Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Spindlin-1  

UniProtKB / Swiss-Prot ID :  SPIN1_HUMAN

Gene Name (Synonyms) : 
SPIN1, OCR, SPIN  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. 

Protein Function :  May play a role in cell-cycle regulation during the transition from gamete to embryo (By similarity). 

Protein Sequence MKTPFGKTPGQRSRADAGHAGVSANMMKKRTSHKKHRSSVGPSKPVSQPRRNIVGCRIQHGWKEGNGPVT...
Predicted Secondary Structure CCCCCCCCCCHHHHCCCCCCCCEEEEEECHHHHHHHHCCCCCCCCCCCCCCCEEEEEEECCEECCCCCCE...
Protein Variant
LocationDescription
221A -> P (in dbSNP:rs34794905). VAR_053690
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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
Predicted PTM Sites
Protein Variant
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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
7N6-acetyllysineTPFGKTPGQ
CCCCCCCCH
52.50HPRD
Link-
7N6-acetyllysineTPFGKTPGQ
CCCCCCCCH
52.50Phosphositeplus
Link-
7N6-acetyllysine.TPFGKTPGQ
CCCCCCCCH
52.50UniProtKB
Link-
13PhosphoserinePGQRSRADA
CCHHHHCCC
24.75HPRD
Link-
38PhosphoserineKKHRSSVGP
HHHHCCCCC
29.15HPRD
Link-
38PhosphoserineKKHRSSVGP
HHHHCCCCC
29.15PhosphoELM
Link-
38PhosphoserineKKHRSSVGP
HHHHCCCCC
29.15Phosphositeplus
Link-
38Phosphoserine.KKHRSSVGP
HHHHCCCCC
29.15UniProtKB
Link-
39PhosphoserineKHRSSVGPS
HHHCCCCCC
30.93HPRD
Link-
39PhosphoserineKHRSSVGPS
HHHCCCCCC
30.93PhosphoELM
Link-
39PhosphoserineKHRSSVGPS
HHHCCCCCC
30.93Phosphositeplus
Link-
39Phosphoserine.KHRSSVGPS
HHHCCCCCC
30.93UniProtKB
Link-
43PhosphoserineSVGPSKPVS
CCCCCCCCC
43.60HPRD
Link-
63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QHGWKEGNG
ECCEECCCC
61.41Phosphositeplus
Link
91PhosphotyrosineYLIKYDGFD
EEEEECCCE
17.82Phosphositeplus
Link
91Phosphotyrosine.YLIKYDGFD
EEEEECCCE
17.82UniProtKB
Link
98PhosphotyrosineFDCVYGLEL
CEEEEEEEE
23.48Phosphositeplus
Link
98Phosphotyrosine.FDCVYGLEL
CEEEEEEEE
23.48UniProtKB
Link
109PhosphoserineDERVSALEV
CCCEEEEEE
33.10Phosphositeplus
Link
120PhosphothreonineDRVATSRIS
CCCCCCCCC
18.71Phosphositeplus
Link
121PhosphoserineRVATSRISD
CCCCCCCCH
20.20HPRD
Link
124PhosphoserineTSRISDAHL
CCCCCHHHH
27.86HPRD
Link
124PhosphoserineTSRISDAHL
CCCCCHHHH
27.86PhosphoELM
Link
124PhosphoserineTSRISDAHL
CCCCCHHHH
27.86Phosphositeplus
Link
124PhosphoserineTSRISDAHL
CCCCCHHHH
27.86SysPTM
Link
124Phosphoserine.TSRISDAHL
CCCCCHHHH
27.86UniProtKB
Link
196PhosphoserineIMPDSNDSP
ECCCCCCCC
36.34HPRD
Link-
199PhosphoserineDSNDSPPAE
CCCCCCCCC
36.71HPRD
Link-
199PhosphoserineDSNDSPPAE
CCCCCCCCC
36.71PhosphoELM
Link-
199PhosphoserineDSNDSPPAE
CCCCCCCCC
36.71Phosphositeplus
Link-
199PhosphoserineDSNDSPPAE
CCCCCCCCC
36.71SysPTM
Link-
199Phosphoserine.DSNDSPPAE
CCCCCCCCC
36.71UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PTN_HUMANphysical interactionEBI-737696
intact16169070
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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
"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-7, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-91 AND TYR-98, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-39, AND MASSSPECTROMETRY.
"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-124 AND SER-199, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures