TGON2_HUMAN - dbPTM
TGON2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TGON2_HUMAN
UniProt AC O43493
Protein Name Trans-Golgi network integral membrane protein 2
Gene Name TGOLN2
Organism Homo sapiens (Human).
Sequence Length 479
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane
Single-pass type I membrane protein. Primarily in trans-Golgi network. Cycles between the trans-Golgi network and the cell surface returning via endoso
Protein Description May be involved in regulating membrane traffic to and from trans-Golgi network..
Protein Sequence MRFVVALVLLNVAAAGAVPLLATESVKQEEAGVRPSAGNVSTHPSLSQRPGGSTKSHPEPQTPKDSPSKSSAEAQTPEDTPNKSGAEAKTQKDSSNKSGAEAKTQKGSTSKSGSEAQTTKDSTSKSHPELQTPKDSTGKSGAEAQTPEDSPNRSGAEAKTQKDSPSKSGSEAQTTKDVPNKSGADGQTPKDGSSKSGAEDQTPKDVPNKSGAEKQTPKDGSNKSGAEEQGPIDGPSKSGAEEQTSKDSPNKVVPEQPSRKDHSKPISNPSDNKELPKADTNQLADKGKLSPHAFKTESGEETDLISPPQEEVKSSEPTEDVEPKEAEDDDTGPEEGSPPKEEKEKMSGSASSENREGTLSDSTGSEKDDLYPNGSGNGSAESSHFFAYLVTAAILVAVLYIAHHNKRKIIAFVLEGKRSKVTRRPKASDYQRLDQKYVLILNVFPAPPKRSFFPVLTEWYIPLEKDERHQWIVLLSFQL
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
23O-linked_GlycosylationGAVPLLATESVKQEE
CCCCCCCCCCHHHHH
28.85OGP
36O-linked_GlycosylationEEAGVRPSAGNVSTH
HHCCCCCCCCCCCCC
37.9455833463
39N-linked_GlycosylationGVRPSAGNVSTHPSL
CCCCCCCCCCCCCCH
25.04UniProtKB CARBOHYD
41O-linked_GlycosylationRPSAGNVSTHPSLSQ
CCCCCCCCCCCCHHC
25.6255833467
42O-linked_GlycosylationPSAGNVSTHPSLSQR
CCCCCCCCCCCHHCC
33.2655833471
45O-linked_GlycosylationGNVSTHPSLSQRPGG
CCCCCCCCHHCCCCC
32.8055833475
47O-linked_GlycosylationVSTHPSLSQRPGGST
CCCCCCHHCCCCCCC
28.6055833479
53O-linked_GlycosylationLSQRPGGSTKSHPEP
HHCCCCCCCCCCCCC
38.2855833483
54O-linked_GlycosylationSQRPGGSTKSHPEPQ
HCCCCCCCCCCCCCC
39.5855833487
56O-linked_GlycosylationRPGGSTKSHPEPQTP
CCCCCCCCCCCCCCC
44.3455824035
62O-linked_GlycosylationKSHPEPQTPKDSPSK
CCCCCCCCCCCCCCC
42.9255824039
62PhosphorylationKSHPEPQTPKDSPSK
CCCCCCCCCCCCCCC
42.9226091039
66PhosphorylationEPQTPKDSPSKSSAE
CCCCCCCCCCCCCCC
36.8829255136
68O-linked_GlycosylationQTPKDSPSKSSAEAQ
CCCCCCCCCCCCCCC
49.47OGP
68PhosphorylationQTPKDSPSKSSAEAQ
CCCCCCCCCCCCCCC
49.4729255136
70O-linked_GlycosylationPKDSPSKSSAEAQTP
CCCCCCCCCCCCCCC
38.83OGP
70PhosphorylationPKDSPSKSSAEAQTP
CCCCCCCCCCCCCCC
38.8329255136
71O-linked_GlycosylationKDSPSKSSAEAQTPE
CCCCCCCCCCCCCCC
33.59OGP
71PhosphorylationKDSPSKSSAEAQTPE
CCCCCCCCCCCCCCC
33.5929255136
76O-linked_GlycosylationKSSAEAQTPEDTPNK
CCCCCCCCCCCCCCC
35.38OGP
76PhosphorylationKSSAEAQTPEDTPNK
CCCCCCCCCCCCCCC
35.3829255136
80PhosphorylationEAQTPEDTPNKSGAE
CCCCCCCCCCCCHHH
27.4023927012
82N-linked_GlycosylationQTPEDTPNKSGAEAK
CCCCCCCCCCHHHHH
53.90UniProtKB CARBOHYD
84PhosphorylationPEDTPNKSGAEAKTQ
CCCCCCCCHHHHHHC
50.2922798277
94PhosphorylationEAKTQKDSSNKSGAE
HHHHCCCCCCCCCHH
42.7317287340
95PhosphorylationAKTQKDSSNKSGAEA
HHHCCCCCCCCCHHH
59.4121601212
96N-linked_GlycosylationKTQKDSSNKSGAEAK
HHCCCCCCCCCHHHH
46.60UniProtKB CARBOHYD
98PhosphorylationQKDSSNKSGAEAKTQ
CCCCCCCCCHHHHHC
47.7017287340
114PhosphorylationGSTSKSGSEAQTTKD
CCCCCCCCCCCCCCC
36.53-
118O-linked_GlycosylationKSGSEAQTTKDSTSK
CCCCCCCCCCCCCCC
42.7555829725
118PhosphorylationKSGSEAQTTKDSTSK
CCCCCCCCCCCCCCC
42.75-
119O-linked_GlycosylationSGSEAQTTKDSTSKS
CCCCCCCCCCCCCCC
22.3055829731
119PhosphorylationSGSEAQTTKDSTSKS
CCCCCCCCCCCCCCC
22.30-
122O-linked_GlycosylationEAQTTKDSTSKSHPE
CCCCCCCCCCCCCCC
35.8255829737
123O-linked_GlycosylationAQTTKDSTSKSHPEL
CCCCCCCCCCCCCCC
50.7555829741
123PhosphorylationAQTTKDSTSKSHPEL
CCCCCCCCCCCCCCC
50.7524275569
124O-linked_GlycosylationQTTKDSTSKSHPELQ
CCCCCCCCCCCCCCC
35.7955829745
126O-linked_GlycosylationTKDSTSKSHPELQTP
CCCCCCCCCCCCCCC
44.0055823947
126PhosphorylationTKDSTSKSHPELQTP
CCCCCCCCCCCCCCC
44.00-
132O-linked_GlycosylationKSHPELQTPKDSTGK
CCCCCCCCCCCCCCC
44.9536033481
132PhosphorylationKSHPELQTPKDSTGK
CCCCCCCCCCCCCCC
44.9520068231
136O-linked_GlycosylationELQTPKDSTGKSGAE
CCCCCCCCCCCCCCC
45.2355833185
136PhosphorylationELQTPKDSTGKSGAE
CCCCCCCCCCCCCCC
45.23-
137O-linked_GlycosylationLQTPKDSTGKSGAEA
CCCCCCCCCCCCCCC
59.7855833189
137PhosphorylationLQTPKDSTGKSGAEA
CCCCCCCCCCCCCCC
59.78-
140PhosphorylationPKDSTGKSGAEAQTP
CCCCCCCCCCCCCCC
44.5822798277
146O-linked_GlycosylationKSGAEAQTPEDSPNR
CCCCCCCCCCCCCCC
35.38OGP
146PhosphorylationKSGAEAQTPEDSPNR
CCCCCCCCCCCCCCC
35.3826699800
147 (in isoform 6)Phosphorylation-31.1724275569
150PhosphorylationEAQTPEDSPNRSGAE
CCCCCCCCCCCCHHH
23.5521815630
150 (in isoform 6)Phosphorylation-23.5526699800
152N-linked_GlycosylationQTPEDSPNRSGAEAK
CCCCCCCCCCHHHCC
55.49UniProtKB CARBOHYD
154PhosphorylationPEDSPNRSGAEAKTQ
CCCCCCCCHHHCCCC
49.3328192239
158 (in isoform 6)Phosphorylation-21.4725849741
159 (in isoform 6)Phosphorylation-42.8926699800
160PhosphorylationRSGAEAKTQKDSPSK
CCHHHCCCCCCCCCC
48.1523312004
162 (in isoform 6)Phosphorylation-66.4626699800
164PhosphorylationEAKTQKDSPSKSGSE
HCCCCCCCCCCCCCC
37.8023312004
166PhosphorylationKTQKDSPSKSGSEAQ
CCCCCCCCCCCCCCC
43.3223312004
168PhosphorylationQKDSPSKSGSEAQTT
CCCCCCCCCCCCCCC
52.4623312004
170PhosphorylationDSPSKSGSEAQTTKD
CCCCCCCCCCCCCCC
36.5324505115
174O-linked_GlycosylationKSGSEAQTTKDVPNK
CCCCCCCCCCCCCCC
42.75OGP
175O-linked_GlycosylationSGSEAQTTKDVPNKS
CCCCCCCCCCCCCCC
17.11OGP
180N-linked_GlycosylationQTTKDVPNKSGADGQ
CCCCCCCCCCCCCCC
51.48UniProtKB CARBOHYD
182O-linked_GlycosylationTKDVPNKSGADGQTP
CCCCCCCCCCCCCCC
45.94OGP
188O-linked_GlycosylationKSGADGQTPKDGSSK
CCCCCCCCCCCCCCC
37.52OGP
194O-linked_GlycosylationQTPKDGSSKSGAEDQ
CCCCCCCCCCCCCCC
36.05OGP
196PhosphorylationPKDGSSKSGAEDQTP
CCCCCCCCCCCCCCC
45.2228102081
202O-linked_GlycosylationKSGAEDQTPKDVPNK
CCCCCCCCCCCCCCC
44.6355829345
202PhosphorylationKSGAEDQTPKDVPNK
CCCCCCCCCCCCCCC
44.6328102081
208N-linked_GlycosylationQTPKDVPNKSGAEKQ
CCCCCCCCCCCCCCC
51.48UniProtKB CARBOHYD
210PhosphorylationPKDVPNKSGAEKQTP
CCCCCCCCCCCCCCC
50.2928857561
221PhosphorylationKQTPKDGSNKSGAEE
CCCCCCCCCCCCCHH
51.7429255136
222N-linked_GlycosylationQTPKDGSNKSGAEEQ
CCCCCCCCCCCCHHC
48.30UniProtKB CARBOHYD
224O-linked_GlycosylationPKDGSNKSGAEEQGP
CCCCCCCCCCHHCCC
47.70OGP
224PhosphorylationPKDGSNKSGAEEQGP
CCCCCCCCCCHHCCC
47.7029255136
236O-linked_GlycosylationQGPIDGPSKSGAEEQ
CCCCCCCCCCCCCCC
45.0155832785
236PhosphorylationQGPIDGPSKSGAEEQ
CCCCCCCCCCCCCCC
45.0128355574
238O-linked_GlycosylationPIDGPSKSGAEEQTS
CCCCCCCCCCCCCCC
47.80OGP
238PhosphorylationPIDGPSKSGAEEQTS
CCCCCCCCCCCCCCC
47.8022798277
244PhosphorylationKSGAEEQTSKDSPNK
CCCCCCCCCCCCCCC
40.8124719451
245O-linked_GlycosylationSGAEEQTSKDSPNKV
CCCCCCCCCCCCCCC
33.8768999563
245PhosphorylationSGAEEQTSKDSPNKV
CCCCCCCCCCCCCCC
33.8722798277
245 (in isoform 4)Phosphorylation-33.8724275569
248 (in isoform 4)Phosphorylation-33.8226699800
256 (in isoform 4)Phosphorylation-34.8925849741
257 (in isoform 4)Phosphorylation-34.1426699800
260 (in isoform 4)Phosphorylation-65.2226699800
263O-linked_GlycosylationQPSRKDHSKPISNPS
CCCCCCCCCCCCCCC
50.7068999757
263PhosphorylationQPSRKDHSKPISNPS
CCCCCCCCCCCCCCC
50.7024275569
267O-linked_GlycosylationKDHSKPISNPSDNKE
CCCCCCCCCCCCCCC
51.7455832319
267PhosphorylationKDHSKPISNPSDNKE
CCCCCCCCCCCCCCC
51.74-
270O-linked_GlycosylationSKPISNPSDNKELPK
CCCCCCCCCCCCCCC
59.0555832325
270PhosphorylationSKPISNPSDNKELPK
CCCCCCCCCCCCCCC
59.05-
272 (in isoform 6)Phosphorylation-44.0028152594
274 (in isoform 6)Phosphorylation-76.2628152594
290O-linked_GlycosylationLADKGKLSPHAFKTE
HHHHCCCCCCCEECC
20.37101661085
290PhosphorylationLADKGKLSPHAFKTE
HHHHCCCCCCCEECC
20.3723927012
296O-linked_GlycosylationLSPHAFKTESGEETD
CCCCCEECCCCCCCC
29.00OGP
296PhosphorylationLSPHAFKTESGEETD
CCCCCEECCCCCCCC
29.0029255136
298PhosphorylationPHAFKTESGEETDLI
CCCEECCCCCCCCCC
57.6529255136
302PhosphorylationKTESGEETDLISPPQ
ECCCCCCCCCCCCCH
31.6323927012
306PhosphorylationGEETDLISPPQEEVK
CCCCCCCCCCHHHHC
37.5123927012
314PhosphorylationPPQEEVKSSEPTEDV
CCHHHHCCCCCCCCC
45.1425849741
315O-linked_GlycosylationPQEEVKSSEPTEDVE
CHHHHCCCCCCCCCC
41.71OGP
315PhosphorylationPQEEVKSSEPTEDVE
CHHHHCCCCCCCCCC
41.7125849741
318O-linked_GlycosylationEVKSSEPTEDVEPKE
HHCCCCCCCCCCCCC
40.5455832013
318PhosphorylationEVKSSEPTEDVEPKE
HHCCCCCCCCCCCCC
40.5429507054
331PhosphorylationKEAEDDDTGPEEGSP
CCCCCCCCCCCCCCC
62.72-
347PhosphorylationKEEKEKMSGSASSEN
HHHHHHHCCCCCCCC
40.4422617229
349PhosphorylationEKEKMSGSASSENRE
HHHHHCCCCCCCCCC
20.0525159151
351PhosphorylationEKMSGSASSENREGT
HHHCCCCCCCCCCCC
39.6228355574
352PhosphorylationKMSGSASSENREGTL
HHCCCCCCCCCCCCC
38.3130278072
358PhosphorylationSSENREGTLSDSTGS
CCCCCCCCCCCCCCC
20.5220639409
359UbiquitinationSENREGTLSDSTGSE
CCCCCCCCCCCCCCC
8.6633845483
360PhosphorylationENREGTLSDSTGSEK
CCCCCCCCCCCCCCC
29.3830576142
362PhosphorylationREGTLSDSTGSEKDD
CCCCCCCCCCCCCCC
31.1520639409
363PhosphorylationEGTLSDSTGSEKDDL
CCCCCCCCCCCCCCC
50.1220639409
365PhosphorylationTLSDSTGSEKDDLYP
CCCCCCCCCCCCCCC
41.3720639409
368UbiquitinationDSTGSEKDDLYPNGS
CCCCCCCCCCCCCCC
47.2829967540
370 (in isoform 4)Phosphorylation-12.5828152594
372 (in isoform 4)Phosphorylation-46.1028152594
373N-linked_GlycosylationEKDDLYPNGSGNGSA
CCCCCCCCCCCCCCH
43.64UniProtKB CARBOHYD
377N-linked_GlycosylationLYPNGSGNGSAESSH
CCCCCCCCCCHHHHH
42.83UniProtKB CARBOHYD
417UbiquitinationIAFVLEGKRSKVTRR
EEEEECCCCCCCCCC
44.0933845483
419PhosphorylationFVLEGKRSKVTRRPK
EEECCCCCCCCCCCC
34.6629514088
426UbiquitinationSKVTRRPKASDYQRL
CCCCCCCCHHHHHHC
59.7329967540
428PhosphorylationVTRRPKASDYQRLDQ
CCCCCCHHHHHHCCC
42.8728152594
428 (in isoform 2)Phosphorylation-42.8728152594
430PhosphorylationRRPKASDYQRLDQKY
CCCCHHHHHHCCCEE
7.9528152594
430 (in isoform 2)Phosphorylation-7.9528152594

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
71SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
221SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
298SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
302TPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
351SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TGON2_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 TGON2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITB1_HUMANITGB1physical
11208159
AP1M1_HUMANAP1M1physical
10814565
AP2M1_HUMANAP2M1physical
10814565
AP3M1_HUMANAP3M1physical
10814565
KR109_HUMANKRTAP10-9physical
25416956
MDN1_HUMANMDN1physical
26186194
DPOE1_HUMANPOLEphysical
26186194
AT1A3_HUMANATP1A3physical
26186194
NU188_HUMANNUP188physical
26186194
HEAT1_HUMANHEATR1physical
26186194
GPD1L_HUMANGPD1Lphysical
26186194
INT12_HUMANINTS12physical
26186194
SYLM_HUMANLARS2physical
26186194
IPO13_HUMANIPO13physical
26186194
INT4_HUMANINTS4physical
26186194
RUS1_HUMANC16orf58physical
26186194
GOPC_HUMANGOPCphysical
26186194
NUP85_HUMANNUP85physical
26186194
LTN1_HUMANLTN1physical
26186194
PDS5B_HUMANPDS5Bphysical
26186194
CHD1L_HUMANCHD1Lphysical
26186194
XPR1_HUMANXPR1physical
26186194
GALT2_HUMANGALNT2physical
26186194
AP1M1_HUMANAP1M1physical
26186194
INT1_HUMANINTS1physical
26186194
HS2ST_HUMANHS2ST1physical
26186194
INT2_HUMANINTS2physical
26186194
ITIH3_HUMANITIH3physical
26186194
ALG2_HUMANALG2physical
26186194
GNL3L_HUMANGNL3Lphysical
26186194
ARF6_HUMANARF6physical
26186194
HS12A_HUMANHSPA12Aphysical
26186194
RHBD3_HUMANRHBDD3physical
26186194
ARF5_HUMANARF5physical
26186194
UGDH_HUMANUGDHphysical
26186194
INT5_HUMANINTS5physical
26186194
RAB18_HUMANRAB18physical
26186194
NF1_HUMANNF1physical
26186194
LCHN_HUMANKIAA1147physical
26186194
RAB14_HUMANRAB14physical
26186194
RRAGB_HUMANRRAGBphysical
26186194
RUFY1_HUMANRUFY1physical
26186194
RAB3A_HUMANRAB3Aphysical
26186194
RAB3B_HUMANRAB3Bphysical
26186194
RAB13_HUMANRAB13physical
26186194
RA51C_HUMANRAD51Cphysical
26186194
TBL3_HUMANTBL3physical
26186194
ALG2_HUMANALG2physical
28514442
ARF6_HUMANARF6physical
28514442
GOPC_HUMANGOPCphysical
28514442
INT4_HUMANINTS4physical
28514442
IPO13_HUMANIPO13physical
28514442
GPD1L_HUMANGPD1Lphysical
28514442
RRAGB_HUMANRRAGBphysical
28514442
RUFY1_HUMANRUFY1physical
28514442
INT1_HUMANINTS1physical
28514442
RHBD3_HUMANRHBDD3physical
28514442
LTN1_HUMANLTN1physical
28514442
GALT2_HUMANGALNT2physical
28514442
RAB3B_HUMANRAB3Bphysical
28514442
RAB3A_HUMANRAB3Aphysical
28514442
INT5_HUMANINTS5physical
28514442
AP1M1_HUMANAP1M1physical
28514442
HS12A_HUMANHSPA12Aphysical
28514442
XPR1_HUMANXPR1physical
28514442
MDN1_HUMANMDN1physical
28514442
GPN3_HUMANGPN3physical
28514442
SYLM_HUMANLARS2physical
28514442
LCHN_HUMANKIAA1147physical
28514442

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 TGON2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70, AND MASSSPECTROMETRY.
"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-71, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-98, AND MASSSPECTROMETRY.

TOP