PEX1_HUMAN - dbPTM
PEX1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEX1_HUMAN
UniProt AC O43933
Protein Name Peroxisome biogenesis factor 1
Gene Name PEX1
Organism Homo sapiens (Human).
Sequence Length 1283
Subcellular Localization Cytoplasm. Peroxisome membrane. Associated with peroxisomal membranes.
Protein Description Required for stability of PEX5 and protein import into the peroxisome matrix. Anchored by PEX26 to peroxisome membranes, possibly to form heteromeric AAA ATPase complexes required for the import of proteins into peroxisomes..
Protein Sequence MWGSDRLAGAGGGGAAVTVAFTNARDCFLHLPRRLVAQLHLLQNQAIEVVWSHQPAFLSWVEGRHFSDQGENVAEINRQVGQKLGLSNGGQVFLKPCSHVVSCQQVEVEPLSADDWEILELHAVSLEQHLLDQIRIVFPKAIFPVWVDQQTYIFIQIVALIPAASYGRLETDTKLLIQPKTRRAKENTFSKADAEYKKLHSYGRDQKGMMKELQTKQLQSNTVGITESNENESEIPVDSSSVASLWTMIGSIFSFQSEKKQETSWGLTEINAFKNMQSKVVPLDNIFRVCKSQPPSIYNASATSVFHKHCAIHVFPWDQEYFDVEPSFTVTYGKLVKLLSPKQQQSKTKQNVLSPEKEKQMSEPLDQKKIRSDHNEEDEKACVLQVVWNGLEELNNAIKYTKNVEVLHLGKVWIPDDLRKRLNIEMHAVVRITPVEVTPKIPRSLKLQPRENLPKDISEEDIKTVFYSWLQQSTTTMLPLVISEEEFIKLETKDGLKEFSLSIVHSWEKEKDKNIFLLSPNLLQKTTIQVLLDPMVKEENSEEIDFILPFLKLSSLGGVNSLGVSSLEHITHSLLGRPLSRQLMSLVAGLRNGALLLTGGKGSGKSTLAKAICKEAFDKLDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAGLPAVPEHEHSPDAVQSQRLAHALNDMIKEFISMGSLVALIATSQSQQSLHPLLVSAQGVHIFQCVQHIQPPNQEQRCEILCNVIKNKLDCDINKFTDLDLQHVAKETGGFVARDFTVLVDRAIHSRLSRQSISTREKLVLTTLDFQKALRGFLPASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHGMLLSSGLQDGSSSSDSDLSLSSMVFLNHSSGSDDSAGDGECGLDQSLVSLEMSEILPDESKFNMYRLYFGSSYESELGNGTSSDLSSQCLSAPSSMTQDLPGVPGKDQLFSQPPVLRTASQEGCQELTQEQRDQLRADISIIKGRYRSQSGEDESMNQPGPIKTRLAISQSHLMTALGHTRPSISEDDWKNFAELYESFQNPKRRKNQSGTMFRPGQKVTLA
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
133UbiquitinationLEQHLLDQIRIVFPK
HHHHHHHHHHHHCCC		27.16-
189UbiquitinationRRAKENTFSKADAEY
HHHHHCCCCHHHHHH		12.14-
191UbiquitinationAKENTFSKADAEYKK
HHHCCCCHHHHHHHH		46.20-
191UbiquitinationAKENTFSKADAEYKK
HHHCCCCHHHHHHHH		46.20-
198UbiquitinationKADAEYKKLHSYGRD
HHHHHHHHHHHCCCC		51.00-
202PhosphorylationEYKKLHSYGRDQKGM
HHHHHHHCCCCHHHH		12.87-
211UbiquitinationRDQKGMMKELQTKQL
CCHHHHHHHHHHHHH		46.51-
215PhosphorylationGMMKELQTKQLQSNT
HHHHHHHHHHHHHCC		33.1229759185
260UbiquitinationFSFQSEKKQETSWGL
HCCCCCCCCCCCCCH		49.68-
264PhosphorylationSEKKQETSWGLTEIN
CCCCCCCCCCHHHHH		20.56-
274UbiquitinationLTEINAFKNMQSKVV
HHHHHHHCCCCCCEE		49.45-
278PhosphorylationNAFKNMQSKVVPLDN
HHHCCCCCCEECHHH		19.35-
279UbiquitinationAFKNMQSKVVPLDNI
HHCCCCCCEECHHHH		30.29-
291UbiquitinationDNIFRVCKSQPPSIY
HHHHHHHHCCCCCCC		49.63-
337UbiquitinationVTYGKLVKLLSPKQQ
EEHHHHHHHHCHHHH		54.89-
340PhosphorylationGKLVKLLSPKQQQSK
HHHHHHHCHHHHHCC		40.2524719451
342UbiquitinationLVKLLSPKQQQSKTK
HHHHHCHHHHHCCHH		58.31-
349UbiquitinationKQQQSKTKQNVLSPE
HHHHCCHHHCCCCHH		43.54-
354PhosphorylationKTKQNVLSPEKEKQM
CHHHCCCCHHHHHHC		27.0829496963
357UbiquitinationQNVLSPEKEKQMSEP
HCCCCHHHHHHCCCC		73.86-
402UbiquitinationNNAIKYTKNVEVLHL
HHHHHHCCCCEEEEC		56.77-
411UbiquitinationVEVLHLGKVWIPDDL
CEEEECCEEECCHHH		40.53-
434UbiquitinationHAVVRITPVEVTPKI
EEEEEEECCCCCCCC		20.21-
438PhosphorylationRITPVEVTPKIPRSL
EEECCCCCCCCCCCC		12.8323312004
441UbiquitinationPVEVTPKIPRSLKLQ
CCCCCCCCCCCCCCC		3.45-
446UbiquitinationPKIPRSLKLQPRENL
CCCCCCCCCCCCCCC		46.45-
455UbiquitinationQPRENLPKDISEEDI
CCCCCCCCCCCHHHH		71.51-
484UbiquitinationMLPLVISEEEFIKLE
EEEEEECHHHHEEEE		50.8821890473
484UbiquitinationMLPLVISEEEFIKLE
EEEEEECHHHHEEEE		50.88-
494UbiquitinationFIKLETKDGLKEFSL
HEEEECCCCCCEEEE		75.08-
500PhosphorylationKDGLKEFSLSIVHSW
CCCCCEEEEEEECCC		23.4629396449
502PhosphorylationGLKEFSLSIVHSWEK
CCCEEEEEEECCCHH		22.7429396449
511UbiquitinationVHSWEKEKDKNIFLL
ECCCHHHCCCCEEEE		82.28-
511UbiquitinationVHSWEKEKDKNIFLL
ECCCHHHCCCCEEEE		82.28-
513UbiquitinationSWEKEKDKNIFLLSP
CCHHHCCCCEEEECH		64.11-
519UbiquitinationDKNIFLLSPNLLQKT
CCCEEEECHHHHCHH		17.56-
541PhosphorylationPMVKEENSEEIDFIL
HHHCCCCHHHCCCHH		39.6327251275
554PhosphorylationILPFLKLSSLGGVNS
HHHHHHHHHCCCCCC		23.1722210691
555PhosphorylationLPFLKLSSLGGVNSL
HHHHHHHHCCCCCCC		41.2822210691
565UbiquitinationGVNSLGVSSLEHITH
CCCCCCHHCHHHHHH		27.66-
584UbiquitinationRPLSRQLMSLVAGLR
CHHHHHHHHHHHHHH		1.89-
585PhosphorylationPLSRQLMSLVAGLRN
HHHHHHHHHHHHHHC		28.43-
591UbiquitinationMSLVAGLRNGALLLT
HHHHHHHHCCEEEEE		38.32-
601UbiquitinationALLLTGGKGSGKSTL
EEEEECCCCCCHHHH		51.77-
605UbiquitinationTGGKGSGKSTLAKAI
ECCCCCCHHHHHHHH		41.80-
610UbiquitinationSGKSTLAKAICKEAF
CCHHHHHHHHHHHHH		41.20-
611UbiquitinationGKSTLAKAICKEAFD
CHHHHHHHHHHHHHH		13.55-
614UbiquitinationTLAKAICKEAFDKLD
HHHHHHHHHHHHHHH		46.06-
619UbiquitinationICKEAFDKLDAHVER
HHHHHHHHHHHHHHH		41.64-
630UbiquitinationHVERVDCKALRGKRL
HHHHHHHHHHCCHHH		46.09-
679UbiquitinationAVPEHEHSPDAVQSQ
CCCCCCCCCHHHHHH		22.84-
756UbiquitinationLCNVIKNKLDCDINK
HHHHHHHHCCCCCCC		40.47-
763UbiquitinationKLDCDINKFTDLDLQ
HCCCCCCCCCCCCHH		50.39-
774UbiquitinationLDLQHVAKETGGFVA
CCHHHHHHHHCCCCC		55.51-
794PhosphorylationLVDRAIHSRLSRQSI
HHHHHHHHHHHCCCC		28.8924043423
797PhosphorylationRAIHSRLSRQSISTR
HHHHHHHHCCCCCCH		27.4524043423
800PhosphorylationHSRLSRQSISTREKL
HHHHHCCCCCCHHHH		19.8624043423
802PhosphorylationRLSRQSISTREKLVL
HHHCCCCCCHHHHHH		27.0224043423
803PhosphorylationLSRQSISTREKLVLT
HHCCCCCCHHHHHHH		40.9724043423
806UbiquitinationQSISTREKLVLTTLD
CCCCCHHHHHHHHHH		40.3721890473
806UbiquitinationQSISTREKLVLTTLD
CCCCCHHHHHHHHHH		40.3721890473
810PhosphorylationTREKLVLTTLDFQKA
CHHHHHHHHHHHHHH		20.17-
811PhosphorylationREKLVLTTLDFQKAL
HHHHHHHHHHHHHHH		21.85-
816UbiquitinationLTTLDFQKALRGFLP
HHHHHHHHHHCCCCC		49.75-
833UbiquitinationLRSVNLHKPRDLGWD
HHCCCCCCCCCCCCC		44.9317370265
841UbiquitinationPRDLGWDKIGGLHEV
CCCCCCCCCCCHHHH		36.42-
855PhosphorylationVRQILMDTIQLPAKY
HHHHHHHHCCCCCCC		9.1725332170
880PhosphorylationQRTGILLYGPPGTGK
CCCEEEEECCCCCCH		24.9223917254
882UbiquitinationTGILLYGPPGTGKTL
CEEEEECCCCCCHHH		15.59-
885PhosphorylationLLYGPPGTGKTLLAG
EEECCCCCCHHHHHH		41.08-
887UbiquitinationYGPPGTGKTLLAGVI
ECCCCCCHHHHHHHH		35.52-
888PhosphorylationGPPGTGKTLLAGVIA
CCCCCCHHHHHHHHH		28.4822985185
902UbiquitinationARESRMNFISVKGPE
HHHHCCCEEEECCHH		3.00-
906UbiquitinationRMNFISVKGPELLSK
CCCEEEECCHHHHHH		63.06-
913UbiquitinationKGPELLSKYIGASEQ
CCHHHHHHHCCCCHH		40.64-
933UbiquitinationFIRAQAAKPCILFFD
HHHHHCCCCEEEEEC		43.36-
942UbiquitinationCILFFDEFESIAPRR
EEEEECCCHHCCCCC		10.85-
944PhosphorylationLFFDEFESIAPRRGH
EEECCCHHCCCCCCC		29.3924719451
1001UbiquitinationLRPGRLDKCVYCPPP
CCCCCCCCCEECCCH		30.14-
1143PhosphorylationSELGNGTSSDLSSQC
CCCCCCCCCCHHHHH		24.2128857561
1144PhosphorylationELGNGTSSDLSSQCL
CCCCCCCCCHHHHHH		42.2728857561
1147PhosphorylationNGTSSDLSSQCLSAP
CCCCCCHHHHHHCCC		24.2928857561
1148PhosphorylationGTSSDLSSQCLSAPS
CCCCCHHHHHHCCCC		32.0128857561
1172PhosphorylationPGKDQLFSQPPVLRT
CCCHHHHCCCCCHHC		50.8225159151
1179PhosphorylationSQPPVLRTASQEGCQ
CCCCCHHCCCHHHHH		26.8829255136
1181PhosphorylationPPVLRTASQEGCQEL
CCCHHCCCHHHHHHH		28.3129255136
1189PhosphorylationQEGCQELTQEQRDQL
HHHHHHHCHHHHHHH		29.3429396449
1201PhosphorylationDQLRADISIIKGRYR
HHHHHHHHEEECCCC		20.8621712546
1204UbiquitinationRADISIIKGRYRSQS
HHHHHEEECCCCCCC		35.35-
1207PhosphorylationISIIKGRYRSQSGED
HHEEECCCCCCCCCC		24.2423927012
1209PhosphorylationIIKGRYRSQSGEDES
EEECCCCCCCCCCCC		21.5529255136
1211PhosphorylationKGRYRSQSGEDESMN
ECCCCCCCCCCCCCC		45.4519664994
1216PhosphorylationSQSGEDESMNQPGPI
CCCCCCCCCCCCCCC		35.0425159151
1224UbiquitinationMNQPGPIKTRLAISQ
CCCCCCCHHHHHCCH		30.632190698
1257PhosphorylationWKNFAELYESFQNPK
HHHHHHHHHHHCCCC		10.8827642862
1259PhosphorylationNFAELYESFQNPKRR
HHHHHHHHHCCCCCC		20.6927251275
1264UbiquitinationYESFQNPKRRKNQSG
HHHHCCCCCCCCCCC		72.83-
1270PhosphorylationPKRRKNQSGTMFRPG
CCCCCCCCCCCCCCC		45.7025159151
1272PhosphorylationRRKNQSGTMFRPGQK
CCCCCCCCCCCCCCC		20.5528857561
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 PEX1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEX1_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 PEX1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PEX6_HUMANPEX6physical
9588209
PEX6_HUMANPEX6physical
9671729
Drug and Disease Associations
Kegg Disease
H00205 Zellweger syndrome spectrum, including: Zellweger syndrome (ZS); Adrenoleukodystrophy, neonatal (NAL
OMIM Disease
214100Peroxisome biogenesis disorder complementation group 1 (PBD-CG1)
214100Peroxisome biogenesis disorder 1A (PBD1A)
601539Peroxisome biogenesis disorder 1B (PBD1B)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PEX1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1181 AND SER-1211, ANDMASS SPECTROMETRY.
"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-1181, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-833, AND MASSSPECTROMETRY.

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