SNF8_HUMAN - dbPTM
SNF8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNF8_HUMAN
UniProt AC Q96H20
Protein Name Vacuolar-sorting protein SNF8
Gene Name SNF8
Organism Homo sapiens (Human).
Sequence Length 258
Subcellular Localization Cytoplasm. Endosome membrane. Nucleus . Late endosome membrane. Recruited to the endosome membrane to participate in vesicle formation.
Protein Description Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation by participating in derepression of transcription by RNA polymerase II, possibly via its interaction with ELL. Required for degradation of both endocytosed EGF and EGFR, but not for the EGFR ligand-mediated internalization. It is also required for the degradation of CXCR4. Required for the exosomal release of SDCBP, CD63 and syndecan. [PubMed: 22660413]
Protein Sequence MHRRGVGAGAIAKKKLAEAKYKERGTVLAEDQLAQMSKQLDMFKTNLEEFASKHKQEIRKNPEFRVQFQDMCATIGVDPLASGKGFWSEMLGVGDFYYELGVQIIEVCLALKHRNGGLITLEELHQQVLKGRGKFAQDVSQDDLIRAIKKLKALGTGFGIIPVGGTYLIQSVPAELNMDHTVVLQLAEKNGYVTVSEIKASLKWETERARQVLEHLLKEGLAWLDLQAPGEAHYWLPALFTDLYSQEITAEEAREALP
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
4Methylation----MHRRGVGAGAI
----CCCCCCCHHHH		29.4824129315
13UbiquitinationVGAGAIAKKKLAEAK
CCHHHHHHHHHHHCH		44.3133845483
14UbiquitinationGAGAIAKKKLAEAKY
CHHHHHHHHHHHCHH		43.95-
202-HydroxyisobutyrylationKKKLAEAKYKERGTV
HHHHHHCHHHHHCCC		48.65-
21PhosphorylationKKLAEAKYKERGTVL
HHHHHCHHHHHCCCC		25.7320068231
26UbiquitinationAKYKERGTVLAEDQL
CHHHHHCCCCCHHHH		20.6823000965
27UbiquitinationKYKERGTVLAEDQLA
HHHHHCCCCCHHHHH		5.4822817900
30UbiquitinationERGTVLAEDQLAQMS
HHCCCCCHHHHHHHH		41.9723000965
36UbiquitinationAEDQLAQMSKQLDMF
CHHHHHHHHHHHHHH		4.4932015554
36SulfoxidationAEDQLAQMSKQLDMF
CHHHHHHHHHHHHHH		4.4921406390
38 (in isoform 1)Ubiquitination-49.9221890473
38UbiquitinationDQLAQMSKQLDMFKT
HHHHHHHHHHHHHHH		49.9221963094
38 (in isoform 2)Ubiquitination-49.9221890473
44 (in isoform 2)Ubiquitination-29.8421890473
44 (in isoform 1)Ubiquitination-29.8421890473
44UbiquitinationSKQLDMFKTNLEEFA
HHHHHHHHHCHHHHH		29.8421906983
45UbiquitinationKQLDMFKTNLEEFAS
HHHHHHHHCHHHHHH		33.5029967540
53AcetylationNLEEFASKHKQEIRK
CHHHHHHHHHHHHHH		51.9325953088
53 (in isoform 1)Ubiquitination-51.9321890473
53 (in isoform 2)Ubiquitination-51.9321890473
53UbiquitinationNLEEFASKHKQEIRK
CHHHHHHHHHHHHHH		51.9321906983
55UbiquitinationEEFASKHKQEIRKNP
HHHHHHHHHHHHHCH		54.0522817900
99UbiquitinationGVGDFYYELGVQIIE
CCCHHHHHHHHHHHH		27.8932015554
113UbiquitinationEVCLALKHRNGGLIT
HHHHHHHHCCCCEEE		29.3223000965
117UbiquitinationALKHRNGGLITLEEL
HHHHCCCCEEEHHHH		19.9123000965
120PhosphorylationHRNGGLITLEELHQQ
HCCCCEEEHHHHHHH		32.91-
130 (in isoform 2)Ubiquitination-47.9421890473
130UbiquitinationELHQQVLKGRGKFAQ
HHHHHHHCCCCCCCC		47.9423000965
130 (in isoform 1)Ubiquitination-47.9421890473
132UbiquitinationHQQVLKGRGKFAQDV
HHHHHCCCCCCCCCC		43.4729967540
134 (in isoform 2)Ubiquitination-35.8421890473
134AcetylationQVLKGRGKFAQDVSQ
HHHCCCCCCCCCCCH		35.8425953088
134UbiquitinationQVLKGRGKFAQDVSQ
HHHCCCCCCCCCCCH		35.8423000965
134 (in isoform 1)Ubiquitination-35.8421890473
149UbiquitinationDDLIRAIKKLKALGT
HHHHHHHHHHHHCCC		51.5829967540
186UbiquitinationDHTVVLQLAEKNGYV
CCEEEEEEHHHCCEE		6.0932015554
192PhosphorylationQLAEKNGYVTVSEIK
EEHHHCCEEEHHHHH		11.4428152594
194PhosphorylationAEKNGYVTVSEIKAS
HHHCCEEEHHHHHHH		15.1628152594
196PhosphorylationKNGYVTVSEIKASLK
HCCEEEHHHHHHHCC		25.0028152594
201PhosphorylationTVSEIKASLKWETER
EHHHHHHHCCCCHHH		26.02-
202UbiquitinationVSEIKASLKWETERA
HHHHHHHCCCCHHHH		9.9932015554
203UbiquitinationSEIKASLKWETERAR
HHHHHHCCCCHHHHH		40.2532015554
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 SNF8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNF8_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 SNF8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS25_HUMANVPS25physical
16189514
NIF3L_HUMANNIF3L1physical
16189514
VPS25_HUMANVPS25physical
16371348
SNF8_HUMANSNF8physical
16371348
VPS36_HUMANVPS36physical
16371348
VPS20_YEASTVPS20physical
16371348
VPS25_YEASTVPS25physical
16371348
SNF8_YEASTSNF8physical
16371348
VPS36_YEASTVPS36physical
16371348
CHMP6_HUMANCHMP6physical
16371348
SNF8_HUMANSNF8physical
16973552
VPS36_HUMANVPS36physical
16973552
VPS25_HUMANVPS25physical
16973552
TS101_HUMANTSG101physical
16973552
CHMP6_HUMANCHMP6physical
14505570
VPS36_HUMANVPS36physical
14505570
SNF8_HUMANSNF8physical
14505570
TS101_HUMANTSG101physical
14505570
VPS25_HUMANVPS25physical
17010938
VPS36_HUMANVPS36physical
17010938
RET1_HUMANRBP1physical
19819239
MCM2_HUMANMCM2physical
19819239
ELL_HUMANELLphysical
19819239
KDM1A_HUMANKDM1Aphysical
23455924
ANM6_HUMANPRMT6physical
23455924
SUV92_HUMANSUV39H2physical
23455924
T2FA_HUMANGTF2F1physical
22863883
VAC14_HUMANVAC14physical
25416956
TRI54_HUMANTRIM54physical
25416956
VPS25_HUMANVPS25physical
25416956
TLN2_HUMANTLN2physical
26344197
VPS25_HUMANVPS25physical
21516116
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 SNF8_HUMAN

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Related Literatures of Post-Translational Modification

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