PEX14_HUMAN - dbPTM
PEX14_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PEX14_HUMAN
UniProt AC O75381
Protein Name Peroxisomal membrane protein PEX14
Gene Name PEX14
Organism Homo sapiens (Human).
Sequence Length 377
Subcellular Localization Peroxisome membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description Peroxisome membrane protein that is an essential component of the peroxisomal import machinery. Functions as a docking factor for the predominantly cytoplasmic PTS1 receptor (PEX5). Plays a key role for peroxisome movement through a direct interaction with tubulin..
Protein Sequence MASSEQAEQPSQPSSTPGSENVLPREPLIATAVKFLQNSRVRQSPLATRRAFLKKKGLTDEEIDMAFQQSGTAADEPSSLGPATQVVPVQPPHLISQPYSPAGSRWRDYGALAIIMAGIAFGFHQLYKKYLLPLILGGREDRKQLERMEAGLSELSGSVAQTVTQLQTTLASVQELLIQQQQKIQELAHELAAAKATTSTNWILESQNINELKSEINSLKGLLLNRRQFPPSPSAPKIPSWQIPVKSPSPSSPAAVNHHSSSDISPVSNESTSSSPGKEGHSPEGSTVTYHLLGPQEEGEGVVDVKGQVRMEVQGEEEKREDKEDEEDEEDDDVSHVDEEDCLGVQREDRRGGDGQINEQVEKLRRPEGASNESERD
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------MASSEQAEQ
------CCCHHHCCC		23.0525944712
3Phosphorylation-----MASSEQAEQP
-----CCCHHHCCCC		32.8621955146
4Phosphorylation----MASSEQAEQPS
----CCCHHHCCCCC		24.9621955146
11PhosphorylationSEQAEQPSQPSSTPG
HHHCCCCCCCCCCCC		55.1821955146
14PhosphorylationAEQPSQPSSTPGSEN
CCCCCCCCCCCCCCC		38.9321955146
15PhosphorylationEQPSQPSSTPGSENV
CCCCCCCCCCCCCCC		45.3525159151
15UbiquitinationEQPSQPSSTPGSENV
CCCCCCCCCCCCCCC		45.3522817900
16PhosphorylationQPSQPSSTPGSENVL
CCCCCCCCCCCCCCC		35.6925159151
19PhosphorylationQPSSTPGSENVLPRE
CCCCCCCCCCCCCCC		27.4821955146
34 (in isoform 1)Ubiquitination-37.5821890473
34 (in isoform 2)Ubiquitination-37.5821890473
34UbiquitinationPLIATAVKFLQNSRV
HHHHHHHHHHHCCCC		37.5823000965
34AcetylationPLIATAVKFLQNSRV
HHHHHHHHHHHCCCC		37.5819608861
39PhosphorylationAVKFLQNSRVRQSPL
HHHHHHCCCCCCCHH		21.1327067055
44PhosphorylationQNSRVRQSPLATRRA
HCCCCCCCHHHHHHH		16.0030266825
48UbiquitinationVRQSPLATRRAFLKK
CCCCHHHHHHHHHHH		28.5021890473
96PhosphorylationVQPPHLISQPYSPAG
CCCCCCCCCCCCCCC		31.3122468782
104PhosphorylationQPYSPAGSRWRDYGA
CCCCCCCCCHHHHHH		30.6722468782
149UbiquitinationRKQLERMEAGLSELS
HHHHHHHHHHHHHHH		45.8922817900
156UbiquitinationEAGLSELSGSVAQTV
HHHHHHHHHHHHHHH		25.6021890473
168O-linked_GlycosylationQTVTQLQTTLASVQE
HHHHHHHHHHHHHHH		32.16OGP
170 (in isoform 2)Ubiquitination-3.6721890473
170UbiquitinationVTQLQTTLASVQELL
HHHHHHHHHHHHHHH		3.6722817900
177 (in isoform 2)Ubiquitination-3.0621890473
177UbiquitinationLASVQELLIQQQQKI
HHHHHHHHHHHHHHH		3.0621890473
184UbiquitinationLIQQQQKIQELAHEL
HHHHHHHHHHHHHHH		3.1522817900
191UbiquitinationIQELAHELAAAKATT
HHHHHHHHHHHHCHH		2.5621890473
194UbiquitinationLAHELAAAKATTSTN
HHHHHHHHHCHHCCH		9.0822817900
195UbiquitinationAHELAAAKATTSTNW
HHHHHHHHCHHCCHH		41.3529967540
201UbiquitinationAKATTSTNWILESQN
HHCHHCCHHHHHCCC		24.4521890473
213UbiquitinationSQNINELKSEINSLK
CCCHHHHHHHHHHHH		39.6021906983
213 (in isoform 1)Ubiquitination-39.6021890473
218PhosphorylationELKSEINSLKGLLLN
HHHHHHHHHHHHHHC		36.8030576142
220UbiquitinationKSEINSLKGLLLNRR
HHHHHHHHHHHHCCC		47.5422817900
220 (in isoform 1)Ubiquitination-47.5421890473
227UbiquitinationKGLLLNRRQFPPSPS
HHHHHCCCCCCCCCC		41.2222817900
232PhosphorylationNRRQFPPSPSAPKIP
CCCCCCCCCCCCCCC		31.5530266825
234PhosphorylationRQFPPSPSAPKIPSW
CCCCCCCCCCCCCCC		62.6330266825
234UbiquitinationRQFPPSPSAPKIPSW
CCCCCCCCCCCCCCC		62.6321890473
240PhosphorylationPSAPKIPSWQIPVKS
CCCCCCCCCCCCCCC		34.7825002506
246UbiquitinationPSWQIPVKSPSPSSP
CCCCCCCCCCCCCCC		51.8229967540
247PhosphorylationSWQIPVKSPSPSSPA
CCCCCCCCCCCCCCC		30.7425159151
249PhosphorylationQIPVKSPSPSSPAAV
CCCCCCCCCCCCCHH		44.5025159151
251PhosphorylationPVKSPSPSSPAAVNH
CCCCCCCCCCCHHCC		53.9825159151
252PhosphorylationVKSPSPSSPAAVNHH
CCCCCCCCCCHHCCC		23.1825159151
260PhosphorylationPAAVNHHSSSDISPV
CCHHCCCCCCCCCCC		24.8025159151
261PhosphorylationAAVNHHSSSDISPVS
CHHCCCCCCCCCCCC		27.8925159151
262PhosphorylationAVNHHSSSDISPVSN
HHCCCCCCCCCCCCC		41.8125159151
265PhosphorylationHHSSSDISPVSNEST
CCCCCCCCCCCCCCC		25.0025159151
268PhosphorylationSSDISPVSNESTSSS
CCCCCCCCCCCCCCC		37.9628176443
271PhosphorylationISPVSNESTSSSPGK
CCCCCCCCCCCCCCC		37.5323401153
272PhosphorylationSPVSNESTSSSPGKE
CCCCCCCCCCCCCCC		26.8425159151
273PhosphorylationPVSNESTSSSPGKEG
CCCCCCCCCCCCCCC		37.7926503892
274PhosphorylationVSNESTSSSPGKEGH
CCCCCCCCCCCCCCC		40.4125159151
275PhosphorylationSNESTSSSPGKEGHS
CCCCCCCCCCCCCCC		37.1226503892
282PhosphorylationSPGKEGHSPEGSTVT
CCCCCCCCCCCCEEE		35.1930266825
286PhosphorylationEGHSPEGSTVTYHLL
CCCCCCCCEEEEEEC		20.3130266825
287PhosphorylationGHSPEGSTVTYHLLG
CCCCCCCEEEEEECC		27.9429255136
289PhosphorylationSPEGSTVTYHLLGPQ
CCCCCEEEEEECCCC		12.8129255136
290PhosphorylationPEGSTVTYHLLGPQE
CCCCEEEEEECCCCC		6.0229255136
299UbiquitinationLLGPQEEGEGVVDVK
ECCCCCCCCCEEECC		35.8821890473
306UbiquitinationGEGVVDVKGQVRMEV
CCCEEECCCEEEEEE		38.8833845483
320UbiquitinationVQGEEEKREDKEDEE
ECCCHHCCCCCCCCC		61.7021890473
320 (in isoform 2)Ubiquitination-61.7021890473
334UbiquitinationEDEEDDDVSHVDEED
CCCCCCCCCCCCHHH		5.6921890473
335PhosphorylationDEEDDDVSHVDEEDC
CCCCCCCCCCCHHHH		25.4521955146
344UbiquitinationVDEEDCLGVQREDRR
CCHHHHCCCCCCCCC		21.6121890473
351MethylationGVQREDRRGGDGQIN
CCCCCCCCCCCCHHH		66.81115487039
363UbiquitinationQINEQVEKLRRPEGA
HHHHHHHHHHCCCCC		48.7322817900
363 (in isoform 1)Ubiquitination-48.7321890473
371PhosphorylationLRRPEGASNESERD-
HHCCCCCCCCCCCC-		52.5721955146
374PhosphorylationPEGASNESERD----
CCCCCCCCCCC----		42.0321955146
377UbiquitinationASNESERD-------
CCCCCCCC-------		59.8421890473
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 PEX14_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PEX14_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 PEX14_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED8_HUMANMED8physical
16169070
ZHX1_HUMANZHX1physical
16169070
SMRC2_HUMANSMARCC2physical
16169070
PEX5_HUMANPEX5physical
10837480
PEX5_HUMANPEX5physical
11865044
PEX13_HUMANPEX13physical
11865044
PEX5_HUMANPEX5physical
10212238
PEX7_HUMANPEX7physical
10212238
PEX14_HUMANPEX14physical
10212238
PEX5_HUMANPEX5physical
12096124
PEX14_HUMANPEX14physical
12096124
PEX19_HUMANPEX19physical
12096124
PEX13_HUMANPEX13physical
12096124
PEX5_HUMANPEX5physical
10022913
ABCD3_HUMANABCD3physical
21525035
ADAS_HUMANAGPSphysical
21525035
ATAD1_HUMANATAD1physical
21525035
CNOT1_HUMANCNOT1physical
21525035
DHRS4_HUMANDHRS4physical
21525035
FACR1_HUMANFAR1physical
21525035
GNPAT_HUMANGNPATphysical
21525035
DHB4_HUMANHSD17B4physical
21525035
IMDH2_HUMANIMPDH2physical
21525035
MP2K2_HUMANMAP2K2physical
21525035
PEX10_HUMANPEX10physical
21525035
PEX12_HUMANPEX12physical
21525035
PEX13_HUMANPEX13physical
21525035
PEX14_HUMANPEX14physical
21525035
PEX16_HUMANPEX16physical
21525035
PEX19_HUMANPEX19physical
21525035
PEX3_HUMANPEX3physical
21525035
PEX5_HUMANPEX5physical
21525035
PEX2_HUMANPEX2physical
21525035
TTC1_HUMANTTC1physical
21525035
ARHG2_HUMANARHGEF2physical
21525035
TCPB_HUMANCCT2physical
21525035
TCPG_HUMANCCT3physical
21525035
TCPD_HUMANCCT4physical
21525035
TCPE_HUMANCCT5physical
21525035
TCPZ_HUMANCCT6Aphysical
21525035
TCPH_HUMANCCT7physical
21525035
TCPQ_HUMANCCT8physical
21525035
CN37_HUMANCNPphysical
21525035
DCTN1_HUMANDCTN1physical
21525035
DNM1L_HUMANDNM1Lphysical
21525035
DYN2_HUMANDNM2physical
21525035
DYHC1_HUMANDYNC1H1physical
21525035
DC1I2_HUMANDYNC1I2physical
21525035
DYHC2_HUMANDYNC2H1physical
21525035
IQGA1_HUMANIQGAP1physical
21525035
IQGA2_HUMANIQGAP2physical
21525035
KIF11_HUMANKIF11physical
21525035
LPPRC_HUMANLRPPRCphysical
21525035
TBB8_HUMANTUBB8physical
21525035
TCPA_HUMANTCP1physical
21525035
TBA1A_HUMANTUBA1Aphysical
21525035
TBA4A_HUMANTUBA4Aphysical
21525035
TBB5_HUMANTUBBphysical
21525035
TBB2A_HUMANTUBB2Aphysical
21525035
TBB2B_HUMANTUBB2Bphysical
21525035
TBB4B_HUMANTUBB4Bphysical
21525035
TBB3_HUMANTUBB3physical
21525035
TBB4A_HUMANTUBB4Aphysical
21525035
TBB6_HUMANTUBB6physical
21525035
TBG2_HUMANTUBG2physical
21525035
Drug and Disease Associations
Kegg Disease
H00205 Zellweger syndrome spectrum, including: Zellweger syndrome (ZS); Adrenoleukodystrophy, neonatal (NAL
OMIM Disease
614887Peroxisome biogenesis disorder complementation group K (PBD-CGK)
614887Peroxisome biogenesis disorder 13A (PBD13A)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PEX14_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.
"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-34, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, AND MASSSPECTROMETRY.

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