Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  SAP domain-containing ribonucleoprotein  

UniProtKB / Swiss-Prot ID :  SARNP_HUMAN

Gene Name (Synonyms) : 
SARNP, HCC1 HSPC316  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  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. 

Protein Sequence MATETVELHKLKLAELKQECLARGLETKGIKQDLIHRLQAYLEEHAEEEANEEDVLGDETEEEETKPIEL...
Predicted Secondary Structure  -
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATETV
---
17.72UniProtKB
Link-
92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KKVVKITSE
43.16Phosphositeplus
Link-
115PhosphoserineNVPVSLESK
21.98HPRD
Link-
115PhosphoserineNVPVSLESK
21.98Phosphositeplus
Link-
135Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SVPTKGLSS
52.35Phosphositeplus
Link-
142N6-acetyllysineSSDNKPMVN
39.21HPRD
Link-
142N6-acetyllysineSSDNKPMVN
39.21Phosphositeplus
Link-
142N6-acetyllysine.SSDNKPMVN
39.21UniProtKB
Link-
162PhosphoserineGLNVSSISR
22.38HPRD
Link-
162PhosphoserineGLNVSSISR
22.38PhosphoELM
Link-
163PhosphoserineLNVSSISRK
21.94HPRD
Link-
163PhosphoserineLNVSSISRK
21.94Phosphositeplus
Link-
163PhosphoserineLNVSSISRK
21.94SysPTM
Link-
163Phosphoserine.LNVSSISRK
21.94UniProtKB
Link-
199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DTEAKKRKR
47.05Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures