ZRAN1_HUMAN - dbPTM
ZRAN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZRAN1_HUMAN
UniProt AC Q9UGI0
Protein Name Ubiquitin thioesterase ZRANB1
Gene Name ZRANB1
Organism Homo sapiens (Human).
Sequence Length 708
Subcellular Localization Cytoplasm. Nucleus. Enriched in punctate localization in the cytoplasm.
Protein Description Specifically hydrolyzes 'Lys-29'-linked and 'Lys-33'-linked diubiquitin. Also cleaves 'Lys-63'-linked chains, but with 40-fold less efficiency compared to 'Lys-29'-linked ones. Positive regulator of the Wnt signaling pathway that deubiquitinates APC protein, a negative regulator of Wnt-mediated transcription. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the stress fiber dynamics and cell migration. May also modulate TNF-alpha signaling..
Protein Sequence MSERGIKWACEYCTYENWPSAIKCTMCRAQRPSGTIITEDPFKSGSSDVGRDWDPSSTEGGSSPLICPDSSARPRVKSSYSMENANKWSCHMCTYLNWPRAIRCTQCLSQRRTRSPTESPQSSGSGSRPVAFSVDPCEEYNDRNKLNTRTQHWTCSVCTYENWAKAKRCVVCDHPRPNNIEAIELAETEEASSIINEQDRARWRGSCSSGNSQRRSPPATKRDSEVKMDFQRIELAGAVGSKEELEVDFKKLKQIKNRMKKTDWLFLNACVGVVEGDLAAIEAYKSSGGDIARQLTADEVRLLNRPSAFDVGYTLVHLAIRFQRQDMLAILLTEVSQQAAKCIPAMVCPELTEQIRREIAASLHQRKGDFACYFLTDLVTFTLPADIEDLPPTVQEKLFDEVLDRDVQKELEEESPIINWSLELATRLDSRLYALWNRTAGDCLLDSVLQATWGIYDKDSVLRKALHDSLHDCSHWFYTRWKDWESWYSQSFGLHFSLREEQWQEDWAFILSLASQPGASLEQTHIFVLAHILRRPIIVYGVKYYKSFRGETLGYTRFQGVYLPLLWEQSFCWKSPIALGYTRGHFSALVAMENDGYGNRGAGANLNTDDDVTITFLPLVDSERKLLHVHFLSAQELGNEEQQEKLLREWLDCCVTEGGVLVAMQKSSRRRNHPLVTQMVEKWLDRYRQIRPCTSLSDGEEDEDDEDE
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
35PhosphorylationRAQRPSGTIITEDPF
CCCCCCCCEEECCCC		17.3422617229
38PhosphorylationRPSGTIITEDPFKSG
CCCCCEEECCCCCCC		30.4122617229
43UbiquitinationIITEDPFKSGSSDVG
EEECCCCCCCCCCCC		60.3327667366
69UbiquitinationSSPLICPDSSARPRV
CCCCCCCCCCCCCCC		51.3027667366
77UbiquitinationSSARPRVKSSYSMEN
CCCCCCCCCCCCCCC		34.6623000965
78PhosphorylationSARPRVKSSYSMENA
CCCCCCCCCCCCCCC		31.48-
86UbiquitinationSYSMENANKWSCHMC
CCCCCCCCCCEEEHH		58.8927667366
103UbiquitinationLNWPRAIRCTQCLSQ
CCCHHHHHHHHHHHH		19.2223000965
105PhosphorylationWPRAIRCTQCLSQRR
CHHHHHHHHHHHHCC		16.6826074081
109PhosphorylationIRCTQCLSQRRTRSP
HHHHHHHHHCCCCCC		29.3026074081
113PhosphorylationQCLSQRRTRSPTESP
HHHHHCCCCCCCCCC		37.3728985074
115PhosphorylationLSQRRTRSPTESPQS
HHHCCCCCCCCCCCC		35.2430576142
117PhosphorylationQRRTRSPTESPQSSG
HCCCCCCCCCCCCCC		50.7930576142
119PhosphorylationRTRSPTESPQSSGSG
CCCCCCCCCCCCCCC		30.6228348404
122PhosphorylationSPTESPQSSGSGSRP
CCCCCCCCCCCCCCC		39.8030576142
123PhosphorylationPTESPQSSGSGSRPV
CCCCCCCCCCCCCCE		31.5630576142
125PhosphorylationESPQSSGSGSRPVAF
CCCCCCCCCCCCEEE		35.2330576142
127PhosphorylationPQSSGSGSRPVAFSV
CCCCCCCCCCEEEEE		34.8030576142
206PhosphorylationDRARWRGSCSSGNSQ
HHHHHCCCCCCCCCC		11.40-
208PhosphorylationARWRGSCSSGNSQRR
HHHCCCCCCCCCCCC		42.87-
209PhosphorylationRWRGSCSSGNSQRRS
HHCCCCCCCCCCCCC		46.45-
212PhosphorylationGSCSSGNSQRRSPPA
CCCCCCCCCCCCCCC		28.70-
216PhosphorylationSGNSQRRSPPATKRD
CCCCCCCCCCCCCCC		37.1126657352
220UbiquitinationQRRSPPATKRDSEVK
CCCCCCCCCCCCCCC		32.1727667366
227UbiquitinationTKRDSEVKMDFQRIE
CCCCCCCCCCHHHHH		28.8033845483
250UbiquitinationEELEVDFKKLKQIKN
HHHHCCHHHHHHHHH		53.3732015554
260AcetylationKQIKNRMKKTDWLFL
HHHHHHHHHCCHHHH		49.65-
336PhosphorylationAILLTEVSQQAAKCI
HHHHHHHHHHHHHHC		15.4422210691
546UbiquitinationVYGVKYYKSFRGETL
EEEEEEEHHHCCCCC		39.7727667366
552PhosphorylationYKSFRGETLGYTRFQ
EHHHCCCCCCEEEEE		28.4524719451
555PhosphorylationFRGETLGYTRFQGVY
HCCCCCCEEEEECEE		9.61-
556PhosphorylationRGETLGYTRFQGVYL
CCCCCCEEEEECEEH		24.18-
572UbiquitinationLLWEQSFCWKSPIAL
EEEECEECCCCCCCC		5.6127667366
575PhosphorylationEQSFCWKSPIALGYT
ECEECCCCCCCCCCC		9.3129523821
581PhosphorylationKSPIALGYTRGHFSA
CCCCCCCCCCCCHHE		8.3029523821
582PhosphorylationSPIALGYTRGHFSAL
CCCCCCCCCCCHHEE		28.5129523821
694PhosphorylationYRQIRPCTSLSDGEE
HHHHCCCCCCCCCCC		35.0728102081
695PhosphorylationRQIRPCTSLSDGEED
HHHCCCCCCCCCCCC		32.3728102081
697PhosphorylationIRPCTSLSDGEEDED
HCCCCCCCCCCCCCC		43.2530576142
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
78SPhosphorylationKinaseAKT1P31749
PSP
117TPhosphorylationKinaseAKT1P31749
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZRAN1_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 ZRAN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2AAB_HUMANPPP2R1Bphysical
19615732
P5CS_HUMANALDH18A1physical
19615732
STRN_HUMANSTRNphysical
19615732
SLMAP_HUMANSLMAPphysical
19615732
HERC2_HUMANHERC2physical
19615732
M4K4_HUMANMAP4K4physical
19615732
GCC2_HUMANGCC2physical
19615732
KEAP1_HUMANKEAP1physical
19615732
BICD2_HUMANBICD2physical
19615732
HECD1_HUMANHECTD1physical
19615732
PHOCN_HUMANMOB4physical
19615732
FGOP2_HUMANFGFR1OP2physical
19615732
CYBP_HUMANCACYBPphysical
19615732
STRN4_HUMANSTRN4physical
19615732
STRN3_HUMANSTRN3physical
19615732
CT2NL_HUMANCTTNBP2NLphysical
19615732
STRP2_HUMANSTRIP2physical
19615732
CTTB2_HUMANCTTNBP2physical
19615732
STRP1_HUMANSTRIP1physical
19615732
PGAM5_HUMANPGAM5physical
19615732
UBC_HUMANUBCphysical
18281465
UBC_HUMANUBCphysical
20622874
UBE2S_HUMANUBE2Sphysical
20622874
TRAF6_HUMANTRAF6physical
20622874
UBC_HUMANUBCphysical
19373254
UBC_HUMANUBCphysical
22157957
STRN4_HUMANSTRN4physical
23277359
STRN3_HUMANSTRN3physical
23277359
STRP1_HUMANSTRIP1physical
23277359
STRN_HUMANSTRNphysical
23277359
SLMAP_HUMANSLMAPphysical
23277359
CTTB2_HUMANCTTNBP2physical
23277359
CT2NL_HUMANCTTNBP2NLphysical
23277359
HECD1_HUMANHECTD1physical
23277359
CORO7_HUMANCORO7physical
24768539
UBC_HUMANUBCphysical
23827681
UBC_HUMANUBCphysical
25527291
UBC_HUMANUBCphysical
25752573
UBC_HUMANUBCphysical
25752577
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 ZRAN1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-260, AND MASS SPECTROMETRY.

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