UBAP1_HUMAN - dbPTM
UBAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBAP1_HUMAN
UniProt AC Q9NZ09
Protein Name Ubiquitin-associated protein 1
Gene Name UBAP1
Organism Homo sapiens (Human).
Sequence Length 502
Subcellular Localization Cytoplasm, cytosol . Endosome . Predominantly cytosolic. Recruited to endosomes as part of the ESCRT-I complex.
Protein Description Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Plays a role in the proteasomal degradation of ubiquitinated cell-surface proteins, such as EGFR and BST2..
Protein Sequence MASKKLGADFHGTFSYLDDVPFKTGDKFKTPAKVGLPIGFSLPDCLQVVREVQYDFSLEKKTIEWAEEIKKIEEAEREAECKIAEAEAKVNSKSGPEGDSKMSFSKTHSTATMPPPINPILASLQHNSILTPTRVSSSATKQKVLSPPHIKADFNLADFECEEDPFDNLELKTIDEKEELRNILVGTTGPIMAQLLDNNLPRGGSGSVLQDEEVLASLERATLDFKPLHKPNGFITLPQLGNCEKMSLSSKVSLPPIPAVSNIKSLSFPKLDSDDSNQKTAKLASTFHSTSCLRNGTFQNSLKPSTQSSASELNGHHTLGLSALNLDSGTEMPALTSSQMPSLSVLSVCTEESSPPNTGPTVTPPNFSVSQVPNMPSCPQAYSELQMLSPSERQCVETVVNMGYSYECVLRAMKKKGENIEQILDYLFAHGQLCEKGFDPLLVEEALEMHQCSEEKMMEFLQLMSKFKEMGFELKDIKEVLLLHNNDQDNALEDLMARAGAS
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
4Acetylation----MASKKLGADFH
----CCCCCCCCCCC		42.3419821673
41PhosphorylationVGLPIGFSLPDCLQV
CCCCCCCCHHHHHHH		33.5028348404
49 (in isoform 4)Phosphorylation-2.5224247654
49 (in isoform 3)Phosphorylation-2.5224247654
61UbiquitinationYDFSLEKKTIEWAEE
CCCCCCHHHHHHHHH		45.41-
89 (in isoform 2)Ubiquitination-33.1921890473
89UbiquitinationKIAEAEAKVNSKSGP
HHHHHHHHHCCCCCC		33.1921906983
92PhosphorylationEAEAKVNSKSGPEGD
HHHHHHCCCCCCCCC		31.05-
93 (in isoform 2)Ubiquitination-54.9821890473
93UbiquitinationAEAKVNSKSGPEGDS
HHHHHCCCCCCCCCC		54.9821906983
94PhosphorylationEAKVNSKSGPEGDSK
HHHHCCCCCCCCCCC		60.44-
100PhosphorylationKSGPEGDSKMSFSKT
CCCCCCCCCCCCCCC		40.91-
101UbiquitinationSGPEGDSKMSFSKTH
CCCCCCCCCCCCCCC		43.22-
103PhosphorylationPEGDSKMSFSKTHST
CCCCCCCCCCCCCCC		30.0624719451
105PhosphorylationGDSKMSFSKTHSTAT
CCCCCCCCCCCCCCC		29.36-
107PhosphorylationSKMSFSKTHSTATMP
CCCCCCCCCCCCCCC		21.6228348404
109PhosphorylationMSFSKTHSTATMPPP
CCCCCCCCCCCCCCC		25.6021712546
110PhosphorylationSFSKTHSTATMPPPI
CCCCCCCCCCCCCCC		20.6728348404
112PhosphorylationSKTHSTATMPPPINP
CCCCCCCCCCCCCCH		30.2427251275
128PhosphorylationLASLQHNSILTPTRV
HHHHHCCCCCCCCCC		19.4925627689
131PhosphorylationLQHNSILTPTRVSSS
HHCCCCCCCCCCCCC		22.4225159151
146PhosphorylationATKQKVLSPPHIKAD
CCCCCCCCCCCEECC		39.1030266825
151UbiquitinationVLSPPHIKADFNLAD
CCCCCCEECCCCCCC		38.58-
153 (in isoform 1)Ubiquitination-28.1521890473
157 (in isoform 1)Ubiquitination-22.1321890473
173 (in isoform 4)Phosphorylation-46.4127251275
177 (in isoform 2)Ubiquitination-53.3821890473
177UbiquitinationELKTIDEKEELRNIL
EEEECCCHHHHHHHH		53.3821906983
205PhosphorylationNNLPRGGSGSVLQDE
CCCCCCCCCCCCCCH		30.6222617229
207PhosphorylationLPRGGSGSVLQDEEV
CCCCCCCCCCCCHHH		22.7321712546
210 (in isoform 4)Phosphorylation-54.6424719451
217PhosphorylationQDEEVLASLERATLD
CCHHHHHHHHHCCCC		26.9723403867
226UbiquitinationERATLDFKPLHKPNG
HHCCCCCCCCCCCCC		46.46-
241 (in isoform 1)Ubiquitination-31.3421890473
247PhosphorylationLGNCEKMSLSSKVSL
CCCCEECCCCCCCCC		35.8528450419
249PhosphorylationNCEKMSLSSKVSLPP
CCEECCCCCCCCCCC		22.3227251275
250PhosphorylationCEKMSLSSKVSLPPI
CEECCCCCCCCCCCC		42.2328450419
251UbiquitinationEKMSLSSKVSLPPIP
EECCCCCCCCCCCCC		32.25-
253PhosphorylationMSLSSKVSLPPIPAV
CCCCCCCCCCCCCCC		38.6125394399
261O-linked_GlycosylationLPPIPAVSNIKSLSF
CCCCCCCCCCCCCCC		34.6423301498
264AcetylationIPAVSNIKSLSFPKL
CCCCCCCCCCCCCCC		49.9825953088
264 (in isoform 2)Ubiquitination-49.9821890473
264UbiquitinationIPAVSNIKSLSFPKL
CCCCCCCCCCCCCCC		49.9821890473
265PhosphorylationPAVSNIKSLSFPKLD
CCCCCCCCCCCCCCC		26.0028857561
267PhosphorylationVSNIKSLSFPKLDSD
CCCCCCCCCCCCCCC		46.7423911959
269 (in isoform 4)Phosphorylation-32.6827251275
270UbiquitinationIKSLSFPKLDSDDSN
CCCCCCCCCCCCCCC		64.02-
271 (in isoform 4)Phosphorylation-8.5224719451
273PhosphorylationLSFPKLDSDDSNQKT
CCCCCCCCCCCCHHH		54.4726074081
276PhosphorylationPKLDSDDSNQKTAKL
CCCCCCCCCHHHHHH		46.2626074081
280PhosphorylationSDDSNQKTAKLASTF
CCCCCHHHHHHHHHH		21.1826074081
281 (in isoform 4)Phosphorylation-16.3527251275
282AcetylationDSNQKTAKLASTFHS
CCCHHHHHHHHHHHH		50.2225953088
285PhosphorylationQKTAKLASTFHSTSC
HHHHHHHHHHHHHHH		41.8823312004
286PhosphorylationKTAKLASTFHSTSCL
HHHHHHHHHHHHHHH		21.5423312004
289PhosphorylationKLASTFHSTSCLRNG
HHHHHHHHHHHHHCC		20.1621757351
290PhosphorylationLASTFHSTSCLRNGT
HHHHHHHHHHHHCCC		18.1928857561
291PhosphorylationASTFHSTSCLRNGTF
HHHHHHHHHHHCCCC		17.7328555341
297PhosphorylationTSCLRNGTFQNSLKP
HHHHHCCCCCCCCCC		26.1226270265
301PhosphorylationRNGTFQNSLKPSTQS
HCCCCCCCCCCCCCC		27.3026270265
317 (in isoform 4)Phosphorylation-24.9624719451
328UbiquitinationLSALNLDSGTEMPAL
CEEEECCCCCCCCCC		51.2721890473
328 (in isoform 1)Ubiquitination-51.2721890473
328UbiquitinationLSALNLDSGTEMPAL
CEEEECCCCCCCCCC		51.2721890473
331 (in isoform 4)Phosphorylation-46.8524719451
350 (in isoform 4)Phosphorylation-40.4027251275
353 (in isoform 4)Phosphorylation-41.7424719451
475UbiquitinationKEMGFELKDIKEVLL
HHCCCCHHCHHHHEE		50.65-
478UbiquitinationGFELKDIKEVLLLHN
CCCHHCHHHHEECCC		52.48-
502PhosphorylationLMARAGAS-------
HHHHHCCC-------		39.5818452278
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 UBAP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBAP1_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 UBAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VP37A_HUMANVPS37Aphysical
21757351
TS101_HUMANTSG101physical
21757351
UBAP1_HUMANUBAP1physical
22405001
TS101_HUMANTSG101physical
22405001
VPS28_HUMANVPS28physical
22405001
VP37A_HUMANVPS37Aphysical
22405001
K1468_HUMANKIAA1468physical
22863883
TS101_HUMANTSG101physical
24284069
VP37A_HUMANVPS37Aphysical
24284069
TS101_HUMANTSG101physical
26456826
UBC_HUMANUBCphysical
26456826
ITA5_HUMANITGA5physical
26456826
VP37A_HUMANVPS37Aphysical
28514442
VP37B_HUMANVPS37Bphysical
28514442
TS101_HUMANTSG101physical
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 UBAP1_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-205, AND MASSSPECTROMETRY.

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