AIP_HUMAN - dbPTM
AIP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AIP_HUMAN
UniProt AC O00170
Protein Name AH receptor-interacting protein
Gene Name AIP
Organism Homo sapiens (Human).
Sequence Length 330
Subcellular Localization Cytoplasm.
Protein Description May play a positive role in AHR-mediated (aromatic hydrocarbon receptor) signaling, possibly by influencing its receptivity for ligand and/or its nuclear targeting.; Cellular negative regulator of the hepatitis B virus (HBV) X protein..
Protein Sequence MADIIARLREDGIQKRVIQEGRGELPDFQDGTKATFHYRTLHSDDEGTVLDDSRARGKPMELIIGKKFKLPVWETIVCTMREGEIAQFLCDIKHVVLYPLVAKSLRNIAVGKDPLEGQRHCCGVAQMREHSSLGHADLDALQQNPQPLIFHMEMLKVESPGTYQQDPWAMTDEEKAKAVPLIHQEGNRLYREGHVKEAAAKYYDAIACLKNLQMKEQPGSPEWIQLDQQITPLLLNYCQCKLVVEEYYEVLDHCSSILNKYDDNVKAYFKRGKAHAAVWNAQEAQADFAKVLELDPALAPVVSRELQALEARIRQKDEEDKARFRGIFSH
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
2Acetylation------MADIIARLR
------CCHHHHHHH		19.40-
15UbiquitinationLREDGIQKRVIQEGR
HHHCCHHHHHHHCCC		46.87-
22MethylationKRVIQEGRGELPDFQ
HHHHHCCCCCCCCCC		34.36-
33UbiquitinationPDFQDGTKATFHYRT
CCCCCCCEEEEEEEE		51.46-
40PhosphorylationKATFHYRTLHSDDEG
EEEEEEEEECCCCCC		22.9628450419
43PhosphorylationFHYRTLHSDDEGTVL
EEEEEECCCCCCCCC		50.2827794612
48PhosphorylationLHSDDEGTVLDDSRA
ECCCCCCCCCCCHHH		18.8228450419
53PhosphorylationEGTVLDDSRARGKPM
CCCCCCCHHHCCCCE		27.7530576142
58UbiquitinationDDSRARGKPMELIIG
CCHHHCCCCEEEEEE		35.32-
60SulfoxidationSRARGKPMELIIGKK
HHHCCCCEEEEEECC		8.1421406390
66AcetylationPMELIIGKKFKLPVW
CEEEEEECCCCCCEE		44.6320167786
66UbiquitinationPMELIIGKKFKLPVW
CEEEEEECCCCCCEE		44.63-
67UbiquitinationMELIIGKKFKLPVWE
EEEEEECCCCCCEEE		42.38-
69UbiquitinationLIIGKKFKLPVWETI
EEEECCCCCCEEEEE		61.84-
79PhosphorylationVWETIVCTMREGEIA
EEEEEEEEECCCHHH		14.3636012995
103AcetylationVLYPLVAKSLRNIAV
HHHHHHHHHHHCCCC		42.4125953088
103UbiquitinationVLYPLVAKSLRNIAV
HHHHHHHHHHHCCCC		42.41-
104PhosphorylationLYPLVAKSLRNIAVG
HHHHHHHHHHCCCCC		23.8710014601
112MalonylationLRNIAVGKDPLEGQR
HHCCCCCCCCCCCCC		49.9626320211
112UbiquitinationLRNIAVGKDPLEGQR
HHCCCCCCCCCCCCC		49.96-
131PhosphorylationVAQMREHSSLGHADL
HHHHHHHHCCCCCCH		23.6220873877
132PhosphorylationAQMREHSSLGHADLD
HHHHHHHCCCCCCHH		40.0320873877
159PhosphorylationMEMLKVESPGTYQQD
EEEEECCCCCCCCCC		31.4525159151
162PhosphorylationLKVESPGTYQQDPWA
EECCCCCCCCCCCCC		22.8828796482
163PhosphorylationKVESPGTYQQDPWAM
ECCCCCCCCCCCCCC		15.3028796482
170SulfoxidationYQQDPWAMTDEEKAK
CCCCCCCCCHHHHHH		4.2430846556
171PhosphorylationQQDPWAMTDEEKAKA
CCCCCCCCHHHHHHH		32.29110734987
175UbiquitinationWAMTDEEKAKAVPLI
CCCCHHHHHHHCCEE		53.81-
177UbiquitinationMTDEEKAKAVPLIHQ
CCHHHHHHHCCEECC		62.07-
196UbiquitinationLYREGHVKEAAAKYY
HHHCCCHHHHHHHHH		35.64-
201AcetylationHVKEAAAKYYDAIAC
CHHHHHHHHHHHHHH		39.3525953088
201UbiquitinationHVKEAAAKYYDAIAC
CHHHHHHHHHHHHHH		39.35-
202PhosphorylationVKEAAAKYYDAIACL
HHHHHHHHHHHHHHH		11.2328796482
203PhosphorylationKEAAAKYYDAIACLK
HHHHHHHHHHHHHHH		9.7428796482
208S-nitrosylationKYYDAIACLKNLQMK
HHHHHHHHHHHCCCC		4.5519483679
208GlutathionylationKYYDAIACLKNLQMK
HHHHHHHHHHHCCCC		4.5522555962
208S-nitrosocysteineKYYDAIACLKNLQMK
HHHHHHHHHHHCCCC		4.55-
210AcetylationYDAIACLKNLQMKEQ
HHHHHHHHHCCCCCC		56.3425953088
210UbiquitinationYDAIACLKNLQMKEQ
HHHHHHHHHCCCCCC		56.34-
238S-nitrosylationTPLLLNYCQCKLVVE
HHHHHHHHCCCHHHH		3.5919483679
238S-nitrosocysteineTPLLLNYCQCKLVVE
HHHHHHHHCCCHHHH		3.59-
240S-nitrosocysteineLLLNYCQCKLVVEEY
HHHHHHCCCHHHHHH		3.08-
240S-nitrosylationLLLNYCQCKLVVEEY
HHHHHHCCCHHHHHH		3.0819483679
247PhosphorylationCKLVVEEYYEVLDHC
CCHHHHHHHHHHHHH		7.4528796482
248PhosphorylationKLVVEEYYEVLDHCS
CHHHHHHHHHHHHHH		11.6628796482
255PhosphorylationYEVLDHCSSILNKYD
HHHHHHHHHHHHHCC		19.5926552605
256PhosphorylationEVLDHCSSILNKYDD
HHHHHHHHHHHHCCH		36.1724719451
260UbiquitinationHCSSILNKYDDNVKA
HHHHHHHHCCHHHHH		46.76-
261PhosphorylationCSSILNKYDDNVKAY
HHHHHHHCCHHHHHH		27.7027642862
266UbiquitinationNKYDDNVKAYFKRGK
HHCCHHHHHHHHCCH		43.56-
273UbiquitinationKAYFKRGKAHAAVWN
HHHHHCCHHHHHHHC		40.82-
273MalonylationKAYFKRGKAHAAVWN
HHHHHCCHHHHHHHC		40.8226320211
290UbiquitinationEAQADFAKVLELDPA
HHHHHHHHHHCCCHH		47.55-
316UbiquitinationLEARIRQKDEEDKAR
HHHHHHCCCHHHHHH		58.20-
321UbiquitinationRQKDEEDKARFRGIF
HCCCHHHHHHHCCCC		44.75-
329PhosphorylationARFRGIFSH------
HHHCCCCCC------		26.7721777215
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
43SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AIP_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 AIP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AHR_HUMANAHRphysical
10986286
HS90A_HUMANHSP90AA1physical
21170051
STIP1_HUMANSTIP1physical
21170051
GNA13_HUMANGNA13physical
19390533
GDIB_HUMANGDI2physical
22939629
CLC7A_HUMANCLEC7Aphysical
21988832
IF2G_HUMANEIF2S3physical
22863883
LAMP1_HUMANLAMP1physical
22863883
AGO1_HUMANAGO1physical
24778252
CDC37_HUMANCDC37physical
25036637
HS90A_HUMANHSP90AA1physical
25036637
HS90B_HUMANHSP90AB1physical
25036637
UBP19_HUMANUSP19physical
25036637
NADE_HUMANNADSYN1physical
25036637
TEBP_HUMANPTGES3physical
25036637
KTU_HUMANDNAAF2physical
25036637
GNAQ_HUMANGNAQphysical
19390533
RET_HUMANRETphysical
19366855
IPYR_HUMANPPA1physical
26344197
IPYR2_HUMANPPA2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
102200Pituitary adenoma, growth hormone-secreting, 1 (PAGH1)
219090ACTH-secreting pituitary adenoma (ASPA)
600634Prolactin-secreting pituitary adenoma (PSPA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AIP_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 ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-248, AND MASSSPECTROMETRY.

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