SPF27_HUMAN - dbPTM
SPF27_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPF27_HUMAN
UniProt AC O75934
Protein Name Pre-mRNA-splicing factor SPF27
Gene Name BCAS2
Organism Homo sapiens (Human).
Sequence Length 225
Subcellular Localization Nucleus, nucleolus .
Protein Description Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR)..
Protein Sequence MAGTGLVAGEVVVDALPYFDQGYEAPGVREAAAALVEEETRRYRPTKNYLSYLTAPDYSAFETDIMRNEFERLAARQPIELLSMKRYELPAPSSGQKNDITAWQECVNNSMAQLEHQAVRIENLELMSQHGCNAWKVYNENLVHMIEHAQKELQKLRKHIQDLNWQRKNMQLTAGSKLREMESNWVSLVSKNYEIERTIVQLENEIYQIKQQHGEANKENIRQDF
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
2Acetylation------MAGTGLVAG
------CCCCCCCCC		25.0122814378
4Phosphorylation----MAGTGLVAGEV
----CCCCCCCCCEE		20.1518491316
23PhosphorylationLPYFDQGYEAPGVRE
CCCCCCCCCCCCHHH		11.86-
47AcetylationTRRYRPTKNYLSYLT
HHHHCCCCCHHHHHC		46.4026051181
47UbiquitinationTRRYRPTKNYLSYLT
HHHHCCCCCHHHHHC		46.40-
59PhosphorylationYLTAPDYSAFETDIM
HHCCCCCCHHHHHHH		33.58-
83PhosphorylationRQPIELLSMKRYELP
CCCHHHHHCEEEECC		34.5820068231
85UbiquitinationPIELLSMKRYELPAP
CHHHHHCEEEECCCC		48.75-
87PhosphorylationELLSMKRYELPAPSS
HHHHCEEEECCCCCC		19.1228796482
93PhosphorylationRYELPAPSSGQKNDI
EEECCCCCCCCCCCH		49.5620068231
94PhosphorylationYELPAPSSGQKNDIT
EECCCCCCCCCCCHH		44.1525159151
97UbiquitinationPAPSSGQKNDITAWQ
CCCCCCCCCCHHHHH		61.18-
136UbiquitinationQHGCNAWKVYNENLV
HCCCCCHHHHHHHHH		32.22-
136AcetylationQHGCNAWKVYNENLV
HCCCCCHHHHHHHHH		32.2225953088
151AcetylationHMIEHAQKELQKLRK
HHHHHHHHHHHHHHH		62.2627452117
158AcetylationKELQKLRKHIQDLNW
HHHHHHHHHHHHHHH		56.3427452117
158UbiquitinationKELQKLRKHIQDLNW
HHHHHHHHHHHHHHH		56.34-
168UbiquitinationQDLNWQRKNMQLTAG
HHHHHHHHHCCCCCC		41.49-
173PhosphorylationQRKNMQLTAGSKLRE
HHHHCCCCCCHHHHH		16.4521406692
176PhosphorylationNMQLTAGSKLREMES
HCCCCCCHHHHHHHH		26.5021406692
177AcetylationMQLTAGSKLREMESN
CCCCCCHHHHHHHHH		51.1225953088
177UbiquitinationMQLTAGSKLREMESN
CCCCCCHHHHHHHHH		51.12-
183PhosphorylationSKLREMESNWVSLVS
HHHHHHHHHHHHHHH		34.3824260401
187PhosphorylationEMESNWVSLVSKNYE
HHHHHHHHHHHCCCE		18.0529759185
190PhosphorylationSNWVSLVSKNYEIER
HHHHHHHHCCCEEEE		22.0729759185
191UbiquitinationNWVSLVSKNYEIERT
HHHHHHHCCCEEEEE		56.95-
193PhosphorylationVSLVSKNYEIERTIV
HHHHHCCCEEEEEEE		23.2425219547
198PhosphorylationKNYEIERTIVQLENE
CCCEEEEEEEHHHHH		16.8327174698
207PhosphorylationVQLENEIYQIKQQHG
EHHHHHHHHHHHHHC		9.6725219547
210UbiquitinationENEIYQIKQQHGEAN
HHHHHHHHHHHCHHC		28.5121906983
218UbiquitinationQQHGEANKENIRQDF
HHHCHHCHHHHHHCC		60.22-
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 SPF27_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPF27_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 SPF27_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRP19_HUMANPRPF19physical
21536736
CDC5L_HUMANCDC5Lphysical
21536736
PLRG1_HUMANPLRG1physical
21536736
U2AF2_HUMANU2AF2physical
21536736
PRP19_HUMANPRPF19physical
20176811
CDC5L_HUMANCDC5Lphysical
20176811
HSP7C_HUMANHSPA8physical
20176811
CTBL1_HUMANCTNNBL1physical
20176811
PLRG1_HUMANPLRG1physical
20176811
CWC15_HUMANCWC15physical
20176811
U520_HUMANSNRNP200physical
22939629
U5S1_HUMANEFTUD2physical
22939629
U2AF1_HUMANU2AF1physical
22939629
TRIO_HUMANTRIOphysical
22939629
VASN_HUMANVASNphysical
22939629
TFPI1_HUMANTFPIphysical
22939629
SF3B4_HUMANSF3B4physical
22365833
SF01_HUMANSF1physical
22365833
PRP8_HUMANPRPF8physical
22365833
PRP19_HUMANPRPF19physical
22365833
CDC5L_HUMANCDC5Lphysical
22365833
ESR1_HUMANESR1physical
15694360
ESR2_HUMANESR2physical
15694360
TRXR2_HUMANTXNRD2physical
15694360
PRGR_HUMANPGRphysical
15694360
PPARG_HUMANPPARGphysical
15694360
EP300_HUMANEP300physical
21988832
POTE1_HUMANPOT1physical
21988832
IKZF3_HUMANIKZF3physical
25416956
K1C40_HUMANKRT40physical
25416956
PSMD3_HUMANPSMD3physical
26344197
RS10_HUMANRPS10physical
26344197
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 SPF27_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

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