SARNP_HUMAN - dbPTM
SARNP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SARNP_HUMAN
UniProt AC P82979
Protein Name SAP domain-containing ribonucleoprotein
Gene Name SARNP
Organism Homo sapiens (Human).
Sequence Length 210
Subcellular Localization Nucleus. Nucleus speckle.
Protein Description Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production..
Protein Sequence MATETVELHKLKLAELKQECLARGLETKGIKQDLIHRLQAYLEEHAEEEANEEDVLGDETEEEETKPIELPVKEEEPPEKTVDVAAEKKVVKITSEIPQTERMQKRAERFNVPVSLESKKAARAARFGISSVPTKGLSSDNKPMVNLDKLKERAQRFGLNVSSISRKSEDDEKLKKRKERFGIVTSSAGTGTTEDTEAKKRKRAERFGIA
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------MATETVELH
------CCCCHHHHH		17.7222223895
102-HydroxyisobutyrylationTETVELHKLKLAELK
CCHHHHHHHHHHHHH		61.00-
10AcetylationTETVELHKLKLAELK
CCHHHHHHHHHHHHH		61.0023954790
10UbiquitinationTETVELHKLKLAELK
CCHHHHHHHHHHHHH		61.0021890473
10MalonylationTETVELHKLKLAELK
CCHHHHHHHHHHHHH		61.0032601280
122-HydroxyisobutyrylationTVELHKLKLAELKQE
HHHHHHHHHHHHHHH		50.91-
12MalonylationTVELHKLKLAELKQE
HHHHHHHHHHHHHHH		50.9126320211
17UbiquitinationKLKLAELKQECLARG
HHHHHHHHHHHHHCC		35.2432015554
17AcetylationKLKLAELKQECLARG
HHHHHHHHHHHHHCC		35.2425953088
20GlutathionylationLAELKQECLARGLET
HHHHHHHHHHCCCCC		3.1422555962
28MalonylationLARGLETKGIKQDLI
HHCCCCCCCHHHHHH		49.6226320211
28UbiquitinationLARGLETKGIKQDLI
HHCCCCCCCHHHHHH		49.6232015554
31AcetylationGLETKGIKQDLIHRL
CCCCCCHHHHHHHHH		46.5626051181
31UbiquitinationGLETKGIKQDLIHRL
CCCCCCHHHHHHHHH		46.5624816145
312-HydroxyisobutyrylationGLETKGIKQDLIHRL
CCCCCCHHHHHHHHH		46.56-
31SuccinylationGLETKGIKQDLIHRL
CCCCCCHHHHHHHHH		46.5623954790
60PhosphorylationEDVLGDETEEEETKP
CCCCCCCCCCCCCCC		54.1329507054
65PhosphorylationDETEEEETKPIELPV
CCCCCCCCCCCCCCC		45.4630576142
66SumoylationETEEEETKPIELPVK
CCCCCCCCCCCCCCC		47.48-
66SumoylationETEEEETKPIELPVK
CCCCCCCCCCCCCCC		47.48-
80UbiquitinationKEEEPPEKTVDVAAE
CCCCCCCCCCCHHHH		60.6733845483
81PhosphorylationEEEPPEKTVDVAAEK
CCCCCCCCCCHHHHH		21.9226074081
88UbiquitinationTVDVAAEKKVVKITS
CCCHHHHHCEEEEEC		46.2533845483
88AcetylationTVDVAAEKKVVKITS
CCCHHHHHCEEEEEC		46.2523749302
89UbiquitinationVDVAAEKKVVKITSE
CCHHHHHCEEEEECC		43.7122817900
92AcetylationAAEKKVVKITSEIPQ
HHHHCEEEEECCCCC		43.1626822725
92UbiquitinationAAEKKVVKITSEIPQ
HHHHCEEEEECCCCC		43.1622817900
100PhosphorylationITSEIPQTERMQKRA
EECCCCCHHHHHHHH		21.8728555341
115O-linked_GlycosylationERFNVPVSLESKKAA
HHHCCCCCHHHHHHH		21.9830620550
115PhosphorylationERFNVPVSLESKKAA
HHHCCCCCHHHHHHH		21.9825159151
118PhosphorylationNVPVSLESKKAARAA
CCCCCHHHHHHHHHH		44.7621815630
119UbiquitinationVPVSLESKKAARAAR
CCCCHHHHHHHHHHH		36.7432015554
1192-HydroxyisobutyrylationVPVSLESKKAARAAR
CCCCHHHHHHHHHHH		36.74-
119AcetylationVPVSLESKKAARAAR
CCCCHHHHHHHHHHH		36.7423749302
120AcetylationPVSLESKKAARAARF
CCCHHHHHHHHHHHH		57.4630586061
130PhosphorylationRAARFGISSVPTKGL
HHHHHCCCCCCCCCC		26.1828857561
131PhosphorylationAARFGISSVPTKGLS
HHHHCCCCCCCCCCC		30.1428857561
134PhosphorylationFGISSVPTKGLSSDN
HCCCCCCCCCCCCCC		35.2723186163
135AcetylationGISSVPTKGLSSDNK
CCCCCCCCCCCCCCC		52.3525953088
135UbiquitinationGISSVPTKGLSSDNK
CCCCCCCCCCCCCCC		52.3522817900
135MethylationGISSVPTKGLSSDNK
CCCCCCCCCCCCCCC		52.35-
138PhosphorylationSVPTKGLSSDNKPMV
CCCCCCCCCCCCCCC		44.2924247654
139PhosphorylationVPTKGLSSDNKPMVN
CCCCCCCCCCCCCCC		50.6925159151
142AcetylationKGLSSDNKPMVNLDK
CCCCCCCCCCCCHHH		39.2123954790
142UbiquitinationKGLSSDNKPMVNLDK
CCCCCCCCCCCCHHH		39.2124816145
144SulfoxidationLSSDNKPMVNLDKLK
CCCCCCCCCCHHHHH		3.1321406390
149AcetylationKPMVNLDKLKERAQR
CCCCCHHHHHHHHHH		65.7026822725
149UbiquitinationKPMVNLDKLKERAQR
CCCCCHHHHHHHHHH		65.7033845483
162PhosphorylationQRFGLNVSSISRKSE
HHHCCCHHHHCCCCC		22.3825159151
163PhosphorylationRFGLNVSSISRKSED
HHCCCHHHHCCCCCC		21.9423401153
165PhosphorylationGLNVSSISRKSEDDE
CCCHHHHCCCCCCHH		35.2921712546
168PhosphorylationVSSISRKSEDDEKLK
HHHHCCCCCCHHHHH		45.1821712546
173UbiquitinationRKSEDDEKLKKRKER
CCCCCHHHHHHHHHH		73.0224816145
185O-linked_GlycosylationKERFGIVTSSAGTGT
HHHHCEEECCCCCCC		18.2930620550
185PhosphorylationKERFGIVTSSAGTGT
HHHHCEEECCCCCCC		18.2928555341
186O-linked_GlycosylationERFGIVTSSAGTGTT
HHHCEEECCCCCCCC		13.8030620550
186PhosphorylationERFGIVTSSAGTGTT
HHHCEEECCCCCCCC		13.8028555341
187O-linked_GlycosylationRFGIVTSSAGTGTTE
HHCEEECCCCCCCCC		22.7330620550
187PhosphorylationRFGIVTSSAGTGTTE
HHCEEECCCCCCCCC		22.7325849741
190PhosphorylationIVTSSAGTGTTEDTE
EEECCCCCCCCCCHH		30.9521815630
192PhosphorylationTSSAGTGTTEDTEAK
ECCCCCCCCCCHHHH		27.1828555341
193PhosphorylationSSAGTGTTEDTEAKK
CCCCCCCCCCHHHHH		32.9628985074
196PhosphorylationGTGTTEDTEAKKRKR
CCCCCCCHHHHHHHH		31.4528985074
199AcetylationTTEDTEAKKRKRAER
CCCCHHHHHHHHHHH		47.0525953088
199UbiquitinationTTEDTEAKKRKRAER
CCCCHHHHHHHHHHH		47.0521906983
200UbiquitinationTEDTEAKKRKRAERF
CCCHHHHHHHHHHHH		70.9222817900
200AcetylationTEDTEAKKRKRAERF
CCCHHHHHHHHHHHH		70.9225953088
202UbiquitinationDTEAKKRKRAERFGI
CHHHHHHHHHHHHCC		65.9122817900
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 SARNP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SARNP_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 SARNP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FUS_HUMANFUSphysical
17196963
DX39A_HUMANDDX39Aphysical
17196963
VDAC3_HUMANVDAC3physical
22939629
SOSB1_HUMANNABP2physical
22939629
SRCAP_HUMANSRCAPphysical
22939629
TIM44_HUMANTIMM44physical
22939629
TAGL_HUMANTAGLNphysical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
UBL4A_HUMANUBL4Aphysical
22939629
SBDS_HUMANSBDSphysical
22939629
MPLKI_HUMANMPLKIPphysical
22939629
TBL2_HUMANTBL2physical
22939629
STX7_HUMANSTX7physical
22939629
SRPRB_HUMANSRPRBphysical
22939629
THY1_HUMANTHY1physical
22939629
SRRM2_HUMANSRRM2physical
22939629
TPX2_HUMANTPX2physical
22939629
THIK_HUMANACAA1physical
22939629
UBC9_HUMANUBE2Iphysical
22939629
UBE4B_HUMANUBE4Bphysical
22939629
TIAR_HUMANTIAL1physical
22939629
PLCG1_HUMANPLCG1physical
22863883
RIC8A_HUMANRIC8Aphysical
22863883
WDR61_HUMANWDR61physical
22863883
DX39A_HUMANDDX39Aphysical
15338056
ZC11A_HUMANZC3H11Aphysical
28514442
CCDC9_HUMANCCDC9physical
28514442
ZC3HE_HUMANZC3H14physical
28514442
UIF_HUMANFYTTD1physical
28514442
KBTB7_HUMANKBTBD7physical
28514442
ACINU_HUMANACIN1physical
28514442
CHTOP_HUMANCHTOPphysical
28514442
NCBP3_HUMANC17orf85physical
28514442
RNPS1_HUMANRNPS1physical
28514442
PPIG_HUMANPPIGphysical
28514442
PDIP3_HUMANPOLDIP3physical
28514442
MGN_HUMANMAGOHphysical
28514442
2ABD_HUMANPPP2R2Dphysical
28514442
PININ_HUMANPNNphysical
28514442
CRIP2_HUMANCRIP2physical
28514442
THOC5_HUMANTHOC5physical
28514442
THOC1_HUMANTHOC1physical
28514442
CPVL_HUMANCPVLphysical
28514442
IF4A3_HUMANEIF4A3physical
28514442
WIPI3_HUMANWDR45Bphysical
28514442
CHRD1_HUMANCHORDC1physical
27173435
SEPT7_HUMANSEPT7physical
27173435
PRCC_HUMANPRCCphysical
27173435
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 SARNP_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.
"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-142, AND MASS SPECTROMETRY.
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-163, AND MASSSPECTROMETRY.

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