ULP2_SCHPO - dbPTM
ULP2_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ULP2_SCHPO
UniProt AC O13769
Protein Name Ubiquitin-like-specific protease 2
Gene Name ulp2
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 638
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MRDSKDALDDKSGSFTSLLPPFGKQRGTSPNDAIPIKSPLERLANSVTSPEKPTVRTAIQKDSPRRKQIDDDQTPPKHLKRSFQNVTVVSPRKKKTIDVVELPFTKGGYGGFYDPRPGCLKFTTHEINVSYTDTSIPVIHIPVQLLKRCCWLQGWRDNLVESPVHAIHLTLKNRDMKRITIGDSASLLFLYNPLHVESARAGLDLLDQSDFSLTSPSSAKEFKQLLTLKQSTIIPRTPQKTVRSIVKQTSSPHSSKMPKHSLPSSPTPFNSNSGDSLLSRIKNSNQSSSERPTANNGAQEQNQSSSSAGNTSNDFSTLCSQGSDKTLLSDASCTTILVYPFSGTNSIAITNTDLTRLNEGEFLNDTIVDFYLRYLYCKLQTQNPSLANDTHIFNTFFYNRLTSKDKDGKRLGHRGVRKWTQKVDLFHKKYIIVPINETFHWYLAIICNIDRLMPVDTKLEEQDEIVMSSVEQPSASKTRQAELTSNSPAILIFDSLANLHKGALNYLREYLLEEAFERKNVHLKSTDIRGFHAKVPQQSNFSDCGIYALHFVELFLETPEQVIANTLDKSLRRTDAKNFDQQWNLQKINTMRCDLKGLIRRLSTEWSSNNERQSLSSGSNDEEDKENDDDLAILPITN
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
28PhosphorylationPFGKQRGTSPNDAIP
CCCCCCCCCCCCCCC		43.1125720772
29PhosphorylationFGKQRGTSPNDAIPI
CCCCCCCCCCCCCCC		25.2429996109
38PhosphorylationNDAIPIKSPLERLAN
CCCCCCCCHHHHHHH		35.1225720772
46PhosphorylationPLERLANSVTSPEKP
HHHHHHHCCCCCCCC		22.5929996109
48PhosphorylationERLANSVTSPEKPTV
HHHHHCCCCCCCCCH		38.0829996109
49PhosphorylationRLANSVTSPEKPTVR
HHHHCCCCCCCCCHH		28.9829996109
63PhosphorylationRTAIQKDSPRRKQID
HHHHHCCCCCHHCCC		27.6029996109
74PhosphorylationKQIDDDQTPPKHLKR
HCCCCCCCCCHHHHH		48.8629996109
87PhosphorylationKRSFQNVTVVSPRKK
HHHHCCCEEECCCCC		23.8028889911
90PhosphorylationFQNVTVVSPRKKKTI
HCCCEEECCCCCCEE		18.0428889911
237PhosphorylationQSTIIPRTPQKTVRS
HCCCCCCCCHHHHHH		25.3924763107
261PhosphorylationSSKMPKHSLPSSPTP
CCCCCCCCCCCCCCC		48.3724763107
264PhosphorylationMPKHSLPSSPTPFNS
CCCCCCCCCCCCCCC		55.0028889911
265PhosphorylationPKHSLPSSPTPFNSN
CCCCCCCCCCCCCCC		30.7421712547
267PhosphorylationHSLPSSPTPFNSNSG
CCCCCCCCCCCCCCH		42.3225720772
271PhosphorylationSSPTPFNSNSGDSLL
CCCCCCCCCCHHHHH		32.5221712547
276PhosphorylationFNSNSGDSLLSRIKN
CCCCCHHHHHHHHHC		34.4321712547
526PhosphorylationKNVHLKSTDIRGFHA
CCCCCCCCCCCCCCC		33.5828889911
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 ULP2_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ULP2_SCHPO !!
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 ULP2_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PMT3_SCHPOpmt3physical
24818994
IF4G_SCHPOtif471physical
24818994
RPA1_SCHPOnuc1physical
24818994
YIW2_SCHPOSPAC694.02physical
24818994
XRN1_SCHPOexo2physical
24818994
RPA2_SCHPOrpa2physical
24818994
XRN2_SCHPOdhp1physical
24818994
EF3_SCHPOtef3physical
24818994
EIF3A_SCHPOtif32physical
24818994
EIF3C_SCHPOtif33physical
24818994
PFKA_SCHPOpfk1physical
24818994
EF2_SCHPOeft202physical
24818994
ACON2_SCHPOSPBP4H10.15physical
24818994
ULP2_SCHPOulp2physical
24818994
EIF3B_SCHPOSPAC25G10.08physical
24818994
PAT1_SCHPOSPBC19G7.10cphysical
24818994
NOP2_SCHPOnop2physical
24818994
KRI1_SCHPOkri1physical
24818994
YKY4_SCHPOSPAC1142.04physical
24818994
YBPC_SCHPOSPBC16H5.12cphysical
24818994
SSB1_SCHPOsks2physical
24818994
TRM6_SCHPOgcd10physical
24818994
DBP2_SCHPOdbp2physical
24818994
TCG1_SCHPOtcg1physical
24818994
PRP19_SCHPOprp19physical
24818994
LAH1_SCHPOsla1physical
24818994
RL3A_SCHPOrpl301physical
24818994
RL3B_SCHPOrpl302physical
24818994
EIF3H_SCHPOSPAC821.05physical
24818994
IF2B_SCHPOtif212physical
24818994
PROB_SCHPOSPAC17H9.13cphysical
24818994
RFC5_SCHPOrfc5physical
24818994
G3P1_SCHPOtdh1physical
24818994
RML2_SCHPOrml2physical
24818994
G3P2_SCHPOgpd3physical
24818994
IF2A_SCHPOtif211physical
24818994
RRP5_SCHPOSPCC1183.07physical
24818994
RENT1_SCHPOupf1physical
24818994
PABP_SCHPOpabpphysical
24818994
NU132_SCHPOnup132genetic
26221037
PLI1_SCHPOpli1genetic
26221037
PMT3_SCHPOpmt3genetic
21444718
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ULP2_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526, AND MASSSPECTROMETRY.

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