HIP1R_HUMAN - dbPTM
HIP1R_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HIP1R_HUMAN
UniProt AC O75146
Protein Name Huntingtin-interacting protein 1-related protein
Gene Name HIP1R
Organism Homo sapiens (Human).
Sequence Length 1068
Subcellular Localization Cytoplasm, perinuclear region. Endomembrane system. Cytoplasmic vesicle, clathrin-coated vesicle membrane. Membrane-associated protein, mainly localized at the endocytic compartments and in the perinuclear region.
Protein Description Component of clathrin-coated pits and vesicles, that may link the endocytic machinery to the actin cytoskeleton. Binds 3-phosphoinositides (via ENTH domain). May act through the ENTH domain to promote cell survival by stabilizing receptor tyrosine kinases following ligand-induced endocytosis..
Protein Sequence MNSIKNVPARVLSRRPGHSLEAEREQFDKTQAISISKAINTQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIREIGDLWGHLHDRYGQLVNVYTKLLLTKISFHLKHPQFPAGLEVTDEVLEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLLFKLHSCLPADTLQGHRDRFHEQFHSLRNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEDEEPENLIEISTGPPAGEPVVVADLFDQTFGPPNGSVKDDRDLQIESLKREVEMLRSELEKIKLEAQRYIAQLKSQVNALEGELEEQRKQKQKALVDNEQLRHELAQLRAAQLEGERSQGLREEAERKASATEARYNKLKEKHSELVHVHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQVEQVKRESELKLEEKSDQLEKLKRELEAKAGELARAQEALSHTEQSKSELSSRLDTLSAEKDALSGAVRQREADLLAAQSLVRETEAALSREQQRSSQEQGELQGRLAERESQEQGLRQRLLDEQFAVLRGAAAEAAGILQDAVSKLDDPLHLRCTSSPDYLVSRAQEALDAVSTLEEGHAQYLTSLADASALVAALTRFSHLAADTIINGGATSHLAPTDPADRLIDTCRECGARALELMGQLQDQQALRHMQASLVRTPLQGILQLGQELKPKSLDVRQEELGAVVDKEMAATSAAIEDAVRRIEDMMNQARHASSGVKLEVNERILNSCTDLMKAIRLLVTTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVGWGATQLVEAADKVVLHTGKYEELIVCSHEIAASTAQLVAASKVKANKHSPHLSRLQECSRTVNERAANVVASTKSGQEQIEDRDTMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERMRLGELRKQHYVLAGASGSPGEEVAIRPSTAPRSVTTKKPPLAQKPSVAPRQDHQLDKKDGIYPAQLVNY
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
1Acetylation-------MNSIKNVP
-------CCCCCCCC		39.7122814378
3Phosphorylation-----MNSIKNVPAR
-----CCCCCCCCHH		46.9628857561
5Acetylation---MNSIKNVPARVL
---CCCCCCCCHHHH		52.277676297
5Ubiquitination---MNSIKNVPARVL
---CCCCCCCCHHHH		52.27-
13PhosphorylationNVPARVLSRRPGHSL
CCCHHHHCCCCCCCH		24.3226074081
19PhosphorylationLSRRPGHSLEAEREQ
HCCCCCCCHHHHHHH		33.5426074081
29UbiquitinationAEREQFDKTQAISIS
HHHHHCCHHHHHHHH		43.77-
29AcetylationAEREQFDKTQAISIS
HHHHHCCHHHHHHHH		43.7726051181
34PhosphorylationFDKTQAISISKAINT
CCHHHHHHHHHHCCC		24.6724719451
37UbiquitinationTQAISISKAINTQEA
HHHHHHHHHCCCCCC		52.17-
80PhosphorylationGLPLPSSSILSWKFC
CCCCCCHHHHHHHHH		31.7024719451
83PhosphorylationLPSSSILSWKFCHVL
CCCHHHHHHHHHHHH		26.9224719451
126PhosphorylationWGHLHDRYGQLVNVY
HHHHHHHHHHHHHHH		18.4522210691
133PhosphorylationYGQLVNVYTKLLLTK
HHHHHHHHHHHHHHH		7.9222210691
134PhosphorylationGQLVNVYTKLLLTKI
HHHHHHHHHHHHHHH		15.7822210691
139PhosphorylationVYTKLLLTKISFHLK
HHHHHHHHHHHHHCC		26.7122210691
146UbiquitinationTKISFHLKHPQFPAG
HHHHHHCCCCCCCCC		44.6721890473
146AcetylationTKISFHLKHPQFPAG
HHHHHHCCCCCCCCC		44.6721466224
146UbiquitinationTKISFHLKHPQFPAG
HHHHHHCCCCCCCCC		44.6721890473
259PhosphorylationRFHEQFHSLRNFFRR
HHHHHHHHHHHHHHH		30.2520873877
268PhosphorylationRNFFRRASDMLYFKR
HHHHHHHHHHHHHHH		23.0328857561
293PhosphorylationPPNFLRASALAEHIK
CCCCHHHHHHHHHCC		19.8523312004
404UbiquitinationEQRKQKQKALVDNEQ
HHHHHHHHHHCCHHH		51.20-
476PhosphorylationADTAKQLTVTQQSQE
CCHHHHHEECHHHHH		21.0024043423
478PhosphorylationTAKQLTVTQQSQEEV
HHHHHEECHHHHHHH		18.6924043423
481PhosphorylationQLTVTQQSQEEVARV
HHEECHHHHHHHHHH		29.7330624053
541PhosphorylationALSHTEQSKSELSSR
HHHCCHHHHHHHHHH		31.73-
5422-HydroxyisobutyrylationLSHTEQSKSELSSRL
HHCCHHHHHHHHHHH		47.87-
542AcetylationLSHTEQSKSELSSRL
HHCCHHHHHHHHHHH		47.8726051181
553PhosphorylationSSRLDTLSAEKDALS
HHHHHHHHHHHHHHH		36.1526091039
556AcetylationLDTLSAEKDALSGAV
HHHHHHHHHHHHHHH		48.2826051181
560PhosphorylationSAEKDALSGAVRQRE
HHHHHHHHHHHHHHH		26.82-
575PhosphorylationADLLAAQSLVRETEA
HHHHHHHHHHHHHHH		24.8924719451
592PhosphorylationSREQQRSSQEQGELQ
HHHHHHHHHHHHHHH		39.6721815630
640PhosphorylationGILQDAVSKLDDPLH
HHHHHHHHCCCCCCC		29.2621406692
651O-linked_GlycosylationDPLHLRCTSSPDYLV
CCCCCCCCCCHHHHH		26.30OGP
652PhosphorylationPLHLRCTSSPDYLVS
CCCCCCCCCHHHHHH		43.4224719451
652O-linked_GlycosylationPLHLRCTSSPDYLVS
CCCCCCCCCHHHHHH		43.42OGP
653PhosphorylationLHLRCTSSPDYLVSR
CCCCCCCCHHHHHHH		12.0227251275
771PhosphorylationGQELKPKSLDVRQEE
CHHCCCCCCCCCHHH		38.0320068231
831SulfoxidationLNSCTDLMKAIRLLV
HHHHHHHHHHHHHHH		2.8321406390
832AcetylationNSCTDLMKAIRLLVT
HHHHHHHHHHHHHHH		48.2126051181
839PhosphorylationKAIRLLVTTSTSLQK
HHHHHHHHCCHHHHH		18.26-
840PhosphorylationAIRLLVTTSTSLQKE
HHHHHHHCCHHHHHH		23.64-
842PhosphorylationRLLVTTSTSLQKEIV
HHHHHCCHHHHHHHH		31.22-
843PhosphorylationLLVTTSTSLQKEIVE
HHHHCCHHHHHHHHH		28.6823403867
862PhosphorylationAATQQEFYAKNSRWT
HHHHHHHHHHCCCCC		18.8626330541
864UbiquitinationTQQEFYAKNSRWTEG
HHHHHHHHCCCCCHH		44.04-
866PhosphorylationQEFYAKNSRWTEGLI
HHHHHHCCCCCHHHH		28.6126330541
869PhosphorylationYAKNSRWTEGLISAS
HHHCCCCCHHHHHHH		21.0426330541
929PhosphorylationKVKANKHSPHLSRLQ
HHHCCCCCCCHHHHH		18.6728348404
972PhosphorylationTMDFSGLSLIKLKKQ
CCCCCCCHHHHHCHH		31.4124719451
983PhosphorylationLKKQEMETQVRVLEL
HCHHHHHHHHHHHHH		30.9323025827
1009PhosphorylationGELRKQHYVLAGASG
HHHHHCCEEEECCCC		8.4827251275
1015PhosphorylationHYVLAGASGSPGEEV
CEEEECCCCCCCCEE		38.6024732914
1017PhosphorylationVLAGASGSPGEEVAI
EEECCCCCCCCEEEE		27.5125159151
1027PhosphorylationEEVAIRPSTAPRSVT
CEEEECCCCCCCCCC		27.6124732914
1028PhosphorylationEVAIRPSTAPRSVTT
EEEECCCCCCCCCCC		43.2824732914
1045PhosphorylationPPLAQKPSVAPRQDH
CCCCCCCCCCCCCCC		37.6423403867
1061PhosphorylationLDKKDGIYPAQLVNY
CCCCCCCCCHHHCCC		9.69-
1068PhosphorylationYPAQLVNY-------
CCHHHCCC-------		16.6727642862
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 HIP1R_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HIP1R_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 HIP1R_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SH3K1_HUMANSH3KBP1physical
15090612
PICAL_HUMANPICALMphysical
22939629
I2BP1_HUMANIRF2BP1physical
26344197
MTMR6_HUMANMTMR6physical
26344197
TATD1_HUMANTATDN1physical
26344197
VPS28_HUMANVPS28physical
26344197
SYWC_HUMANWARSphysical
26344197
BOP1_HUMANBOP1physical
25825154
HIP1_HUMANHIP1physical
28514442
REPS1_HUMANREPS1physical
28514442
RBP1_HUMANRALBP1physical
28514442
GAK_HUMANGAKphysical
28514442
PPM1A_HUMANPPM1Aphysical
28514442
PPM1B_HUMANPPM1Bphysical
28514442
AP1B1_HUMANAP1B1physical
28514442
SFPQ_HUMANSFPQphysical
28514442
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 HIP1R_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1017, AND MASSSPECTROMETRY.

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