TXLNG_HUMAN - dbPTM
TXLNG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TXLNG_HUMAN
UniProt AC Q9NUQ3
Protein Name Gamma-taxilin
Gene Name TXLNG
Organism Homo sapiens (Human).
Sequence Length 528
Subcellular Localization Nucleus membrane . Cytoplasm, cytosol .
Protein Description May be involved in intracellular vesicle traffic. Inhibits ATF4-mediated transcription, possibly by dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May be involved in regulating bone mass density through an ATF4-dependent pathway. May be involved in cell cycle progression..
Protein Sequence MATRVEEAARGRGGGAEEATEAGRGGRRRSPRQKFEIGTMEEAGICGLGVKADMLCNSQSNDILQHQGSNCGGTSNKHSLEEDEGSDFITENRNLVSPAYCTQESREEIPGGEARTDPPDGQQDSECNRNKEKTLGKEVLLLMQALNTLSTPEEKLAALCKKYADLLEESRSVQKQMKILQKKQAQIVKEKVHLQSEHSKAILARSKLESLCRELQRHNKTLKEENMQQAREEEERRKEATAHFQITLNEIQAQLEQHDIHNAKLRQENIELGEKLKKLIEQYALREEHIDKVFKHKELQQQLVDAKLQQTTQLIKEADEKHQREREFLLKEATESRHKYEQMKQQEVQLKQQLSLYMDKFEEFQTTMAKSNELFTTFRQEMEKMTKKIKKLEKETIIWRTKWENNNKALLQMAEEKTVRDKEYKALQIKLERLEKLCRALQTERNELNEKVEVLKEQVSIKAAIKAANRDLATPVMQPCTALDSHKELNTSSKRALGAHLEAEPKSQRSAVQKPPSTGSAPAIESVD
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
10MethylationTRVEEAARGRGGGAE
CHHHHHHCCCCCCHH
42.25115368707
12MethylationVEEAARGRGGGAEEA
HHHHHCCCCCCHHHH
34.7224129315
24MethylationEEATEAGRGGRRRSP
HHHHHCCCCCCCCCH
51.9824129315
27MethylationTEAGRGGRRRSPRQK
HHCCCCCCCCCHHHC
33.3930989833
30PhosphorylationGRGGRRRSPRQKFEI
CCCCCCCCHHHCEEC
23.7122817900
43UbiquitinationEIGTMEEAGICGLGV
ECCCHHHHCCCCCCC
10.1932015554
54SulfoxidationGLGVKADMLCNSQSN
CCCCCHHHHCCCCCC
5.7021406390
58PhosphorylationKADMLCNSQSNDILQ
CHHHHCCCCCCCHHH
33.7123663014
60PhosphorylationDMLCNSQSNDILQHQ
HHHCCCCCCCHHHHC
35.9723663014
69PhosphorylationDILQHQGSNCGGTSN
CHHHHCCCCCCCCCC
23.5229978859
70UbiquitinationILQHQGSNCGGTSNK
HHHHCCCCCCCCCCC
34.9621890473
72UbiquitinationQHQGSNCGGTSNKHS
HHCCCCCCCCCCCCC
46.8122817900
73UbiquitinationHQGSNCGGTSNKHSL
HCCCCCCCCCCCCCC
28.3322817900
74PhosphorylationQGSNCGGTSNKHSLE
CCCCCCCCCCCCCCC
17.8926714015
75UbiquitinationGSNCGGTSNKHSLEE
CCCCCCCCCCCCCCC
47.3532015554
75PhosphorylationGSNCGGTSNKHSLEE
CCCCCCCCCCCCCCC
47.3527251275
79PhosphorylationGGTSNKHSLEEDEGS
CCCCCCCCCCCCCCC
38.8030576142
86PhosphorylationSLEEDEGSDFITENR
CCCCCCCCCCCCCCC
27.5725159151
88UbiquitinationEEDEGSDFITENRNL
CCCCCCCCCCCCCCC
8.7924816145
90PhosphorylationDEGSDFITENRNLVS
CCCCCCCCCCCCCCC
27.4829978859
97PhosphorylationTENRNLVSPAYCTQE
CCCCCCCCCCCCCHH
13.6419664994
100PhosphorylationRNLVSPAYCTQESRE
CCCCCCCCCCHHHHC
10.2223927012
102PhosphorylationLVSPAYCTQESREEI
CCCCCCCCHHHHCCC
23.7722167270
105PhosphorylationPAYCTQESREEIPGG
CCCCCHHHHCCCCCC
34.8623927012
116PhosphorylationIPGGEARTDPPDGQQ
CCCCCCCCCCCCCCC
60.9626074081
126UbiquitinationPDGQQDSECNRNKEK
CCCCCCCCCCHHHCH
44.0624816145
134PhosphorylationCNRNKEKTLGKEVLL
CCHHHCHHHHHHHHH
41.66-
143UbiquitinationGKEVLLLMQALNTLS
HHHHHHHHHHHHCCC
1.9033845483
143UbiquitinationGKEVLLLMQALNTLS
HHHHHHHHHHHHCCC
1.9021890473
143NeddylationGKEVLLLMQALNTLS
HHHHHHHHHHHHCCC
1.9032015554
145UbiquitinationEVLLLMQALNTLSTP
HHHHHHHHHHCCCCH
6.7122817900
146UbiquitinationVLLLMQALNTLSTPE
HHHHHHHHHCCCCHH
2.5722817900
161UbiquitinationEKLAALCKKYADLLE
HHHHHHHHHHHHHHH
50.0632015554
162AcetylationKLAALCKKYADLLEE
HHHHHHHHHHHHHHH
44.6826051181
163PhosphorylationLAALCKKYADLLEES
HHHHHHHHHHHHHHH
7.2820068231
170PhosphorylationYADLLEESRSVQKQM
HHHHHHHHHHHHHHH
22.0820068231
172PhosphorylationDLLEESRSVQKQMKI
HHHHHHHHHHHHHHH
37.8728509920
175UbiquitinationEESRSVQKQMKILQK
HHHHHHHHHHHHHHH
50.6429967540
199UbiquitinationVHLQSEHSKAILARS
HHCCCHHHHHHHHHH
21.5224816145
207UbiquitinationKAILARSKLESLCRE
HHHHHHHHHHHHHHH
51.2032015554
210PhosphorylationLARSKLESLCRELQR
HHHHHHHHHHHHHHH
43.1124719451
220UbiquitinationRELQRHNKTLKEENM
HHHHHHHHHHHHHHH
49.4624816145
223AcetylationQRHNKTLKEENMQQA
HHHHHHHHHHHHHHH
69.1126051181
238UbiquitinationREEEERRKEATAHFQ
HHHHHHHHHHHHHHH
58.9032015554
275NeddylationENIELGEKLKKLIEQ
HHHHHHHHHHHHHHH
64.9032015554
275UbiquitinationENIELGEKLKKLIEQ
HHHHHHHHHHHHHHH
64.9022817900
277UbiquitinationIELGEKLKKLIEQYA
HHHHHHHHHHHHHHH
57.5122817900
278UbiquitinationELGEKLKKLIEQYAL
HHHHHHHHHHHHHHH
66.2022817900
283PhosphorylationLKKLIEQYALREEHI
HHHHHHHHHHHHHHH
8.5320068231
292AcetylationLREEHIDKVFKHKEL
HHHHHHHHHHCCHHH
49.3026051181
292UbiquitinationLREEHIDKVFKHKEL
HHHHHHHHHHCCHHH
49.30-
301UbiquitinationFKHKELQQQLVDAKL
HCCHHHHHHHHHHHH
51.7224816145
307UbiquitinationQQQLVDAKLQQTTQL
HHHHHHHHHHHHHHH
42.2229967540
309UbiquitinationQLVDAKLQQTTQLIK
HHHHHHHHHHHHHHH
37.5624816145
319UbiquitinationTQLIKEADEKHQRER
HHHHHHHHHHHHHHH
67.5729967540
331UbiquitinationREREFLLKEATESRH
HHHHHHHHHHHHHHH
47.6624816145
370UbiquitinationEFQTTMAKSNELFTT
HHHHHHHHHCHHHHH
42.8832015554
371PhosphorylationFQTTMAKSNELFTTF
HHHHHHHHCHHHHHH
26.4620068231
374UbiquitinationTMAKSNELFTTFRQE
HHHHHCHHHHHHHHH
5.5924816145
376PhosphorylationAKSNELFTTFRQEME
HHHCHHHHHHHHHHH
37.3320068231
377PhosphorylationKSNELFTTFRQEMEK
HHCHHHHHHHHHHHH
14.9720068231
382UbiquitinationFTTFRQEMEKMTKKI
HHHHHHHHHHHHHHH
4.5524816145
386PhosphorylationRQEMEKMTKKIKKLE
HHHHHHHHHHHHHHH
40.0117081983
388AcetylationEMEKMTKKIKKLEKE
HHHHHHHHHHHHHHH
51.0612436935
402AcetylationETIIWRTKWENNNKA
HHHHEEECCCCCHHH
43.8925953088
430AcetylationEYKALQIKLERLEKL
HHHHHHHHHHHHHHH
31.1926051181
451UbiquitinationERNELNEKVEVLKEQ
HHHHHHHHHHHHHHH
42.4929967540
460PhosphorylationEVLKEQVSIKAAIKA
HHHHHHHHHHHHHHH
20.3321406692
474PhosphorylationAANRDLATPVMQPCT
HHCCCCCCCCCCCCC
24.5826462736
481PhosphorylationTPVMQPCTALDSHKE
CCCCCCCCHHHHHCC
36.62-
487AcetylationCTALDSHKELNTSSK
CCHHHHHCCCCCHHH
68.7826051181
491PhosphorylationDSHKELNTSSKRALG
HHHCCCCCHHHHHHH
47.1829214152
506UbiquitinationAHLEAEPKSQRSAVQ
HHHCCCCHHHHHCCC
51.2124816145
510PhosphorylationAEPKSQRSAVQKPPS
CCCHHHHHCCCCCCC
25.7529396449
514UbiquitinationSQRSAVQKPPSTGSA
HHHHCCCCCCCCCCC
52.9024816145
514AcetylationSQRSAVQKPPSTGSA
HHHHCCCCCCCCCCC
52.9030593163
517PhosphorylationSAVQKPPSTGSAPAI
HCCCCCCCCCCCCCC
54.6625159151
518PhosphorylationAVQKPPSTGSAPAIE
CCCCCCCCCCCCCCC
40.7125159151
520PhosphorylationQKPPSTGSAPAIESV
CCCCCCCCCCCCCCC
31.0325159151
526PhosphorylationGSAPAIESVD-----
CCCCCCCCCC-----
26.0230108239

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 TXLNG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TXLNG_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 TXLNG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBK1_HUMANTBK1physical
21903422
TXLNA_HUMANTXLNAphysical
21903422
TXLNB_HUMANTXLNBphysical
21903422
WIPF2_HUMANWIPF2physical
22939629
UBP3_HUMANUSP3physical
22939629
CHAP1_HUMANCHAMP1physical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
UBA1_HUMANUBA1physical
22939629
CDV3_HUMANCDV3physical
26344197
DDX17_HUMANDDX17physical
26344197
TXLNA_HUMANTXLNAphysical
27173435

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 TXLNG_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, AND MASSSPECTROMETRY.
"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-97 AND SER-517, 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-97 AND SER-105, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97, 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 THR-386, AND MASSSPECTROMETRY.

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