Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Sjoegren syndrome/scleroderma autoantigen 1  

UniProtKB / Swiss-Prot ID :  SSA27_HUMAN

Gene Name (Synonyms) : 
SSSCA1  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Might play a role in mitosis. Antigenic molecule. Could be a centromere-associated protein. May induce anti-centromere antibodies. 

Protein Sequence MALNGAEVDDFSWEPPTEAETKVLQARRERQDRISRLMGDYLLRGYRMLGETCADCGTILLQDKQRKIYC...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHHEEEECCCCEEEE...
Protein Variant
LocationDescription
21T -> M (in dbSNP:rs35971725). VAR_051383
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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
2N-acetylalanine.---MALNGA
---CCCCCC
15.10UniProtKB
Link-
22Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EAETKVLQA
HHHHHHHHH
32.24Phosphositeplus
Link-
81Caspase cleavage aspartic acidDSDVDKDNP
HHHCCCCCC
58.54Phosphositeplus
Link-
82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SDVDKDNPA
HHCCCCCCC
60.29Phosphositeplus
Link-
94PhosphoserineQAALSQARE
HHHHHHHHH
19.64HPRD
Link-
94PhosphoserineQAALSQARE
HHHHHHHHH
19.64PhosphoELM
Link-
94PhosphoserineQAALSQARE
HHHHHHHHH
19.64Phosphositeplus
Link-
94Phosphoserine.QAALSQARE
HHHHHHHHH
19.64UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SSA27_HUMANphysical interactionMINT-67276MINT16189514
Q5SZY0_HUMANphysical interactionMINT-67308MINT16189514
Q8N7U5_HUMANphysical interactionMINT-66327MINT16189514
NOC4L_HUMANphysical interactionMINT-67757MINT16189514
CCD33_HUMANphysical interactionMINT-66941MINT16189514
VTA1_HUMANphysical interactionMINT-67386MINT16189514
SSA27_HUMANphysical interactionEBI-756523
intact16189514
CCD33_HUMANphysical interactionEBI-755422
intact16189514
Q8N374_HUMANphysical interactionEBI-753862
intact16189514
TPC6A_HUMANphysical interactionEBI-755716
intact16189514
NOC4L_HUMANphysical interactionEBI-758122
intact16189514
AL2SA_HUMANphysical interactionEBI-753430
intact16189514
CT195_HUMANphysical interactionEBI-754267
intact16189514
VTA1_HUMANphysical interactionEBI-756895
intact16189514
TCPE_HUMANphysical interactionEBI-758803
intact16189514
DOK2_HUMANphysical interactionEBI-1061286
intact17353931
HNRPL_HUMANphysical interactionEBI-1075029
intact17353931
DSG1_HUMANphysical interactionEBI-1084743
intact17353931
ANM1_HUMANphysical interactionEBI-1085531
intact17353931
LRRC7_HUMANphysical interactionEBI-1081720
intact17353931
OAT_HUMANphysical interactionEBI-1077120
intact17353931
Q65ZQ1_HUMANphysical interactionEBI-1078682
intact17353931
IF3EI_HUMANphysical interactionEBI-1078768
intact17353931
DESP_HUMANphysical interactionEBI-1081188
intact17353931
DCD_HUMANphysical interactionEBI-1080125
intact17353931
QRIC2_HUMANphysical interactionEBI-1077857
intact17353931
RUVB2_HUMANphysical interactionEBI-1079930
intact17353931
TCPH_HUMANin vivoHPRD:06921HPRD11591653
SSA27_HUMANin vivo
yeast 2-hybrid
HPRD:06921HPRD11591653
16189514
AL2SA_HUMANyeast 2-hybridHPRD:06921HPRD16189514
TCPG_HUMANyeast 2-hybridHPRD:06921HPRD16189514
CCNH_HUMANyeast 2-hybridHPRD:06921HPRD16189514
VTA1_HUMANyeast 2-hybridHPRD:06921HPRD16189514
TPC6A_HUMANyeast 2-hybridHPRD:06921HPRD16189514
NOC4L_HUMANyeast 2-hybridHPRD:06921HPRD16189514
CT195_HUMANyeast 2-hybridHPRD:06921HPRD16189514
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Disease Reference
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.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures