SNX29_HUMAN - dbPTM
SNX29_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNX29_HUMAN
UniProt AC Q8TEQ0
Protein Name Sorting nexin-29
Gene Name SNX29
Organism Homo sapiens (Human).
Sequence Length 813
Subcellular Localization
Protein Description
Protein Sequence MSGSQNNDKRQFLLERLLDAVKQCQIRFGGRKEIASDSDSRVTCLCAQFEAVLQHGLKRSRGLALTAAAIKQAAGFASKTETEPVFWYYVKEVLNKHELQRFYSLRHIASDVGRGRAWLRCALNEHSLERYLHMLLADRCRLSTFYEDWSFVMDEERSSMLPTMAAGLNSILFAINIDNKDLNGQSKFAPTVSDLLKESTQNVTSLLKESTQGVSSLFREITASSAVSILIKPEQETDPLPVVSRNVSADAKCKKERKKKKKVTNIISFDDEEDEQNSGDVFKKTPGAGESSEDNSDRSSVNIMSAFESPFGPNSNGSQSSNSWKIDSLSLNGEFGYQKLDVKSIDDEDVDENEDDVYGNSSGRKHRGHSESPEKPLEGNTCLSQMHSWAPLKVLHNDSDILFPVSGVGSYSPADAPLGSLENGTGPEDHVLPDPGLRYSVEASSPGHGSPLSSLLPSASVPESMTISELRQATVAMMNRKDELEEENRSLRNLLDGEMEHSAALRQEVDTLKRKVAEQEERQGMKVQALARENEVLKVQLKKYVGAVQMLKREGQTAEVPNLWSVDGEVTVAEQKPGEIAEELASSYERKLIEVAEMHGELIEFNERLHRALVAKEALVSQMRQELIDLRGPVPGDLSQTSEDQSLSDFEISNRALINVWIPSVFLRGKAANAFHVYQVYIRIKDDEWNIYRRYTEFRSLHHKLQNKYPQVRAYNFPPKKAIGNKDAKFVEERRKQLQNYLRSVMNKVIQMVPEFAASPKKETLIQLMPFFVDITPPGEPVNSRPKAASRFPKLSRGQPRETRNVEPQSGDL
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
71UbiquitinationALTAAAIKQAAGFAS
HHHHHHHHHHCCCCC
29.2029967540
96MalonylationYVKEVLNKHELQRFY
HHHHHCCHHHHHHHH
34.0026320211
104PhosphorylationHELQRFYSLRHIASD
HHHHHHHHHHHHHHH
19.0624719451
163O-linked_GlycosylationERSSMLPTMAAGLNS
HHHCCHHHHHHHHHH
18.5829351928
187UbiquitinationKDLNGQSKFAPTVSD
CCCCCCCCCCCCHHH
37.3429967540
193PhosphorylationSKFAPTVSDLLKEST
CCCCCCHHHHHHHHC
25.6428857561
199PhosphorylationVSDLLKESTQNVTSL
HHHHHHHHCHHHHHH
33.4328348404
200PhosphorylationSDLLKESTQNVTSLL
HHHHHHHCHHHHHHH
25.8428348404
205PhosphorylationESTQNVTSLLKESTQ
HHCHHHHHHHHHHHH
27.6724719451
210PhosphorylationVTSLLKESTQGVSSL
HHHHHHHHHHHHHHH
25.1728857561
211PhosphorylationTSLLKESTQGVSSLF
HHHHHHHHHHHHHHH
30.3628857561
216PhosphorylationESTQGVSSLFREITA
HHHHHHHHHHHHHHH
29.1724719451
254PhosphorylationVSADAKCKKERKKKK
CCCCCHHHHHHHCCC
57.8917081983
256PhosphorylationADAKCKKERKKKKKV
CCCHHHHHHHCCCCC
56.0517081983
257PhosphorylationDAKCKKERKKKKKVT
CCHHHHHHHCCCCCC
66.0417081983
261PhosphorylationKKERKKKKKVTNIIS
HHHHHCCCCCCEEEE
62.4517081983
263PhosphorylationERKKKKKVTNIISFD
HHHCCCCCCEEEECC
7.3217081983
264PhosphorylationRKKKKKVTNIISFDD
HHCCCCCCEEEECCC
29.5830624053
268PhosphorylationKKVTNIISFDDEEDE
CCCCEEEECCCCCCH
20.8730266825
278PhosphorylationDEEDEQNSGDVFKKT
CCCCHHCCCCCCCCC
35.7425159151
291PhosphorylationKTPGAGESSEDNSDR
CCCCCCCCCCCCCCC
37.8017081983
292PhosphorylationTPGAGESSEDNSDRS
CCCCCCCCCCCCCCC
44.67-
328PhosphorylationSNSWKIDSLSLNGEF
CCCEEEEEEEECCCC
24.2730266825
330PhosphorylationSWKIDSLSLNGEFGY
CEEEEEEEECCCCCE
24.6023401153
337PhosphorylationSLNGEFGYQKLDVKS
EECCCCCEEEECCCC
14.0623403867
344PhosphorylationYQKLDVKSIDDEDVD
EEEECCCCCCHHHCC
30.9723401153
358PhosphorylationDENEDDVYGNSSGRK
CCCCCCCCCCCCCCC
19.9925884760
361PhosphorylationEDDVYGNSSGRKHRG
CCCCCCCCCCCCCCC
29.7923403867
362PhosphorylationDDVYGNSSGRKHRGH
CCCCCCCCCCCCCCC
46.7623403867
370PhosphorylationGRKHRGHSESPEKPL
CCCCCCCCCCCCCCC
42.4628450419
372PhosphorylationKHRGHSESPEKPLEG
CCCCCCCCCCCCCCC
41.1827422710
381PhosphorylationEKPLEGNTCLSQMHS
CCCCCCCCHHHHHHH
26.1928450419
384PhosphorylationLEGNTCLSQMHSWAP
CCCCCHHHHHHHCCC
27.8328450419
388PhosphorylationTCLSQMHSWAPLKVL
CHHHHHHHCCCEEEE
21.4226330541
410PhosphorylationFPVSGVGSYSPADAP
EECCCCCCCCCCCCC
21.7425921289
411PhosphorylationPVSGVGSYSPADAPL
ECCCCCCCCCCCCCC
16.8525921289
412PhosphorylationVSGVGSYSPADAPLG
CCCCCCCCCCCCCCC
18.4728857561
420PhosphorylationPADAPLGSLENGTGP
CCCCCCCCCCCCCCC
39.9525921289
425PhosphorylationLGSLENGTGPEDHVL
CCCCCCCCCCCCCCC
62.2328348404
439PhosphorylationLPDPGLRYSVEASSP
CCCCCCCEEEEECCC
23.3128450419
440PhosphorylationPDPGLRYSVEASSPG
CCCCCCEEEEECCCC
13.6728450419
444PhosphorylationLRYSVEASSPGHGSP
CCEEEEECCCCCCCC
24.4530278072
445PhosphorylationRYSVEASSPGHGSPL
CEEEEECCCCCCCCH
41.7830278072
450PhosphorylationASSPGHGSPLSSLLP
ECCCCCCCCHHHHCC
19.5930278072
453PhosphorylationPGHGSPLSSLLPSAS
CCCCCCHHHHCCCCC
23.4821712546
454PhosphorylationGHGSPLSSLLPSASV
CCCCCHHHHCCCCCC
41.4228464451
458PhosphorylationPLSSLLPSASVPESM
CHHHHCCCCCCCCCC
32.9028450419
460PhosphorylationSSLLPSASVPESMTI
HHHCCCCCCCCCCCH
42.4128450419
464PhosphorylationPSASVPESMTISELR
CCCCCCCCCCHHHHH
18.3720068231
466PhosphorylationASVPESMTISELRQA
CCCCCCCCHHHHHHH
30.5420068231
468PhosphorylationVPESMTISELRQATV
CCCCCCHHHHHHHHH
22.7820068231
490PhosphorylationELEEENRSLRNLLDG
HHHHHHHHHHHHHHH
43.1720071362
502PhosphorylationLDGEMEHSAALRQEV
HHHHHHHHHHHHHHH
11.2620071362
526UbiquitinationQEERQGMKVQALARE
HHHHCCCHHHHHHHC
37.7129967540
544PhosphorylationLKVQLKKYVGAVQML
HHHHHHHHHHHHHHH
11.5222817900
616UbiquitinationLHRALVAKEALVSQM
HHHHHHHHHHHHHHH
35.72-
639PhosphorylationGPVPGDLSQTSEDQS
CCCCCCCHHCCCCCC
35.8323401153
641PhosphorylationVPGDLSQTSEDQSLS
CCCCCHHCCCCCCCC
30.6122617229
642PhosphorylationPGDLSQTSEDQSLSD
CCCCHHCCCCCCCCH
31.3830278072
646PhosphorylationSQTSEDQSLSDFEIS
HHCCCCCCCCHHHHC
42.0122617229
648PhosphorylationTSEDQSLSDFEISNR
CCCCCCCCHHHHCCH
45.5622115753
653PhosphorylationSLSDFEISNRALINV
CCCHHHHCCHHHHEE
17.0528450419
709PhosphorylationHHKLQNKYPQVRAYN
HHHHHHCCCCHHCCC
13.3726074081
759PhosphorylationMVPEFAASPKKETLI
HHHHHHCCCCHHHHH
33.5522210691
764PhosphorylationAASPKKETLIQLMPF
HCCCCHHHHHHHCEE
37.7322210691
776PhosphorylationMPFFVDITPPGEPVN
CEEECCCCCCCCCCC
20.9722210691
784PhosphorylationPPGEPVNSRPKAASR
CCCCCCCCCCCHHHC
50.6322210691
790PhosphorylationNSRPKAASRFPKLSR
CCCCCHHHCCCCCCC
39.0424719451
810PhosphorylationTRNVEPQSGDL----
CCCCCCCCCCC----
45.0225159151

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 SNX29_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNX29_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 SNX29_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of SNX29_HUMAN !!

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 SNX29_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-810, AND MASSSPECTROMETRY.
"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-639; THR-641; SER-642;SER-646; SER-648 AND SER-810, AND MASS SPECTROMETRY.

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