ISY1_HUMAN - dbPTM
ISY1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ISY1_HUMAN
UniProt AC Q9ULR0
Protein Name Pre-mRNA-splicing factor ISY1 homolog
Gene Name ISY1
Organism Homo sapiens (Human).
Sequence Length 285
Subcellular Localization Nucleus .
Protein Description May play a role in pre-mRNA splicing as component of the spliceosome..
Protein Sequence MARNAEKAMTALARFRQAQLEEGKVKERRPFLASECTELPKAEKWRRQIIGEISKKVAQIQNAGLGEFRIRDLNDEINKLLREKGHWEVRIKELGGPDYGKVGPKMLDHEGKEVPGNRGYKYFGAAKDLPGVRELFEKEPLPPPRKTRAELMKAIDFEYYGYLDEDDGVIVPLEQEYEKKLRAELVEKWKAEREARLARGEKEEEEEEEEEINIYAVTEEESDEEGSQEKGGDDSQQKFIAHVPVPSQQEIEEALVRRKKMELLQKYASETLQAQSEEARRLLGY
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
7Acetylation-MARNAEKAMTALAR
-CCCHHHHHHHHHHH		40.8425953088
7Ubiquitination-MARNAEKAMTALAR
-CCCHHHHHHHHHHH		40.8424816145
24UbiquitinationQAQLEEGKVKERRPF
HHHHHCCCCCCCCCC		54.1124816145
34PhosphorylationERRPFLASECTELPK
CCCCCCHHHHCCCCH		35.0427174698
37PhosphorylationPFLASECTELPKAEK
CCCHHHHCCCCHHHH		36.1827174698
41AcetylationSECTELPKAEKWRRQ
HHHCCCCHHHHHHHH		80.1226051181
54PhosphorylationRQIIGEISKKVAQIQ
HHHHHHHHHHHHHHH		23.3222985185
56UbiquitinationIIGEISKKVAQIQNA
HHHHHHHHHHHHHHC		35.6929967540
79UbiquitinationDLNDEINKLLREKGH
HHHHHHHHHHHHCCC		55.3424816145
99PhosphorylationKELGGPDYGKVGPKM
HHCCCCCCCCCCHHH		23.2118083107
101AcetylationLGGPDYGKVGPKMLD
CCCCCCCCCCHHHCC		37.4826051181
101UbiquitinationLGGPDYGKVGPKMLD
CCCCCCCCCCHHHCC		37.4824816145
121AcetylationVPGNRGYKYFGAAKD
CCCCCCCCCCCCCCC		36.6125953088
127UbiquitinationYKYFGAAKDLPGVRE
CCCCCCCCCCCCHHH		60.3029967540
127AcetylationYKYFGAAKDLPGVRE
CCCCCCCCCCCCHHH		60.3019608861
138UbiquitinationGVRELFEKEPLPPPR
CHHHHHHCCCCCCCC		58.2424816145
215PhosphorylationEEEEINIYAVTEEES
HHHHCEEEEEECCCC		7.1921406692
218PhosphorylationEINIYAVTEEESDEE
HCEEEEEECCCCCCC		29.5230576142
222PhosphorylationYAVTEEESDEEGSQE
EEEECCCCCCCCCCC		54.3117525332
227PhosphorylationEESDEEGSQEKGGDD
CCCCCCCCCCCCCCC		38.1517525332
235PhosphorylationQEKGGDDSQQKFIAH
CCCCCCCHHCEEEEE		38.9725841592
244PhosphorylationQKFIAHVPVPSQQEI
CEEEEECCCCCHHHH		23.5717525332
247PhosphorylationIAHVPVPSQQEIEEA
EEECCCCCHHHHHHH		44.7417525332
249PhosphorylationHVPVPSQQEIEEALV
ECCCCCHHHHHHHHH		58.9517525332
259GlycationEEALVRRKKMELLQK
HHHHHHHHHHHHHHH		46.00-
260GlycationEALVRRKKMELLQKY
HHHHHHHHHHHHHHH		35.48-
260UbiquitinationEALVRRKKMELLQKY
HHHHHHHHHHHHHHH		35.4829967540
267PhosphorylationKMELLQKYASETLQA
HHHHHHHHHHHHHHH		11.4624719451
269PhosphorylationELLQKYASETLQAQS
HHHHHHHHHHHHHHH		28.2017525332
271PhosphorylationLQKYASETLQAQSEE
HHHHHHHHHHHHHHH		22.9824719451
276PhosphorylationSETLQAQSEEARRLL
HHHHHHHHHHHHHHH		40.18-
282UbiquitinationQSEEARRLLGY----
HHHHHHHHHCC----		3.4729967540
296 (in isoform 1)Phosphorylation--
299 (in isoform 1)Phosphorylation--
303 (in isoform 1)Phosphorylation-28985074
304 (in isoform 1)Phosphorylation-28985074
315 (in isoform 1)Phosphorylation-24275569
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 ISY1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ISY1_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 ISY1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLRG1_HUMANPLRG1physical
22939629
RU2A_HUMANSNRPA1physical
22939629
SYF1_HUMANXAB2physical
22365833
ISY1_HUMANISY1physical
22365833
DHX8_HUMANDHX8physical
22365833
AQR_HUMANAQRphysical
26344197
BUD31_HUMANBUD31physical
26344197
CPSF3_HUMANCPSF3physical
26344197
CRNL1_HUMANCRNKL1physical
26344197
PRP19_HUMANPRPF19physical
26344197
SF3A1_HUMANSF3A1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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.
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ISY1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222; SER-227 ANDSER-247, AND MASS SPECTROMETRY.

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