ATLA3_HUMAN - dbPTM
ATLA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATLA3_HUMAN
UniProt AC Q6DD88
Protein Name Atlastin-3
Gene Name ATL3
Organism Homo sapiens (Human).
Sequence Length 541
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein . Localizes to endoplasmic reticulum tubules and accumulates in punctuate structures corresponding to 3-way junctions, which represent crossing-points at which the tubules build a polygonal
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 MLSPQRVAAAASRGADDAMESSKPGPVQVVLVQKDQHSFELDEKALASILLQDHIRDLDVVVVSVAGAFRKGKSFILDFMLRYLYSQKESGHSNWLGDPEEPLTGFSWRGGSDPETTGIQIWSEVFTVEKPGGKKVAVVLMDTQGAFDSQSTVKDCATIFALSTMTSSVQIYNLSQNIQEDDLQQLQLFTEYGRLAMDEIFQKPFQTLMFLVRDWSFPYEYSYGLQGGMAFLDKRLQVKEHQHEEIQNVRNHIHSCFSDVTCFLLPHPGLQVATSPDFDGKLKDIAGEFKEQLQALIPYVLNPSKLMEKEINGSKVTCRGLLEYFKAYIKIYQGEDLPHPKSMLQATAEANNLAAAASAKDIYYNNMEEVCGGEKPYLSPDILEEKHCEFKQLALDHFKKTKKMGGKDFSFRYQQELEEEIKELYENFCKHNGSKNVFSTFRTPAVLFTGIVALYIASGLTGFIGLEVVAQLFNCMVGLLLIALLTWGYIRYSGQYRELGGAIDFGAAYVLEQASSHIGNSTQATVRDAVVGRPSMDKKAQ
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-----MLSPQRVAAA
-----CCCHHHHHHH		20.0725159151
12PhosphorylationQRVAAAASRGADDAM
HHHHHHHHCCHHHHH		26.9022199227
19SulfoxidationSRGADDAMESSKPGP
HCCHHHHHHHCCCCC		7.0721406390
21PhosphorylationGADDAMESSKPGPVQ
CHHHHHHHCCCCCEE		30.4918491316
22PhosphorylationADDAMESSKPGPVQV
HHHHHHHCCCCCEEE		29.5718491316
23 (in isoform 1)Ubiquitination-64.3721890473
23UbiquitinationDDAMESSKPGPVQVV
HHHHHHCCCCCEEEE		64.3721906983
342-HydroxyisobutyrylationVQVVLVQKDQHSFEL
EEEEEEECCCCCEEC		52.45-
38PhosphorylationLVQKDQHSFELDEKA
EEECCCCCEECCHHH		18.1225159151
85PhosphorylationDFMLRYLYSQKESGH
HHHHHHHHHCCCCCC		10.50-
93PhosphorylationSQKESGHSNWLGDPE
HCCCCCCCCCCCCCC		32.97-
130UbiquitinationSEVFTVEKPGGKKVA
EEEEEEECCCCCEEE		44.63-
239 (in isoform 1)Ubiquitination-36.2021890473
239MalonylationLDKRLQVKEHQHEEI
HHHCCCCCHHCHHHH		36.2026320211
239MethylationLDKRLQVKEHQHEEI
HHHCCCCCHHCHHHH		36.20-
2392-HydroxyisobutyrylationLDKRLQVKEHQHEEI
HHHCCCCCHHCHHHH		36.20-
239UbiquitinationLDKRLQVKEHQHEEI
HHHCCCCCHHCHHHH		36.2021906983
261PhosphorylationHSCFSDVTCFLLPHP
HHHHCCCCEEECCCC		11.52-
2832-HydroxyisobutyrylationPDFDGKLKDIAGEFK
CCCCCCHHHHHHHHH		51.04-
283 (in isoform 1)Ubiquitination-51.0421890473
283MalonylationPDFDGKLKDIAGEFK
CCCCCCHHHHHHHHH		51.0432601280
283UbiquitinationPDFDGKLKDIAGEFK
CCCCCCHHHHHHHHH		51.0421906983
3092-HydroxyisobutyrylationNPSKLMEKEINGSKV
CHHHHCHHHHCCCCC		50.34-
309UbiquitinationNPSKLMEKEINGSKV
CHHHHCHHHHCCCCC		50.34-
315UbiquitinationEKEINGSKVTCRGLL
HHHHCCCCCCHHHHH		42.85-
317PhosphorylationEINGSKVTCRGLLEY
HHCCCCCCHHHHHHH		10.5428270605
324PhosphorylationTCRGLLEYFKAYIKI
CHHHHHHHHHHHHHH		15.4528270605
326UbiquitinationRGLLEYFKAYIKIYQ
HHHHHHHHHHHHHHC		39.10-
328PhosphorylationLLEYFKAYIKIYQGE
HHHHHHHHHHHHCCC		11.8828270605
330UbiquitinationEYFKAYIKIYQGEDL
HHHHHHHHHHCCCCC		23.76-
341UbiquitinationGEDLPHPKSMLQATA
CCCCCCCHHHHHHHH		45.5221906983
341 (in isoform 1)Ubiquitination-45.5221890473
342PhosphorylationEDLPHPKSMLQATAE
CCCCCCHHHHHHHHH		29.2220068231
343SulfoxidationDLPHPKSMLQATAEA
CCCCCHHHHHHHHHH		3.9221406390
347PhosphorylationPKSMLQATAEANNLA
CHHHHHHHHHHHHHH		16.4520068231
358PhosphorylationNNLAAAASAKDIYYN
HHHHHHHHHHHHHHC		30.9930622161
360UbiquitinationLAAAASAKDIYYNNM
HHHHHHHHHHHHCCH		42.01-
375AcetylationEEVCGGEKPYLSPDI
HHHHCCCCCCCCHHH		42.0926051181
379PhosphorylationGGEKPYLSPDILEEK
CCCCCCCCHHHHHHH		18.0625159151
386UbiquitinationSPDILEEKHCEFKQL
CHHHHHHHCCHHHHH		44.15-
3862-HydroxyisobutyrylationSPDILEEKHCEFKQL
CHHHHHHHCCHHHHH		44.15-
391 (in isoform 1)Ubiquitination-23.3121890473
391AcetylationEEKHCEFKQLALDHF
HHHCCHHHHHHHHHH		23.3119608861
391UbiquitinationEEKHCEFKQLALDHF
HHHCCHHHHHHHHHH		23.312189047
3992-HydroxyisobutyrylationQLALDHFKKTKKMGG
HHHHHHHHHHHHCCC		56.99-
399AcetylationQLALDHFKKTKKMGG
HHHHHHHHHHHHCCC		56.9925953088
400AcetylationLALDHFKKTKKMGGK
HHHHHHHHHHHCCCC		65.7119822203
402AcetylationLDHFKKTKKMGGKDF
HHHHHHHHHCCCCCC		50.0319822211
407UbiquitinationKTKKMGGKDFSFRYQ
HHHHCCCCCCCHHHH		50.28-
407MalonylationKTKKMGGKDFSFRYQ
HHHHCCCCCCCHHHH		50.2826320211
410PhosphorylationKMGGKDFSFRYQQEL
HCCCCCCCHHHHHHH		20.9624719451
430UbiquitinationELYENFCKHNGSKNV
HHHHHHHHHCCCCCH		35.65-
515PhosphorylationAYVLEQASSHIGNST
HHHHHHHHHHCCCCC		23.3430576142
522PhosphorylationSSHIGNSTQATVRDA
HHHCCCCCCCHHHHH		26.6530576142
525PhosphorylationIGNSTQATVRDAVVG
CCCCCCCHHHHHHCC		13.2730576142
535PhosphorylationDAVVGRPSMDKKAQ-
HHHCCCCCCCCCCC-		37.9523401153
536SulfoxidationAVVGRPSMDKKAQ--
HHCCCCCCCCCCC--		10.9730846556
538UbiquitinationVGRPSMDKKAQ----
CCCCCCCCCCC----		41.17-
539UbiquitinationGRPSMDKKAQ-----
CCCCCCCCCC-----		47.99-
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 ATLA3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATLA3_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 ATLA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ASPH_HUMANASPHphysical
26344197
CALX_HUMANCANXphysical
26344197
EF1G_HUMANEEF1Gphysical
26344197
PHB2_HUMANPHB2physical
26344197
AL1B1_HUMANALDH1B1physical
26496610
AL3A2_HUMANALDH3A2physical
26496610
COPD_HUMANARCN1physical
26496610
AT2B1_HUMANATP2B1physical
26496610
ATPA_HUMANATP5A1physical
26496610
ATP5E_HUMANATP5Ephysical
26496610
BLMH_HUMANBLMHphysical
26496610
DVL3_HUMANDVL3physical
26496610
ETFB_HUMANETFBphysical
26496610
PUR2_HUMANGARTphysical
26496610
ITB1_HUMANITGB1physical
26496610
RAB1A_HUMANRAB1Aphysical
26496610
RAB5C_HUMANRAB5Cphysical
26496610
RNF5_HUMANRNF5physical
26496610
B3A2_HUMANSLC4A2physical
26496610
SPAG1_HUMANSPAG1physical
26496610
SPT6H_HUMANSUPT6Hphysical
26496610
TAP1_HUMANTAP1physical
26496610
TAP2_HUMANTAP2physical
26496610
VAPB_HUMANVAPBphysical
26496610
LONM_HUMANLONP1physical
26496610
SC22B_HUMANSEC22Bphysical
26496610
LGAT1_HUMANLPGAT1physical
26496610
UBP15_HUMANUSP15physical
26496610
TSSC4_HUMANTSSC4physical
26496610
RTN3_HUMANRTN3physical
26496610
ZN609_HUMANZNF609physical
26496610
ESYT1_HUMANESYT1physical
26496610
AT132_HUMANATP13A2physical
26496610
RAB14_HUMANRAB14physical
26496610
T161A_HUMANTMEM161Aphysical
26496610
DALD3_HUMANDALRD3physical
26496610
RTN4_HUMANRTN4physical
26496610
SNX14_HUMANSNX14physical
26496610
SRPRB_HUMANSRPRBphysical
26496610
FAKD5_HUMANFASTKD5physical
26496610
RBSK_HUMANRBKSphysical
26496610
ATLA2_HUMANATL2physical
26496610
TM109_HUMANTMEM109physical
26496610
TUT7_HUMANZCCHC6physical
26496610
ZN768_HUMANZNF768physical
26496610
L2HDH_HUMANL2HGDHphysical
26496610
RABL3_HUMANRABL3physical
26496610
PRS56_HUMANPRSS56physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615632Neuropathy, hereditary sensory, 1F (HSN1F)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATLA3_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-391, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-535, AND MASSSPECTROMETRY.

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