U2AFM_HUMAN - dbPTM
U2AFM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID U2AFM_HUMAN
UniProt AC Q15696
Protein Name U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
Gene Name ZRSR2
Organism Homo sapiens (Human).
Sequence Length 482
Subcellular Localization Nucleus .
Protein Description Pre-mRNA-binding protein required for splicing of both U2- and U12-type introns. Selectively interacts with the 3'-splice site of U2- and U12-type pre-mRNAs and promotes different steps in U2 and U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent manner and is required for assembly of the prespliceosome, a precursor to other spliceosomal complexes. For U2-type introns, it is selectively and specifically required for the second step of splicing..
Protein Sequence MAAPEKMTFPEKPSHKKYRAALKKEKRKKRRQELARLRDSGLSQKEEEEDTFIEEQQLEEEKLLERERQRLHEEWLLREQKAQEEFRIKKEKEEAAKKRQEEQERKLKEQWEEQQRKEREEEEQKRQEKKEKEEALQKMLDQAENELENGTTWQNPEPPVDFRVMEKDRANCPFYSKTGACRFGDRCSRKHNFPTSSPTLLIKSMFTTFGMEQCRRDDYDPDASLEYSEEETYQQFLDFYEDVLPEFKNVGKVIQFKVSCNLEPHLRGNVYVQYQSEEECQAALSLFNGRWYAGRQLQCEFCPVTRWKMAICGLFEIQQCPRGKHCNFLHVFRNPNNEFWEANRDIYLSPDRTGSSFGKNSERRERMGHHDDYYSRLRGRRNPSPDHSYKRNGESERKSSRHRGKKSHKRTSKSRERHNSRSRGRNRDRSRDRSRGRGSRSRSRSRSRRSRRSRSQSSSRSRSRGRRRSGNRDRTVQSPKSK
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
40PhosphorylationELARLRDSGLSQKEE
HHHHHHHCCCCHHHH		34.8928348404
43PhosphorylationRLRDSGLSQKEEEED
HHHHCCCCHHHHHHC		42.6128348404
45SumoylationRDSGLSQKEEEEDTF
HHCCCCHHHHHHCCH		64.8128112733
51PhosphorylationQKEEEEDTFIEEQQL
HHHHHHCCHHHHHHH		29.7730257219
62UbiquitinationEQQLEEEKLLERERQ
HHHHHHHHHHHHHHH		62.7529967540
62SumoylationEQQLEEEKLLERERQ
HHHHHHHHHHHHHHH		62.7528112733
66UbiquitinationEEEKLLERERQRLHE
HHHHHHHHHHHHHHH		44.3524816145
92UbiquitinationEFRIKKEKEEAAKKR
HHHHHHHHHHHHHHH		70.5024816145
130UbiquitinationEQKRQEKKEKEEALQ
HHHHHHHHHHHHHHH		73.58-
132UbiquitinationKRQEKKEKEEALQKM
HHHHHHHHHHHHHHH		70.50-
138UbiquitinationEKEEALQKMLDQAEN
HHHHHHHHHHHHHHH		42.13-
177UbiquitinationANCPFYSKTGACRFG
CCCCCCCCCCCCCCC		39.33-
207PhosphorylationLLIKSMFTTFGMEQC
EHHHHHHHHHCHHHH		16.75-
252UbiquitinationPEFKNVGKVIQFKVS
HHHCCCCCEEEEEEE		31.7029967540
347PhosphorylationWEANRDIYLSPDRTG
HHHCCCEEECCCCCC		12.8622167270
349PhosphorylationANRDIYLSPDRTGSS
HCCCEEECCCCCCCC		14.0519664994
353PhosphorylationIYLSPDRTGSSFGKN
EEECCCCCCCCCCCC		49.1223927012
355PhosphorylationLSPDRTGSSFGKNSE
ECCCCCCCCCCCCHH		23.1423927012
356PhosphorylationSPDRTGSSFGKNSER
CCCCCCCCCCCCHHH		39.0923927012
361PhosphorylationGSSFGKNSERRERMG
CCCCCCCHHHHHHHC		35.6528555341
374PhosphorylationMGHHDDYYSRLRGRR
HCCCHHHHHHHCCCC		8.36-
384PhosphorylationLRGRRNPSPDHSYKR
HCCCCCCCCCCCCCC		46.6521955146
388PhosphorylationRNPSPDHSYKRNGES
CCCCCCCCCCCCCCC		39.4623403867
389PhosphorylationNPSPDHSYKRNGESE
CCCCCCCCCCCCCCC		15.5623403867
420PhosphorylationKSRERHNSRSRGRNR
HHHHHHHHHHCCCCC		26.0526270265
430PhosphorylationRGRNRDRSRDRSRGR
CCCCCCHHHHHCCCC		42.7020068231
434PhosphorylationRDRSRDRSRGRGSRS
CCHHHHHCCCCCCHH		43.2920068231
439PhosphorylationDRSRGRGSRSRSRSR
HHCCCCCCHHHHHHH		26.2320068231
441PhosphorylationSRGRGSRSRSRSRSR
CCCCCCHHHHHHHHH		35.9820068231
457PhosphorylationSRRSRSQSSSRSRSR
HHHHHHHHHHHHHHH		31.3724260401
458PhosphorylationRRSRSQSSSRSRSRG
HHHHHHHHHHHHHHC		23.3324260401
475PhosphorylationRSGNRDRTVQSPKSK
CCCCCCCCCCCCCCC		27.4726546556
478PhosphorylationNRDRTVQSPKSK---
CCCCCCCCCCCC---		29.9324719451
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 U2AFM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of U2AFM_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 U2AFM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SDCB2_HUMANSDCBP2physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
RL26L_HUMANRPL26L1physical
26186194
PDCD7_HUMANPDCD7physical
26186194
SF3B1_HUMANSF3B1physical
26186194
SPF45_HUMANRBM17physical
26186194
SF3B2_HUMANSF3B2physical
26186194
C1QBP_HUMANC1QBPphysical
26186194
SRPK1_HUMANSRPK1physical
26186194
SRPK2_HUMANSRPK2physical
26186194
RL10A_HUMANRPL10Aphysical
26186194
U1SBP_HUMANSNRNP35physical
26186194
NADAP_HUMANSLC4A1APphysical
26186194
SF3A1_HUMANSF3A1physical
26186194
CD11B_HUMANCDK11Bphysical
26186194
ZCRB1_HUMANZCRB1physical
26186194
CH033_HUMANC8orf33physical
26186194
NOG1_HUMANGTPBP4physical
26186194
CCD97_HUMANCCDC97physical
26186194
RBM5_HUMANRBM5physical
26186194
SNR48_HUMANSNRNP48physical
26186194
SNUT1_HUMANSART1physical
26186194
RBM40_HUMANRNPC3physical
26186194
TTC33_HUMANTTC33physical
26186194
SF3A3_HUMANSF3A3physical
26186194
CHERP_HUMANCHERPphysical
26186194
RL15_HUMANRPL15physical
26186194
JMJD6_HUMANJMJD6physical
26186194
SR140_HUMANU2SURPphysical
26186194
GPT11_HUMANGPATCH11physical
26186194
HUTH_HUMANHALphysical
26186194
SPB8_HUMANSERPINB8physical
26186194
ADIP_HUMANSSX2IPphysical
26186194
NKTR_HUMANNKTRphysical
26186194
SPT2_HUMANSPTY2D1physical
26186194
ZMAT5_HUMANZMAT5physical
26186194
TRPM3_HUMANTRPM3physical
26186194
U1SBP_HUMANSNRNP35physical
28514442
RBM40_HUMANRNPC3physical
28514442
SNR48_HUMANSNRNP48physical
28514442
PDCD7_HUMANPDCD7physical
28514442
ADIP_HUMANSSX2IPphysical
28514442
ZMAT5_HUMANZMAT5physical
28514442
NKTR_HUMANNKTRphysical
28514442
RBM5_HUMANRBM5physical
28514442
CD11B_HUMANCDK11Bphysical
28514442
CHERP_HUMANCHERPphysical
28514442
TTC33_HUMANTTC33physical
28514442
SF3B1_HUMANSF3B1physical
28514442
NADAP_HUMANSLC4A1APphysical
28514442
JMJD6_HUMANJMJD6physical
28514442
SF3A3_HUMANSF3A3physical
28514442
GPT11_HUMANGPATCH11physical
28514442
SPB8_HUMANSERPINB8physical
28514442
SRPK1_HUMANSRPK1physical
28514442
RL26L_HUMANRPL26L1physical
28514442
SPF45_HUMANRBM17physical
28514442
SR140_HUMANU2SURPphysical
28514442
HUTH_HUMANHALphysical
28514442
TRPM3_HUMANTRPM3physical
28514442
SF3A1_HUMANSF3A1physical
28514442
SF3B2_HUMANSF3B2physical
28514442
C1QBP_HUMANC1QBPphysical
28514442
RL5_HUMANRPL5physical
28514442
SPT2_HUMANSPTY2D1physical
28514442
SRPK2_HUMANSRPK2physical
28514442
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 U2AFM_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-384, ANDMASS SPECTROMETRY.

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