ARI2_HUMAN - dbPTM
ARI2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ARI2_HUMAN
UniProt AC O95376
Protein Name E3 ubiquitin-protein ligase ARIH2
Gene Name ARIH2
Organism Homo sapiens (Human).
Sequence Length 493
Subcellular Localization Nucleus . Cytoplasm .
Protein Description E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3. [PubMed: 16118314]
Protein Sequence MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEARVQPNPSKHVPTSHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVGVSCMAQDCPLRTPEDFVFPLLPNEELREKYRRYLFRDYVESHYQLQLCPGADCPMVIRVQEPRARRVQCNRCNEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKCNICIEKNGGCNHMQCSKCKHDFCWMCLGDWKTHGSEYYECSRYKENPDIVNQSQQAQAREALKKYLFYFERWENHNKSLQLEAQTYQRIHEKIQERVMNNLGTWIDWQYLQNAAKLLAKCRYTLQYTYPYAYYMESGPRKKLFEYQQAQLEAEIENLSWKVERADSYDRGDLENQMHIAEQRRRTLLKDFHDT
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
44PhosphorylationDYYVGVASDVEQQGA
HHEEEEECCHHHCCC		39.5226074081
85UbiquitinationTSLASVLKVSHSVAK
HHHHHHHHHHHHHHH		39.26-
113PhosphorylationLDRYKSNSAQLLVEA
HHHHHCCCCEEEEEE		25.2027251275
259UbiquitinationCNEVFCFKCRQMYHA
CCCEEEEECCEECCC		29.68-
279UbiquitinationTIRKWLTKCADDSET
HHHHHHHHHCCCHHH		25.84-
289PhosphorylationDDSETANYISAHTKD
CCHHHHHHHHHCCCC		8.1927642862
295UbiquitinationNYISAHTKDCPKCNI
HHHHHCCCCCCCCCE		47.68-
299UbiquitinationAHTKDCPKCNICIEK
HCCCCCCCCCEEEEE		46.36-
335PhosphorylationGDWKTHGSEYYECSR
CCCCCCCCCCCCCCC		18.1528152594
337PhosphorylationWKTHGSEYYECSRYK
CCCCCCCCCCCCCCC		13.2728152594
338PhosphorylationKTHGSEYYECSRYKE
CCCCCCCCCCCCCCC		13.3528152594
341PhosphorylationGSEYYECSRYKENPD
CCCCCCCCCCCCCCC		27.0628152594
344UbiquitinationYYECSRYKENPDIVN
CCCCCCCCCCCCCCC		50.3221906983
353PhosphorylationNPDIVNQSQQAQARE
CCCCCCHHHHHHHHH		21.0317525332
364UbiquitinationQAREALKKYLFYFER
HHHHHHHHHHHHHHH		48.3021906983
377UbiquitinationERWENHNKSLQLEAQ
HHHHHCCHHHHHHHH		45.0221906983
392UbiquitinationTYQRIHEKIQERVMN
HHHHHHHHHHHHHHH		35.21-
419UbiquitinationNAAKLLAKCRYTLQY
HHHHHHHHHCCEEEE		21.15-
422PhosphorylationKLLAKCRYTLQYTYP
HHHHHHCCEEEECCC		22.6724043423
423PhosphorylationLLAKCRYTLQYTYPY
HHHHHCCEEEECCCC		6.5024043423
426PhosphorylationKCRYTLQYTYPYAYY
HHCCEEEECCCCEEE		16.0224043423
427PhosphorylationCRYTLQYTYPYAYYM
HCCEEEECCCCEEEE		12.6924043423
428PhosphorylationRYTLQYTYPYAYYME
CCEEEECCCCEEEEC		6.8524043423
430PhosphorylationTLQYTYPYAYYMESG
EEEECCCCEEEECCC		9.2324043423
432PhosphorylationQYTYPYAYYMESGPR
EECCCCEEEECCCCC		9.4824043423
433PhosphorylationYTYPYAYYMESGPRK
ECCCCEEEECCCCCH		6.0424043423
436PhosphorylationPYAYYMESGPRKKLF
CCEEEECCCCCHHHH		37.2524043423
441UbiquitinationMESGPRKKLFEYQQA
ECCCCCHHHHHHHHH		60.7421890473
460UbiquitinationEIENLSWKVERADSY
HHHHHCEEEEECCCC		30.7321906983
466PhosphorylationWKVERADSYDRGDLE
EEEEECCCCCCCCHH		28.1320873877
467PhosphorylationKVERADSYDRGDLEN
EEEECCCCCCCCHHH		15.3720873877
488UbiquitinationQRRRTLLKDFHDT--
HHHHHHHHHHCCC--		62.55-
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 ligaseMDM2Q00987
PMID:22940738
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ARI2_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 ARI2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EMAL4_HUMANEML4physical
16169070
WDR91_HUMANWDR91physical
16169070
KCNQ2_HUMANKCNQ2physical
16169070
SGCE_HUMANSGCEphysical
16169070
CBR3_HUMANCBR3physical
16169070
ENSA_HUMANENSAphysical
16169070
IL4RA_HUMANIL4Rphysical
16169070
2AAA_HUMANPPP2R1Aphysical
16169070
EAA4_HUMANSLC1A6physical
16169070
ARAP1_HUMANARAP1physical
16169070
ODO2_HUMANDLSTphysical
16169070
KAT5_HUMANKAT5physical
16169070
SCAM2_HUMANSCAMP2physical
16169070
UT14A_HUMANUTP14Aphysical
16169070
CE126_HUMANKIAA1377physical
16169070
PTN_HUMANPTNphysical
16169070
RL8_HUMANRPL8physical
16169070
P53_HUMANTP53physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
EF1G_HUMANEEF1Gphysical
16169070
UB2L3_HUMANUBE2L3physical
16169070
GFI1_HUMANGFI1physical
17646546
UB2L3_HUMANUBE2L3physical
16118314
UB2L3_HUMANUBE2L3physical
15545318
PML_HUMANPMLphysical
22037423
UBE2N_HUMANUBE2Nphysical
19340006
UBC_HUMANUBCphysical
19340006
P53_HUMANTP53physical
22819825
TRI27_HUMANTRIM27physical
22493164
RHEB_HUMANRHEBphysical
21988832
UB2L3_HUMANUBE2L3physical
24076655
CUL5_HUMANCUL5physical
24076655
ARI2_HUMANARIH2physical
24076655
APEX1_HUMANAPEX1physical
22863883
HXK2_HUMANHK2physical
22863883
NUBP1_HUMANNUBP1physical
22863883
TWF2_HUMANTWF2physical
22863883
PABP2_HUMANPABPN1physical
24486325
CCD33_HUMANCCDC33physical
25416956
ELOB_HUMANTCEB2physical
24076655
ELOC_HUMANTCEB1physical
24076655
CCD33_HUMANCCDC33physical
21516116
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 ARI2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353, AND MASSSPECTROMETRY.

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