dbPTM

LID2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	LID2_SCHPO
UniProt AC	Q9HDV4
Protein Name	Lid2 complex component lid2
Gene Name	lid2
Organism	Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length	1513
Subcellular Localization	Nucleus .
Protein Description
Protein Sequence	MICQLLWHEHNSMGSGREKKIRKLGDNFSLPYLKFDCDHNDKNYRASNRPFGLSTGLSVQLNASNMTDPFKFLLDNWHTIFKNGAIKLLPPEGWQIPVVLDQGAFEFQSKRQCLNKGCLNYEKNYDYFKKLKAFHESRGLYFYHPPIIGNRPVDFLRLRNAISKFTNSGSSLNNEILHKVIIYLRLEDTKEVRQVLTRCYDRYIKPFERDSSPSFKSKRSESSTRKIRNTRSSAQQESPIPETSAQSPVQTIQVNGSTSLKRPLIERGEQCEYCGLDKNPETILLCDGCEAAYHTSCLDPPLTSIPKEDWYCDACKFNISDYDPRKGFKWKLSSLKERSAEIFNTLGERNSSSKLTNLTEDDIELFYWSSLAESNSGFAPLELEGLSQAYTSTIQSSLPSKEVFPLEKYSSEPWNLHNLPFENPCLFNYSFSDLSSLTITRLSIGMVFYTHGWTKSSLSTGLLHHHRFGDTVTWYVLPPDESDAFERYLISSYPQYTMEDLNRSNGLPVIVSPSSLIENGFHPIAIDLRPNEFLVVSPNSYHMGFHQGFSSFESVNFATVNWIKDGLLNSSISVLKSMRIPSSVSYEAVIISMVLSKNPCFSSEWLIKCFEDMIANESASKNEIMKLVPNIQALKLESSVPLEIRCSNCKQPCFLSFMQCHEPKKFICLGDCVKEVSLNATSWMLFYRWDVHELSNLAERFVSLIRGPEEWTNRLRSVLSTSPKPQLKVLKSLLVDAEKAMLTTPETVNLRDFVQNANSWIDSVNECLKVASLKRKKDKKPPLFKAHDHWNNTSNLKDSAVLFKVLQTSRSMAFTCQEIENMKQKAFDLLEFRNRLINSFSGPLDKNTCQRLLTEAELLGFTIPELGIIQKYLIQFEWLDMFYSFETTRTTDSDLERLITYGVSAGIPEDNDYMIFAKAMKGRAEIWENQVYDTLSKSNISYDKLSLLRDEAMNLCVNKELFSKVVGILNNAEEIKNKIATLCERSQEKDFALRPSIDEVKEALASAEKLPILSESTVTLQKMYDVVLEWIRRGKRLFGKANAPLEILGQHLDYVEKRNSASLSLNDRPGPPMEPASRETSPDSEGRLTIRKKKGCIFCFCRLPESGVMIECEICHEWYHAKCLKMSKKKLRQDEKFTCPICDYRVEIPRLSNRPKLEDLQSLYKDVKLLPFQPKETETLRKVVDLASKFRQEMQALAHNPFGLTMAEVPLARFYLRKMEGAEILLVDETNLFRQKLHECVPIAPNPPPIIGESKSTRKPRPTKRQRQIMKQVAEGLLPASAIAPPKSSNEKKSSNNVKAVEAETKSKSEKSPKKNGTNISDANNKNESHVSLMKNWKLGSPAFVTLVKEKNSSCLCGEEFSPRDSFIDCTICERRFHYDCVGLNNEIADSVSKFTCPICMEQSGGIYPWQLRPRNGMHPDHISGFSKEVETDPKLGSSGYTLNNSKFDKAAVSKTLSAQDVSRLQKVSCGEHLYFGTDVFTPLGDMATSASMFSLDDSSEKTDAFTENFLNV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
722	Phosphorylation	LRSVLSTSPKPQLKV HHHHHCCCCCHHHHH	27.79	28889911
1077	Phosphorylation	GPPMEPASRETSPDS CCCCCCCCCCCCCCC	41.17	25720772
1080	Phosphorylation	MEPASRETSPDSEGR CCCCCCCCCCCCCCC	44.44	25720772
1081	Phosphorylation	EPASRETSPDSEGRL CCCCCCCCCCCCCCE	23.20	25720772
1341	Phosphorylation	MKNWKLGSPAFVTLV HHHHCCCCCEEEEEE	24.40	25720772
1458	Phosphorylation	AAVSKTLSAQDVSRL HHHHCCCCHHHHHHH	29.17	24763107

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 LID2_SCHPO !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of LID2_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 LID2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASH2_SCHPO	ash2	physical	14617822
LID2_SCHPO	lid2	physical	14617822
JMJ3_SCHPO	jmj3	physical	14617822
SNT2_SCHPO	snt2	physical	14617822
YIDH_SCHPO	SPAC227.17c	genetic	22681890

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of LID2_SCHPO

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-722, AND MASSSPECTROMETRY.	18257517 [Abstract]