VPS35_HUMAN - dbPTM
VPS35_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPS35_HUMAN
UniProt AC Q96QK1
Protein Name Vacuolar protein sorting-associated protein 35
Gene Name VPS35
Organism Homo sapiens (Human).
Sequence Length 796
Subcellular Localization Cytoplasm. Membrane
Peripheral membrane protein. Endosome . Early endosome . Late endosome . Localizes to tubular profiles adjacent to endosomes.
Protein Description Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may also contribute to cargo selectivity thus questioning the classical function of the CSC. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5 (Probable). Required for retrograde transport of lysosomal enzyme receptor IGF2R and SLC11A2. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). [PubMed: 15078903]
Protein Sequence MPTTQQSPQDEQEKLLDEAIQAVKVQSFQMKRCLDKNKLMDALKHASNMLGELRTSMLSPKSYYELYMAISDELHYLEVYLTDEFAKGRKVADLYELVQYAGNIIPRLYLLITVGVVYVKSFPQSRKDILKDLVEMCRGVQHPLRGLFLRNYLLQCTRNILPDEGEPTDEETTGDISDSMDFVLLNFAEMNKLWVRMQHQGHSRDREKRERERQELRILVGTNLVRLSQLEGVNVERYKQIVLTGILEQVVNCRDALAQEYLMECIIQVFPDEFHLQTLNPFLRACAELHQNVNVKNIIIALIDRLALFAHREDGPGIPADIKLFDIFSQQVATVIQSRQDMPSEDVVSLQVSLINLAMKCYPDRVDYVDKVLETTVEIFNKLNLEHIATSSAVSKELTRLLKIPVDTYNNILTVLKLKHFHPLFEYFDYESRKSMSCYVLSNVLDYNTEIVSQDQVDSIMNLVSTLIQDQPDQPVEDPDPEDFADEQSLVGRFIHLLRSEDPDQQYLILNTARKHFGAGGNQRIRFTLPPLVFAAYQLAFRYKENSKVDDKWEKKCQKIFSFAHQTISALIKAELAELPLRLFLQGALAAGEIGFENHETVAYEFMSQAFSLYEDEISDSKAQLAAITLIIGTFERMKCFSEENHEPLRTQCALAASKLLKKPDQGRAVSTCAHLFWSGRNTDKNGEELHGGKRVMECLKKALKIANQCMDPSLQVQLFIEILNRYIYFYEKENDAVTIQVLNQLIQKIREDLPNLESSEETEQINKHFHNTLEHLRLRRESPESEGPIYEGLIL
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
3Phosphorylation-----MPTTQQSPQD
-----CCCCCCCCHH
35.6224732914
4Phosphorylation----MPTTQQSPQDE
----CCCCCCCCHHH
20.8121955146
7Phosphorylation-MPTTQQSPQDEQEK
-CCCCCCCCHHHHHH
18.0823401153
14UbiquitinationSPQDEQEKLLDEAIQ
CCHHHHHHHHHHHHH
54.7824816145
24UbiquitinationDEAIQAVKVQSFQMK
HHHHHHHHHCHHHHH
37.2621906983
31AcetylationKVQSFQMKRCLDKNK
HHCHHHHHHHCCHHH
29.2225953088
382-HydroxyisobutyrylationKRCLDKNKLMDALKH
HHHCCHHHHHHHHHH
51.43-
38MalonylationKRCLDKNKLMDALKH
HHHCCHHHHHHHHHH
51.4326320211
38AcetylationKRCLDKNKLMDALKH
HHHCCHHHHHHHHHH
51.4325953088
44AcetylationNKLMDALKHASNMLG
HHHHHHHHHHHHHHH
38.5525953088
44UbiquitinationNKLMDALKHASNMLG
HHHHHHHHHHHHHHH
38.5532015554
47PhosphorylationMDALKHASNMLGELR
HHHHHHHHHHHHHHH
23.6120860994
59PhosphorylationELRTSMLSPKSYYEL
HHHHHCCCCHHHHHH
22.95-
64UbiquitinationMLSPKSYYELYMAIS
CCCCHHHHHHHHHHH
13.4224816145
67PhosphorylationPKSYYELYMAISDEL
CHHHHHHHHHHHCHH
3.44-
90UbiquitinationDEFAKGRKVADLYEL
HHHHCCCCHHHHHHH
50.9033845483
102UbiquitinationYELVQYAGNIIPRLY
HHHHHHHCCHHHHHH
22.4224816145
109PhosphorylationGNIIPRLYLLITVGV
CCHHHHHHHHHHHEE
10.7620068231
125PhosphorylationYVKSFPQSRKDILKD
HHHCCCHHHHHHHHH
41.3520068231
131UbiquitinationQSRKDILKDLVEMCR
HHHHHHHHHHHHHHH
49.7224816145
137GlutathionylationLKDLVEMCRGVQHPL
HHHHHHHHHHCCCHH
1.8522555962
145MethylationRGVQHPLRGLFLRNY
HHCCCHHHHHHHHHH
44.19115919853
177PhosphorylationEETTGDISDSMDFVL
CCCCCCCCHHCCEEE
28.5121601212
329UbiquitinationIKLFDIFSQQVATVI
HHHHHHHHHHHHHHH
21.7521890473
350UbiquitinationPSEDVVSLQVSLINL
CCCCCHHHHHHHHHH
3.8321890473
353PhosphorylationDVVSLQVSLINLAMK
CCHHHHHHHHHHHHH
15.57-
367UbiquitinationKCYPDRVDYVDKVLE
HHCCCCCHHHHHHHH
38.3421890473
371UbiquitinationDRVDYVDKVLETTVE
CCCHHHHHHHHHHHH
38.3829967540
382UbiquitinationTTVEIFNKLNLEHIA
HHHHHHHHCCHHHHH
28.1829967540
388UbiquitinationNKLNLEHIATSSAVS
HHCCHHHHHCCHHHH
3.0621890473
390PhosphorylationLNLEHIATSSAVSKE
CCHHHHHCCHHHHHH
23.7020068231
391PhosphorylationNLEHIATSSAVSKEL
CHHHHHCCHHHHHHH
13.7920068231
392PhosphorylationLEHIATSSAVSKELT
HHHHHCCHHHHHHHH
28.4720068231
395PhosphorylationIATSSAVSKELTRLL
HHCCHHHHHHHHHHH
21.8220068231
396UbiquitinationATSSAVSKELTRLLK
HCCHHHHHHHHHHHC
50.5822817900
403UbiquitinationKELTRLLKIPVDTYN
HHHHHHHCCCHHHHH
49.9429967540
408PhosphorylationLLKIPVDTYNNILTV
HHCCCHHHHHCHHHH
28.5129759185
414PhosphorylationDTYNNILTVLKLKHF
HHHHCHHHHHHHCCC
21.7229759185
417UbiquitinationNNILTVLKLKHFHPL
HCHHHHHHHCCCCHH
51.6721890473
419AcetylationILTVLKLKHFHPLFE
HHHHHHHCCCCHHHH
42.5127452117
419UbiquitinationILTVLKLKHFHPLFE
HHHHHHHCCCCHHHH
42.5129967540
432PhosphorylationFEYFDYESRKSMSCY
HHHCCCCCCCCCHHE
38.49-
435PhosphorylationFDYESRKSMSCYVLS
CCCCCCCCCHHEHHH
18.15-
437PhosphorylationYESRKSMSCYVLSNV
CCCCCCCHHEHHHHH
14.91-
448UbiquitinationLSNVLDYNTEIVSQD
HHHHCCCCCCCCCHH
30.7922053931
486UbiquitinationPDPEDFADEQSLVGR
CCHHHCCCHHHHHHH
55.2322053931
507PhosphorylationSEDPDQQYLILNTAR
CCCCCCCEEEEECCH
7.0628152594
512PhosphorylationQQYLILNTARKHFGA
CCEEEEECCHHHCCC
25.13-
515UbiquitinationLILNTARKHFGAGGN
EEEECCHHHCCCCCC
40.6021890473
547PhosphorylationAFRYKENSKVDDKWE
HHHHHHCCCCCHHHH
34.8428270605
552AcetylationENSKVDDKWEKKCQK
HCCCCCHHHHHHHHH
53.4325953088
555AcetylationKVDDKWEKKCQKIFS
CCCHHHHHHHHHHHH
58.7023749302
572UbiquitinationHQTISALIKAELAEL
HHHHHHHHHHHHHHC
3.8824816145
573UbiquitinationQTISALIKAELAELP
HHHHHHHHHHHHHCC
36.3433845483
592UbiquitinationLQGALAAGEIGFENH
HHHHHHHCCCCCCCC
22.8027667366
595UbiquitinationALAAGEIGFENHETV
HHHHCCCCCCCCHHH
21.3624816145
610UbiquitinationAYEFMSQAFSLYEDE
HHHHHHHHHHHHHHH
6.6824816145
627UbiquitinationDSKAQLAAITLIIGT
CCHHHHHHHHHHHHH
12.1427667366
629PhosphorylationKAQLAAITLIIGTFE
HHHHHHHHHHHHHHH
13.7420068231
630UbiquitinationAQLAAITLIIGTFER
HHHHHHHHHHHHHHH
1.8827667366
633UbiquitinationAAITLIIGTFERMKC
HHHHHHHHHHHHHHC
19.8424816145
639UbiquitinationIGTFERMKCFSEENH
HHHHHHHHCCCCCCC
38.0524816145
658PhosphorylationTQCALAASKLLKKPD
HHHHHHHHHHCCCCC
20.4428857561
659UbiquitinationQCALAASKLLKKPDQ
HHHHHHHHHCCCCCC
53.7833845483
659AcetylationQCALAASKLLKKPDQ
HHHHHHHHHCCCCCC
53.7825953088
662AcetylationLAASKLLKKPDQGRA
HHHHHHCCCCCCCCC
73.1025953088
6622-HydroxyisobutyrylationLAASKLLKKPDQGRA
HHHHHHCCCCCCCCC
73.10-
662UbiquitinationLAASKLLKKPDQGRA
HHHHHHCCCCCCCCC
73.1024816145
665UbiquitinationSKLLKKPDQGRAVST
HHHCCCCCCCCCCHH
72.8827667366
671PhosphorylationPDQGRAVSTCAHLFW
CCCCCCCHHHHHHHH
19.4528857561
683PhosphorylationLFWSGRNTDKNGEEL
HHHCCCCCCCCCCCC
47.17-
6942-HydroxyisobutyrylationGEELHGGKRVMECLK
CCCCCCCHHHHHHHH
46.54-
694UbiquitinationGEELHGGKRVMECLK
CCCCCCCHHHHHHHH
46.5427667366
694AcetylationGEELHGGKRVMECLK
CCCCCCCHHHHHHHH
46.547619357
701AcetylationKRVMECLKKALKIAN
HHHHHHHHHHHHHHH
47.8925953088
714PhosphorylationANQCMDPSLQVQLFI
HHHHCCHHHHHHHHH
27.4620068231
759PhosphorylationEDLPNLESSEETEQI
HHCCCCCCHHHHHHH
46.3325627689
760PhosphorylationDLPNLESSEETEQIN
HCCCCCCHHHHHHHH
30.0325627689
768AcetylationEETEQINKHFHNTLE
HHHHHHHHHHHHHHH
49.6421466224
768UbiquitinationEETEQINKHFHNTLE
HHHHHHHHHHHHHHH
49.6429967540
783PhosphorylationHLRLRRESPESEGPI
HHHHHHCCCCCCCCC
31.9619664994
786PhosphorylationLRRESPESEGPIYEG
HHHCCCCCCCCCCCC
51.7630266825
791PhosphorylationPESEGPIYEGLIL--
CCCCCCCCCCCCC--
13.6928796482

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 VPS35_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPS35_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 VPS35_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS35_YEASTVPS35genetic
17916227
WAC2C_HUMANFAM21Cphysical
20923837
TBCD5_HUMANTBC1D5physical
22354992
A4_HUMANAPPphysical
21832049
VPS36_HUMANVPS36physical
22939629
WDR5_HUMANWDR5physical
22939629
VPS35_HUMANVPS35physical
23452853
AN32E_HUMANANP32Ephysical
22863883
COR1C_HUMANCORO1Cphysical
22863883
NIBL1_HUMANFAM129Bphysical
22863883
H33_HUMANH3F3Aphysical
22863883
NUDC_HUMANNUDCphysical
22863883
SAP_HUMANPSAPphysical
22863883
GLYM_HUMANSHMT2physical
22863883
SNX2_HUMANSNX2physical
22863883
SNX6_HUMANSNX6physical
22863883
UBP48_HUMANUSP48physical
22863883
SNX3_HUMANSNX3physical
24344282
NRAM2_HUMANSLC11A2physical
24344282
VP26A_HUMANVPS26Aphysical
24344282
VPS29_HUMANVPS29physical
24344282
VP13A_HUMANVPS13Aphysical
26344197
VPS29_HUMANVPS29physical
26344197
AIMP2_HUMANAIMP2physical
28383562
LAMP2_HUMANLAMP2physical
28383562

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614203Parkinson disease 17 (PARK17)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VPS35_HUMAN

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Related Literatures of Post-Translational Modification

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