ASPC1_HUMAN - dbPTM
ASPC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASPC1_HUMAN
UniProt AC Q9BZE9
Protein Name Tether containing UBX domain for GLUT4
Gene Name ASPSCR1
Organism Homo sapiens (Human).
Sequence Length 553
Subcellular Localization Endomembrane system
Peripheral membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane
Peripheral membrane protein. Cytoplasm . Nucleus .
Protein Description Tethering protein that sequesters GLUT4-containing vesicles in the cytoplasm in the absence of insulin. Modulates the amount of GLUT4 that is available at the cell surface (By similarity). Enhances VCP methylation catalyzed by VCPKMT..
Protein Sequence MAAPAGGGGSAVSVLAPNGRRHTVKVTPSTVLLQVLEDTCRRQDFNPCEYDLKFQRSVLDLSLQWRFANLPNNAKLEMVPASRSREGPENMVRIALQLDDGSRLQDSFCSGQTLWELLSHFPQIRECLQHPGGATPVCVYTRDEVTGEAALRGTTLQSLGLTGGSATIRFVMKCYDPVGKTPGSLGSSASAGQAAASAPLPLESGELSRGDLSRPEDADTSGPCCEHTQEKQSTRAPAAAPFVPFSGGGQRLGGPPGPTRPLTSSSAKLPKSLSSPGGPSKPKKSKSGQDPQQEQEQERERDPQQEQERERPVDREPVDREPVVCHPDLEERLQAWPAELPDEFFELTVDDVRRRLAQLKSERKRLEEAPLVTKAFREAQIKEKLERYPKVALRVLFPDRYVLQGFFRPSETVGDLRDFVRSHLGNPELSFYLFITPPKTVLDDHTQTLFQANLFPAALVHLGAEEPAGVYLEPGLLEHAISPSAADVLVARYMSRAAGSPSPLPAPDPAPKSEPAAEEGALVPPEPIPGTAQPVKRSLGKVPKWLKLPASKR
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
2Acetylation------MAAPAGGGG
------CCCCCCCCC		23.3522223895
27PhosphorylationRRHTVKVTPSTVLLQ
CEEEEEECHHHHHHH		13.0525693802
29PhosphorylationHTVKVTPSTVLLQVL
EEEEECHHHHHHHHH		23.0628348404
30PhosphorylationTVKVTPSTVLLQVLE
EEEECHHHHHHHHHH		19.1728348404
40GlutathionylationLQVLEDTCRRQDFNP
HHHHHHHHHHCCCCC		5.3722555962
57PhosphorylationYDLKFQRSVLDLSLQ
CCHHHHHHHHHHHHH		19.0927251275
75UbiquitinationANLPNNAKLEMVPAS
CCCCCCCEEEEEECC		47.2922817900
75 (in isoform 1)Ubiquitination-47.2921906983
75 (in isoform 2)Ubiquitination-47.2921906983
154PhosphorylationGEAALRGTTLQSLGL
CCHHHCCCEEECCCC		20.2127080861
155PhosphorylationEAALRGTTLQSLGLT
CHHHCCCEEECCCCC		26.1427080861
158PhosphorylationLRGTTLQSLGLTGGS
HCCCEEECCCCCCCC		27.7627080861
162PhosphorylationTLQSLGLTGGSATIR
EEECCCCCCCCEEEE		37.3827080861
165PhosphorylationSLGLTGGSATIRFVM
CCCCCCCCEEEEEEE		24.4727080861
167PhosphorylationGLTGGSATIRFVMKC
CCCCCCEEEEEEEEC		17.8727080861
181PhosphorylationCYDPVGKTPGSLGSS
CCCCCCCCCCCCCCC		27.2728348404
184PhosphorylationPVGKTPGSLGSSASA
CCCCCCCCCCCCCHH		30.6628348404
187PhosphorylationKTPGSLGSSASAGQA
CCCCCCCCCCHHHHH		28.2028348404
187O-linked_GlycosylationKTPGSLGSSASAGQA
CCCCCCCCCCHHHHH		28.2023301498
188PhosphorylationTPGSLGSSASAGQAA
CCCCCCCCCHHHHHH		25.1728348404
190PhosphorylationGSLGSSASAGQAAAS
CCCCCCCHHHHHHHC		34.5728348404
198PhosphorylationAGQAAASAPLPLESG
HHHHHHCCCCCCCCC		12.6232142685
246PhosphorylationAAPFVPFSGGGQRLG
CCCCCCCCCCCCCCC		30.3823312004
246O-linked_GlycosylationAAPFVPFSGGGQRLG
CCCCCCCCCCCCCCC		30.3823301498
259PhosphorylationLGGPPGPTRPLTSSS
CCCCCCCCCCCCCCC		51.3228857561
263PhosphorylationPGPTRPLTSSSAKLP
CCCCCCCCCCCCCCC		29.2820068231
264PhosphorylationGPTRPLTSSSAKLPK
CCCCCCCCCCCCCCC		29.9420068231
265PhosphorylationPTRPLTSSSAKLPKS
CCCCCCCCCCCCCCC		29.1320068231
266PhosphorylationTRPLTSSSAKLPKSL
CCCCCCCCCCCCCCC		29.2320068231
268AcetylationPLTSSSAKLPKSLSS
CCCCCCCCCCCCCCC		68.2425953088
272PhosphorylationSSAKLPKSLSSPGGP
CCCCCCCCCCCCCCC		31.3830183078
274PhosphorylationAKLPKSLSSPGGPSK
CCCCCCCCCCCCCCC		41.3923911959
275PhosphorylationKLPKSLSSPGGPSKP
CCCCCCCCCCCCCCC		32.6223401153
280PhosphorylationLSSPGGPSKPKKSKS
CCCCCCCCCCCCCCC		65.9423403867
281AcetylationSSPGGPSKPKKSKSG
CCCCCCCCCCCCCCC		65.0825953088
283UbiquitinationPGGPSKPKKSKSGQD
CCCCCCCCCCCCCCC		73.7029967540
285PhosphorylationGPSKPKKSKSGQDPQ
CCCCCCCCCCCCCHH		37.8727251275
287PhosphorylationSKPKKSKSGQDPQQE
CCCCCCCCCCCHHHH		49.1027135362
287UbiquitinationSKPKKSKSGQDPQQE
CCCCCCCCCCCHHHH		49.1029967540
297UbiquitinationDPQQEQEQERERDPQ
CHHHHHHHHHHHCHH		55.5321963094
317 (in isoform 4)Phosphorylation-33.9116674116
360UbiquitinationRRRLAQLKSERKRLE
HHHHHHHHHHHHHHH		37.8829967540
364UbiquitinationAQLKSERKRLEEAPL
HHHHHHHHHHHHCCH		58.2329967540
374UbiquitinationEEAPLVTKAFREAQI
HHCCHHHHHHHHHHH		37.7421963094
410O-linked_GlycosylationLQGFFRPSETVGDLR
EEEECCCCCCHHHHH		41.4623301498
484UbiquitinationLEHAISPSAADVLVA
HHHCCCHHHHHHHHH		29.3329967540
493PhosphorylationADVLVARYMSRAAGS
HHHHHHHHHHHHCCC		6.9522115753
495UbiquitinationVLVARYMSRAAGSPS
HHHHHHHHHHCCCCC		15.1629967540
495PhosphorylationVLVARYMSRAAGSPS
HHHHHHHHHHCCCCC		15.1623612710
499 (in isoform 2)Phosphorylation-38.8220068231
500O-linked_GlycosylationYMSRAAGSPSPLPAP
HHHHHCCCCCCCCCC		19.92OGP
500PhosphorylationYMSRAAGSPSPLPAP
HHHHHCCCCCCCCCC		19.9229255136
502PhosphorylationSRAAGSPSPLPAPDP
HHHCCCCCCCCCCCC		40.5419664994
513PhosphorylationAPDPAPKSEPAAEEG
CCCCCCCCCCCHHCC		47.9923090842
519 (in isoform 2)Phosphorylation-45.0721406692
520 (in isoform 2)Phosphorylation-18.7321406692
523 (in isoform 2)Phosphorylation-8.0321406692
531PhosphorylationPPEPIPGTAQPVKRS
CCCCCCCCCCCCHHH		19.4323090842
536UbiquitinationPGTAQPVKRSLGKVP
CCCCCCCHHHCCCCC		42.8429967540
538PhosphorylationTAQPVKRSLGKVPKW
CCCCCHHHCCCCCCC		35.4423090842
541AcetylationPVKRSLGKVPKWLKL
CCHHHCCCCCCCCCC		61.7325953088
547UbiquitinationGKVPKWLKLPASKR-
CCCCCCCCCCCCCC-		51.8429967540
552AcetylationWLKLPASKR------
CCCCCCCCC------		65.3212433901
630Ubiquitination------------------------------------------------------------------------------------
------------------------------------------------------------------------------------		29967540
641Ubiquitination-----------------------------------------------------------------------------------------------
-----------------------------------------------------------------------------------------------		29967540
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 ASPC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASPC1_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 ASPC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
18775313
PPB1_HUMANALPPphysical
18775313
NPL4_HUMANNPLOC4physical
18775313
UFD1_HUMANUFD1Lphysical
18775313
VCIP1_HUMANVCPIP1physical
18775313
PHAX_HUMANPHAXphysical
21900206
TERA_HUMANVCPphysical
21900206
TERA_HUMANVCPphysical
22350894
A4_HUMANAPPphysical
21832049
KR108_HUMANKRTAP10-8physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
TERA_HUMANVCPphysical
25078495
NSF_HUMANNSFphysical
25078495
GDE_HUMANAGLphysical
26344197
YTHD1_HUMANYTHDF1physical
26344197
YTHD2_HUMANYTHDF2physical
26344197
Drug and Disease Associations
Kegg Disease
H00051 Alveolar soft part sarcoma
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 ASPC1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-500 AND SER-502, AND MASS SPECTROMETRY.
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-500 AND SER-502, ANDMASS SPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-500 AND SER-502, AND MASS SPECTROMETRY.
"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-263 AND SER-264, ANDMASS SPECTROMETRY.

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