SUN1_MOUSE - dbPTM
SUN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUN1_MOUSE
UniProt AC Q9D666
Protein Name SUN domain-containing protein 1
Gene Name Sun1
Organism Mus musculus (Mouse).
Sequence Length 913
Subcellular Localization Nucleus inner membrane
Single-pass type II membrane protein . At oocyte MI stage localized around the spindle, at MII stage localized to the spindle poles. In round spermatids mainly localizes to the posterior pole of the nucleus. This localization
Protein Description As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Required for interkinetic nuclear migration (INM) and essential for nucleokinesis and centrosome-nucleus coupling during radial neuronal migration in the cerebral cortex and during glial migration. Involved in telomere attachment to nuclear envelope in the prophase of meiosis implicating a SUN1/2:KASH5 LINC complex in which SUN1 and SUN2 seem to act at least partial redundantly. Required for gametogenesis and involved in selective gene expression of coding and non-coding RNAs needed for gametogenesis. Helps to define the distribution of nuclear pore complexes (NPCs). Required for efficient localization of SYNE4 in the nuclear envelope.; Isoform 5 may be involved in nuclear remodeling during sperm head formation in spermatogenenis. A probable SUN1 isoform 5:SYNE3 LINC complex may tether spermatid nuclei to anterior cytoskeletal structures such as actin filaments present at membraneous junctions of spermatids and Sertoli cells..
Protein Sequence MDFSRLHTYTPPQCVPENTGYTYALSSSYSSDALDFETEHKLEPVFDSPRMSRRSLRLVTTASYSSGDSQAIDSHISTSRATPAKGRETRTVKQRRSASKPAFSINHLSGKGLSSSTSHDSSCSLRSATVLRHPVLDESLIREQTKVDHFWGLDDDGDLKGGNKAATQGNGELAAEVASSNGYTCRDCRMLSARTDALTAHSAIHGTTSRVYSRDRTLKPRGVSFYLDRTLWLAKSTSSSFASFIVQLFQVVLMKLNFETYKLKGYESRAYESQSYETKSHESEAHLGHCGRMTAGELSRVDGESLCDDCKGKKHLEIHTATHSQLPQPHRVAGAMGRLCIYTGDLLVQALRRTRAAGWSVAEAVWSVLWLAVSAPGKAASGTFWWLGSGWYQFVTLISWLNVFLLTRCLRNICKVFVLLLPLLLLLGAGVSLWGQGNFFSLLPVLNWTAMQPTQRVDDSKGMHRPGPLPPSPPPKVDHKASQWPQESDMGQKVASLSAQCHNHDERLAELTVLLQKLQIRVDQVDDGREGLSLWVKNVVGQHLQEMGTIEPPDAKTDFMTFHHDHEVRLSNLEDVLRKLTEKSEAIQKELEETKLKAGSRDEEQPLLDRVQHLELELNLLKSQLSDWQHLKTSCEQAGARIQETVQLMFSEDQQGGSLEWLLEKLSSRFVSKDELQVLLHDLELKLLQNITHHITVTGQAPTSEAIVSAVNQAGISGITEAQAHIIVNNALKLYSQDKTGMVDFALESGGGSILSTRCSETYETKTALLSLFGVPLWYFSQSPRVVIQPDIYPGNCWAFKGSQGYLVVRLSMKIYPTTFTMEHIPKTLSPTGNISSAPKDFAVYGLETEYQEEGQPLGRFTYDQEGDSLQMFHTLERPDQAFQIVELRVLSNWGHPEYTCLYRFRVHGEPIQ
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
48PhosphorylationKLEPVFDSPRMSRRS
CCCCCCCCCCCCHHH		11.7127180971
52PhosphorylationVFDSPRMSRRSLRLV
CCCCCCCCHHHEEEE		26.3122817900
60PhosphorylationRRSLRLVTTASYSSG
HHHEEEEEEEECCCC		22.6425293948
61PhosphorylationRSLRLVTTASYSSGD
HHEEEEEEEECCCCC		13.2125293948
63PhosphorylationLRLVTTASYSSGDSQ
EEEEEEEECCCCCCH		24.3726643407
64PhosphorylationRLVTTASYSSGDSQA
EEEEEEECCCCCCHH		12.3726643407
65PhosphorylationLVTTASYSSGDSQAI
EEEEEECCCCCCHHH		25.9126643407
66PhosphorylationVTTASYSSGDSQAID
EEEEECCCCCCHHHH		38.0826643407
69PhosphorylationASYSSGDSQAIDSHI
EECCCCCCHHHHHHC		25.6626643407
74PhosphorylationGDSQAIDSHISTSRA
CCCHHHHHHCCCCCC		19.3326643407
77PhosphorylationQAIDSHISTSRATPA
HHHHHHCCCCCCCCC		18.2023984901
78PhosphorylationAIDSHISTSRATPAK
HHHHHCCCCCCCCCC		22.9423984901
79PhosphorylationIDSHISTSRATPAKG
HHHHCCCCCCCCCCC		17.0926643407
82PhosphorylationHISTSRATPAKGRET
HCCCCCCCCCCCCCC		23.7526643407
89PhosphorylationTPAKGRETRTVKQRR
CCCCCCCCCHHHHHH		30.2223140645
91PhosphorylationAKGRETRTVKQRRSA
CCCCCCCHHHHHHHC		39.2023140645
97PhosphorylationRTVKQRRSASKPAFS
CHHHHHHHCCCCCEE		38.8025619855
99PhosphorylationVKQRRSASKPAFSIN
HHHHHHCCCCCEEEE		40.1826824392
104PhosphorylationSASKPAFSINHLSGK
HCCCCCEEEECCCCC		25.2925619855
109PhosphorylationAFSINHLSGKGLSSS
CEEEECCCCCCCCCC		30.7929514104
114PhosphorylationHLSGKGLSSSTSHDS
CCCCCCCCCCCCCCC		30.8029514104
115PhosphorylationLSGKGLSSSTSHDSS
CCCCCCCCCCCCCCC		42.5530635358
116PhosphorylationSGKGLSSSTSHDSSC
CCCCCCCCCCCCCCC		30.4728418008
117PhosphorylationGKGLSSSTSHDSSCS
CCCCCCCCCCCCCCC		31.8430635358
118PhosphorylationKGLSSSTSHDSSCSL
CCCCCCCCCCCCCCC		27.5221183079
121PhosphorylationSSSTSHDSSCSLRSA
CCCCCCCCCCCCCCC		28.0224719451
122PhosphorylationSSTSHDSSCSLRSAT
CCCCCCCCCCCCCCC		17.4930635358
124PhosphorylationTSHDSSCSLRSATVL
CCCCCCCCCCCCCHH		28.8521183079
139PhosphorylationRHPVLDESLIREQTK
CCCCCCHHHHCCHHC		28.8526824392
160UbiquitinationLDDDGDLKGGNKAAT
CCCCCCCCCCCCCCC		70.3022790023
160UbiquitinationLDDDGDLKGGNKAAT
CCCCCCCCCCCCCCC		70.30-
202PhosphorylationTDALTAHSAIHGTTS
CCHHHHHHHHHCCCC		26.8429514104
221UbiquitinationRDRTLKPRGVSFYLD
CCCCCCCCCEEEEEE		57.4627667366
224PhosphorylationTLKPRGVSFYLDRTL
CCCCCCEEEEEECEE		15.8222006019
262UbiquitinationKLNFETYKLKGYESR
HCCCCEEECCCCHHC		51.6627667366
266PhosphorylationETYKLKGYESRAYES
CEEECCCCHHCCCCC		14.7828576409
271UbiquitinationKGYESRAYESQSYET
CCCHHCCCCCCCCCC		18.2727667366
280UbiquitinationSQSYETKSHESEAHL
CCCCCCCCCCCCHHC		39.6527667366
283PhosphorylationYETKSHESEAHLGHC
CCCCCCCCCHHCCCC		34.3628418008
291UbiquitinationEAHLGHCGRMTAGEL
CHHCCCCCCCCCHHH		19.4027667366
300UbiquitinationMTAGELSRVDGESLC
CCCHHHCCCCCCCCC		43.0727667366
305PhosphorylationLSRVDGESLCDDCKG
HCCCCCCCCCCCCCC		39.5727566939
472PhosphorylationRPGPLPPSPPPKVDH
CCCCCCCCCCCCCCC		48.3628066266
512PhosphorylationDERLAELTVLLQKLQ
HHHHHHHHHHHHHHC		10.7021659604
517UbiquitinationELTVLLQKLQIRVDQ
HHHHHHHHHCCEEEE		42.18-
812PhosphorylationGYLVVRLSMKIYPTT
CEEEEEEEEEEECCE		13.8930387612
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 SUN1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUN1_MOUSE !!
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 SUN1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TSNAX_MOUSETsnaxphysical
12036294
SYNE2_MOUSESyne2physical
16079285
LMNA_MOUSELmnaphysical
16380439
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SUN1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND SER-52, AND MASSSPECTROMETRY.

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