ATLA2_HUMAN - dbPTM
ATLA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATLA2_HUMAN
UniProt AC Q8NHH9
Protein Name Atlastin-2
Gene Name ATL2
Organism Homo sapiens (Human).
Sequence Length 583
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Localizes at endoplasmic reticulum (ER) three-way tubular junctions (PubMed:27619977).
Protein Description GTPase tethering membranes through formation of trans-homooligomers and mediating homotypic fusion of endoplasmic reticulum membranes. Functions in endoplasmic reticulum tubular network biogenesis. [PubMed: 18270207]
Protein Sequence MAEGDEAARGQQPHQGLWRRRRTSDPSAAVNHVSSTTSLGENYEDDDLVNSDEVMKKPCPVQIVLAHEDDHNFELDEEALEQILLQEHIRDLNIVVVSVAGAFRKGKSFLLDFMLRYMYNKDSQSWIGGNNEPLTGFTWRGGCERETTGIQVWNEVFVIDRPNGTKVAVLLMDTQGAFDSQSTIKDCATVFALSTMTSSVQVYNLSQNIQEDDLQHLQLFTEYGRLAMEEIYQKPFQTLMFLIRDWSYPYEHSYGLEGGKQFLEKRLQVKQNQHEELQNVRKHIHNCFSNLGCFLLPHPGLKVATNPSFDGRLKDIDEDFKRELRNLVPLLLAPENLVEKEISGSKVTCRDLVEYFKAYIKIYQGEELPHPKSMLQATAEANNLAAVAGARDTYCKSMEQVCGGDKPYIAPSDLERKHLDLKEVAIKQFRSVKKMGGDEFCRRYQDQLEAEIEETYANFIKHNDGKNIFYAARTPATLFAVMFAMYIISGLTGFIGLNSIAVLCNLVMGLALIFLCTWAYVKYSGEFREIGTVIDQIAETLWEQVLKPLGDNLMEENIRQSVTNSIKAGLTDQVSHHARLKTD
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
9MethylationAEGDEAARGQQPHQG
CCCCHHHCCCCCCCC		50.96-
23PhosphorylationGLWRRRRTSDPSAAV
CHHHCCCCCCCCHHH		35.3529255136
23 (in isoform 2)Phosphorylation-35.3524719451
24 (in isoform 2)Phosphorylation-45.79-
24PhosphorylationLWRRRRTSDPSAAVN
HHHCCCCCCCCHHHH		45.7929255136
27 (in isoform 2)Phosphorylation-33.57-
27PhosphorylationRRRTSDPSAAVNHVS
CCCCCCCCHHHHHHH		33.5729255136
34 (in isoform 2)Phosphorylation-17.89-
34PhosphorylationSAAVNHVSSTTSLGE
CHHHHHHHCCCCCCC		17.8930278072
35PhosphorylationAAVNHVSSTTSLGEN
HHHHHHHCCCCCCCC		34.3230278072
36PhosphorylationAVNHVSSTTSLGENY
HHHHHHCCCCCCCCC		16.9423927012
37PhosphorylationVNHVSSTTSLGENYE
HHHHHCCCCCCCCCC		24.7323927012
38 (in isoform 2)Phosphorylation-34.17-
38PhosphorylationNHVSSTTSLGENYED
HHHHCCCCCCCCCCC		34.1723927012
43PhosphorylationTTSLGENYEDDDLVN
CCCCCCCCCCCCCCC		19.2123927012
43 (in isoform 2)Phosphorylation-19.21-
51 (in isoform 2)Phosphorylation-27.89-
51PhosphorylationEDDDLVNSDEVMKKP
CCCCCCCCHHHHCCC		27.8923927012
99 (in isoform 3)Ubiquitination-3.7321890473
103UbiquitinationVVSVAGAFRKGKSFL
EEEECHHHHCCHHHH		8.96-
117PhosphorylationLLDFMLRYMYNKDSQ
HHHHHHHHHHCCCCC		10.45-
119PhosphorylationDFMLRYMYNKDSQSW
HHHHHHHHCCCCCCC		15.32-
121 (in isoform 2)Ubiquitination-41.07-
143 (in isoform 3)Ubiquitination-5.0521890473
150 (in isoform 3)Ubiquitination-2.5421890473
190 (in isoform 3)Ubiquitination-1.0921890473
201 (in isoform 3)Ubiquitination-33.6521890473
251 (in isoform 3)Ubiquitination-23.1221890473
265UbiquitinationGGKQFLEKRLQVKQN
HHHHHHHHHHHHCCH		61.63-
270UbiquitinationLEKRLQVKQNQHEEL
HHHHHHHCCHHHHHH		30.4821906983
270MethylationLEKRLQVKQNQHEEL
HHHHHHHCCHHHHHH		30.4824129315
270 (in isoform 1)Ubiquitination-30.4821890473
270 (in isoform 2)Ubiquitination-30.4821890473
290 (in isoform 3)Ubiquitination-21.8721890473
296UbiquitinationSNLGCFLLPHPGLKV
HCCCCEECCCCCCEE		1.5119608861
296AcetylationSNLGCFLLPHPGLKV
HCCCCEECCCCCCEE		1.5119608861
302UbiquitinationLLPHPGLKVATNPSF
ECCCCCCEECCCCCC		35.42-
303AcetylationLPHPGLKVATNPSFD
CCCCCCEECCCCCCC		10.7719608861
303UbiquitinationLPHPGLKVATNPSFD
CCCCCCEECCCCCCC		10.7719608861
308PhosphorylationLKVATNPSFDGRLKD
CEECCCCCCCCCCCC		37.7324719451
308 (in isoform 2)Phosphorylation-37.7324719451
308O-linked_GlycosylationLKVATNPSFDGRLKD
CEECCCCCCCCCCCC		37.7328510447
314UbiquitinationPSFDGRLKDIDEDFK
CCCCCCCCCCCHHHH		51.8019608861
314 (in isoform 1)Ubiquitination-51.8021890473
314AcetylationPSFDGRLKDIDEDFK
CCCCCCCCCCCHHHH		51.8019608861
314 (in isoform 2)Ubiquitination-51.8021890473
314 (in isoform 2)Acetylation-51.80-
321 (in isoform 2)Ubiquitination-58.2321890473
321UbiquitinationKDIDEDFKRELRNLV
CCCCHHHHHHHHHHH		58.2319608861
321 (in isoform 1)Ubiquitination-58.2321890473
321AcetylationKDIDEDFKRELRNLV
CCCCHHHHHHHHHHH		58.2319608861
321 (in isoform 2)Acetylation-58.23-
340UbiquitinationAPENLVEKEISGSKV
CCHHHCCCCCCCCCC		53.52-
343UbiquitinationNLVEKEISGSKVTCR
HHCCCCCCCCCCCHH		37.8021890473
346UbiquitinationEKEISGSKVTCRDLV
CCCCCCCCCCHHHHH		45.12-
361 (in isoform 2)Ubiquitination-23.7621890473
361UbiquitinationEYFKAYIKIYQGEEL
HHHHHHHHHHCCCCC		23.7621890473
361 (in isoform 1)Ubiquitination-23.7621890473
361UbiquitinationEYFKAYIKIYQGEEL
HHHHHHHHHHCCCCC		23.7621890473
372 (in isoform 1)Ubiquitination-45.5221890473
372UbiquitinationGEELPHPKSMLQATA
CCCCCCCHHHHHHHH		45.5221906983
372 (in isoform 2)Ubiquitination-45.5221890473
378PhosphorylationPKSMLQATAEANNLA
CHHHHHHHHHHHHHH		16.4520068231
396UbiquitinationGARDTYCKSMEQVCG
CCHHHHHHHHHHHHC		42.28-
396 (in isoform 3)Ubiquitination-42.2821890473
406AcetylationEQVCGGDKPYIAPSD
HHHHCCCCCCCCCHH		42.8926051181
408PhosphorylationVCGGDKPYIAPSDLE
HHCCCCCCCCCHHHH		18.5627642862
422 (in isoform 1)Ubiquitination-50.2221890473
422 (in isoform 2)Ubiquitination-50.2221890473
422UbiquitinationERKHLDLKEVAIKQF
HHCCCCHHHHHHHHH		50.2221906983
427UbiquitinationDLKEVAIKQFRSVKK
CHHHHHHHHHHHHHH		33.38-
456PhosphorylationEAEIEETYANFIKHN
HHHHHHHHHHHHHHC		11.65-
461 (in isoform 2)Ubiquitination-32.0221890473
461UbiquitinationETYANFIKHNDGKNI
HHHHHHHHHCCCCCE		32.0221906983
461 (in isoform 1)Ubiquitination-32.0221890473
549UbiquitinationWEQVLKPLGDNLMEE
HHHHHHHHCCCHHHH		14.9221890473
550 (in isoform 4)Phosphorylation-30.2229900121
551 (in isoform 4)Phosphorylation-53.4228102081
563 (in isoform 2)Phosphorylation-28.6129900121
564 (in isoform 2)Phosphorylation-39.3128102081
565PhosphorylationIRQSVTNSIKAGLTD
HHHHHHHHHHHCCCC		18.9928348404
567 (in isoform 1)Ubiquitination-35.9021890473
567UbiquitinationQSVTNSIKAGLTDQV
HHHHHHHHHCCCCHH		35.9021890473
571PhosphorylationNSIKAGLTDQVSHHA
HHHHHCCCCHHHHHH		24.3828555341
575PhosphorylationAGLTDQVSHHARLKT
HCCCCHHHHHHCCCC		12.1522496350
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 ATLA2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATLA2_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 ATLA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ADDA_HUMANADD1physical
26496610
KC1G2_HUMANCSNK1G2physical
26496610
SMCA4_HUMANSMARCA4physical
26496610
NELFA_HUMANNELFAphysical
26496610
BCL7B_HUMANBCL7Bphysical
26496610
RPP38_HUMANRPP38physical
26496610
SNR27_HUMANSNRNP27physical
26496610
F120A_HUMANFAM120Aphysical
26496610
NNTM_HUMANNNTphysical
26496610
KLDC2_HUMANKLHDC2physical
26496610
ATLA3_HUMANATL3physical
26496610
STK39_HUMANSTK39physical
26496610
DEN1A_HUMANDENND1Aphysical
26496610
ACRBP_HUMANACRBPphysical
26496610
LSM11_HUMANLSM11physical
26496610
LAMA1_HUMANLAMA1physical
26496610
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 ATLA2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-314 AND LYS-321, AND MASSSPECTROMETRY.
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-24, 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-24, AND MASSSPECTROMETRY.

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