosphorylationQRAVEYDTLFRKYDH
HHHHHHHHHHHHHHH		27.2268851601
573AcetylationEYDTLFRKYDHMRAA
HHHHHHHHHHHHHHH		47.937709533
584UbiquitinationMRAAILEKMPLVERD
HHHHHHHHCCCCCCC		42.232190698
752UbiquitinationFRILNPNKAPLRLKL
HHHHCCCCCCCEEEE		53.27-
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
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:18772139
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP1G2_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 AP1G2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYNRG_HUMANSYNRGphysical
10814529
NEDD4_HUMANNEDD4physical
18772139
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
CENPK_HUMANCENPKphysical
25416956
SYNRG_HUMANSYNRGphysical
28514442
TMX3_HUMANTMX3physical
28514442
ZY11B_HUMANZYG11Bphysical
28514442
ATG2B_HUMANATG2Bphysical
28514442
ZN318_HUMANZNF318physical
28514442
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP1G2_HUMAN

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Related Literatures of Post-Translational Modification

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