Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Signal recognition particle 72 kDa protein  

UniProtKB / Swiss-Prot ID :  SRP72_HUMAN

Gene Name (Synonyms) : 
SRP72  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein Function :  Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. Binds the 7S RNA only in presence of SRP68. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function. 

Protein Sequence MASGGSGGVSVPALWSEVNRYGQNGDFTRALKTVNKILQINKDDVTALHCKVVCLIQNGSFKEALNVINT...
Predicted Secondary Structure CCCCCCHHHHHHHHHHHHHHHHHCHHHHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHHCCHHHHHHHHHH...
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
Predicted 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.---MASGGS
---CCCCCC
19.51UniProtKB
Link-
73Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NTHTKVLAN
HHHHHHCCC
27.87Phosphositeplus
Link-
84Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LSFEKAYCE
HHHHHHHHH
42.52Phosphositeplus
Link-
99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ENALKTIES
HHHHHHHHH
45.08Phosphositeplus
Link-
108PhosphothreonineANQQTDKLK
HHHHHHHHH
25.90HPRD
Link-
108PhosphothreonineANQQTDKLK
HHHHHHHHH
25.90Phosphositeplus
Link-
112Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TDKLKELYG
HHHHHHHHH
51.95Phosphositeplus
Link-
376Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AAEIKLTMA
HHHHHHHHH
29.43Phosphositeplus
Link-
383Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MAQLKISQG
HHHHHCCCC
28.38Phosphositeplus
Link-
391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GNISKACLI
CCHHHHHHH
39.04Phosphositeplus
Link-
475Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QQLWKQNPK
HHHHCCCHH
49.11Phosphositeplus
Link-
504Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KALSKHLPS
HHHHHCCCC
50.43Phosphositeplus
Link-
566PhosphotyrosineLPKNYDPKV
CCCCCCCCC
39.48HPRD
Link-
566PhosphotyrosineLPKNYDPKV
CCCCCCCCC
39.48PhosphoELM
Link-
566PhosphotyrosineLPKNYDPKV
CCCCCCCCC
39.48Phosphositeplus
Link-
566Phosphotyrosine.LPKNYDPKV
CCCCCCCCC
39.48UniProtKB
Link-
571PhosphothreonineDPKVTPDPE
CCCCCCCCC
28.27HPRD
Link-
571PhosphothreonineDPKVTPDPE
CCCCCCCCC
28.27PhosphoELM
Link-
571PhosphothreonineDPKVTPDPE
CCCCCCCCC
28.27Phosphositeplus
Link-
571Phosphothreonine.DPKVTPDPE
CCCCCCCCC
28.27UniProtKB
Link-
600Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DQIGKGTQG
CCCCCCCCC
61.49Phosphositeplus
Link-
610PhosphoserineTAGASSELD
CCCCCCHHH
24.35HPRD
Link-
611PhosphoserineAGASSELDA
CCCCCHHHH
41.46HPRD
Link-
616PhosphoserineELDASKTVS
HHHHHHHCC
28.64HPRD
Link-
618PhosphothreonineDASKTVSSP
HHHHHCCCC
24.11HPRD
Link-
618PhosphothreonineDASKTVSSP
HHHHHCCCC
24.11PhosphoELM
Link-
618PhosphothreonineDASKTVSSP
HHHHHCCCC
24.11Phosphositeplus
Link-
618Phosphothreonine.DASKTVSSP
HHHHHCCCC
24.11UniProtKB
Link-
620PhosphoserineSKTVSSPPT
HHHCCCCCC
42.21HPRD
Link-
620PhosphoserineSKTVSSPPT
HHHCCCCCC
42.21PhosphoELM
Link-
620PhosphoserineSKTVSSPPT
HHHCCCCCC
42.21Phosphositeplus
Link-
620Phosphoserine.SKTVSSPPT
HHHCCCCCC
42.21UniProtKB
Link-
621PhosphoserineKTVSSPPTS
HHCCCCCCC
30.48HPRD
Link-
621PhosphoserineKTVSSPPTS
HHCCCCCCC
30.48PhosphoELM
Link-
621PhosphoserineKTVSSPPTS
HHCCCCCCC
30.48Phosphositeplus
Link-
621Phosphoserine.KTVSSPPTS
HHCCCCCCC
30.48UniProtKB
Link-
624PhosphothreonineSSPPTSPRP
CCCCCCCCC
55.54HPRD
Link-
624PhosphothreonineSSPPTSPRP
CCCCCCCCC
55.54PhosphoELM
Link-
624PhosphothreonineSSPPTSPRP
CCCCCCCCC
55.54Phosphositeplus
Link-
625PhosphoserineSPPTSPRPG
CCCCCCCCC
25.37HPRD
Link-
625PhosphoserineSPPTSPRPG
CCCCCCCCC
25.37PhosphoELM
Link-
625PhosphoserineSPPTSPRPG
CCCCCCCCC
25.37Phosphositeplus
Link-
630PhosphoserinePRPGSAATV
CCCCCCCCC
19.88HPRD
Link-
630PhosphoserinePRPGSAATV
CCCCCCCCC
19.88PhosphoELM
Link-
630PhosphoserinePRPGSAATV
CCCCCCCCC
19.88Phosphositeplus
Link-
633PhosphothreonineGSAATVSAS
CCCCCCCCC
18.08HPRD
Link-
633PhosphothreonineGSAATVSAS
CCCCCCCCC
18.08PhosphoELM
Link-
633PhosphothreonineGSAATVSAS
CCCCCCCCC
18.08Phosphositeplus
Link-
635PhosphoserineAATVSASTS
CCCCCCCCC
16.49HPRD
Link-
635PhosphoserineAATVSASTS
CCCCCCCCC
16.49PhosphoELM
Link-
637PhosphoserineTVSASTSNI
CCCCCCCCC
25.51HPRD
Link-
637PhosphoserineTVSASTSNI
CCCCCCCCC
25.51PhosphoELM
Link-
639PhosphoserineSASTSNIIP
CCCCCCCCC
24.44HPRD
Link-
639PhosphoserineSASTSNIIP
CCCCCCCCC
24.44PhosphoELM
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SKIL_HUMANphysical interactionMINT-61670MINT15231748
CASP3_HUMANin vitroHPRD:03671HPRD9857079
SRP54_HUMANENSP00000342181STRING
SRP14_HUMANENSP00000342181STRING
UCN2_HUMANENSP00000342181STRING
SRP19_HUMANENSP00000342181STRING
SRP09_HUMANENSP00000342181STRING
SRP68_HUMANENSP00000342181STRING
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Disease Reference
Kegg disease
OMIM disease
614675Bone marrow failure syndrome 1 (BMFS1)
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571, 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 TYR-566; THR-571; THR-618AND SER-620, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-618 AND SER-620, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-618, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures