U17L2_HUMAN - dbPTM
U17L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID U17L2_HUMAN
UniProt AC Q6R6M4
Protein Name Ubiquitin carboxyl-terminal hydrolase 17
Gene Name USP17L2
Organism Homo sapiens (Human).
Sequence Length 530
Subcellular Localization Nucleus . Endoplasmic reticulum .
Protein Description Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes. Regulates cell proliferation by deubiquitinating and inhibiting RCE1 thereby controlling the small GTPases NRAS and HRAS localization and activation. In parallel, mediates deubiquitination of CDC25A, preventing CDC25A degradation by the proteasome during the G1/S and G2/M phases promoting cell-cycle progression. Also regulates cell proliferation and apoptosis through deubiquitination of SUDS3 a regulator of histone deacetylation. Through activation of the Rho family GTPases RAC1A, CDC42 and RHOA, regulates cell migration. Through the cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains of the cytoplasmic innate immune receptors DDX58 and IFIH1 stimulates the cellular response to viral infection..
Protein Sequence MEDDSLYLGGEWQFNHFSKLTSSRPDAAFAEIQRTSLPEKSPLSSEARVDLCDDLAPVARQLAPRKKLPLSSRRPAAVGAGLQNMGNTCYENASLQCLTYTPPLANYMLSREHSQTCQRPKCCMLCTMQAHITWALHSPGHVIQPSQALAAGFHRGKQEDAHEFLMFTVDAMKKACLPGHKQVDHHSKDTTLIHQIFGGCWRSQIKCLHCHGISDTFDPYLDIALDIQAAQSVKQALEQLVKPEELNGENAYHCGLCLQRAPASKTLTLHTSAKVLILVLKRFSDVTGNKLAKNVQYPECLDMQPYMSQQNTGPLVYVLYAVLVHAGWSCHDGHYFSYVKAQEGQWYKMDDAKVTACSITSVLSQQAYVLFYIQKSEWERHSESVSRGREPRALGAEDTDRRATQGELKRDHPCLQAPELDERLVERATQESTLDHWKFPQEQNKTKPEFNVRKVEGTLPPNVLVIHQSKYKCGMKNHHPEQQSSLLNLSSTTRTDQESVNTGTLASLQGRTRRSKGKNKHSKRALLVCQ
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
272PhosphorylationKTLTLHTSAKVLILV
CEEEEECHHHHHHHH
18.49-
284PhosphorylationILVLKRFSDVTGNKL
HHHHHHHCCCCCCHH
34.89-
287PhosphorylationLKRFSDVTGNKLAKN
HHHHCCCCCCHHHCC
39.77-
358PhosphorylationDAKVTACSITSVLSQ
CCEEEEEEHHHHHHC
26.83-
360PhosphorylationKVTACSITSVLSQQA
EEEEEEHHHHHHCCE
9.11-
361PhosphorylationVTACSITSVLSQQAY
EEEEEHHHHHHCCEE
21.28-
368PhosphorylationSVLSQQAYVLFYIQK
HHHHCCEEEEEEEEH
8.05-
399PhosphorylationRALGAEDTDRRATQG
CCCCCCCCCCHHHHC
23.94-
504PhosphorylationQESVNTGTLASLQGR
HHHCHHCHHHHHCCC
19.6722210691
512PhosphorylationLASLQGRTRRSKGKN
HHHHCCCCCCCCCCC
36.9422210691
515PhosphorylationLQGRTRRSKGKNKHS
HCCCCCCCCCCCCCC
42.3322210691

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 U17L2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of U17L2_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 U17L2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SET_HUMANSETphysical
19615732
CBX1_HUMANCBX1physical
19615732
U17L7_HUMANUSP17L7physical
19615732
MPIP3_HUMANCDC25Cphysical
20228808
H2AX_HUMANH2AFXphysical
24704006
LGMN_HUMANLGMNphysical
24610907
SDS3_HUMANSUDS3physical
21239494
HDAC2_HUMANHDAC2physical
26617781
IL33_HUMANIL33physical
26610488
SNAI1_HUMANSNAI1physical
28198361
SNAI1_HUMANSNAI1physical
28067227
CDK4_HUMANCDK4physical
28067227
CDK6_HUMANCDK6physical
28067227
SNAI2_HUMANSNAI2physical
29088851
TWST1_HUMANTWIST1physical
29088851

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of U17L2_HUMAN

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Related Literatures of Post-Translational Modification

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