SGO1_HUMAN - dbPTM
SGO1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SGO1_HUMAN
UniProt AC Q5FBB7
Protein Name Shugoshin 1 {ECO:0000312|HGNC:HGNC:25088}
Gene Name SGO1 {ECO:0000312|HGNC:HGNC:25088}
Organism Homo sapiens (Human).
Sequence Length 561
Subcellular Localization Nucleus . Chromosome, centromere . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Localizes to the inner centromere throughout prophase until metaphas
Protein Description Plays a central role in chromosome cohesion during mitosis by preventing premature dissociation of cohesin complex from centromeres after prophase, when most of cohesin complex dissociates from chromosomes arms. May act by preventing phosphorylation of the STAG2 subunit of cohesin complex at the centromere, ensuring cohesin persistence at centromere until cohesin cleavage by ESPL1/separase at anaphase. Essential for proper chromosome segregation during mitosis and this function requires interaction with PPP2R1A. Its phosphorylated form is necessary for chromosome congression and for the proper attachment of spindle microtubule to the kinetochore. Necessary for kinetochore localization of PLK1 and CENPF. May play a role in the tension sensing mechanism of the spindle-assembly checkpoint by regulating PLK1 kinetochore affinity. Isoform 3 plays a role in maintaining centriole cohesion involved in controlling spindle pole integrity. Involved in centromeric enrichment of AUKRB in prometaphase..
Protein Sequence MAKERCLKKSFQDSLEDIKKRMKEKRNKNLAEIGKRRSFIAAPCQIITNTSTLLKNYQDNNKMLVLALENEKSKVKEAQDIILQLRKECYYLTCQLYALKGKLTSQQTVEPAQNQEICSSGMDPNSDDSSRNLFVKDLPQIPLEETELPGQGESFQIEDQIPTIPQDTLGVDFDSGEAKSTDNVLPRTVSVRSSLKKHCNSICQFDSLDDFETSHLAGKSFEFERVGFLDPLVNMHIPENVQHNACQWSKDQVNLSPKLIQPGTFTKTKEDILESKSEQTKSKQRDTQERKREEKRKANRRKSKRMSKYKENKSENKKTVPQKKMHKSVSSNDAYNFNLEEGVHLTPFRQKVSNDSNREENNESEVSLCESSGSGDDSDDLYLPTCKYIQNPTSNSDRPVTRPLAKRALKYTDEKETEGSKPTKTPTTTPPETQQSPHLSLKDITNVSLYPVVKIRRLSLSPKKNKASPAVALPKRRCTASVNYKEPTLASKLRRGDPFTDLCFLNSPIFKQKKDLRRSKKRALEVSPAKEAIFILYYVREFVSRFPDCRKCKLETHICLR
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
14PhosphorylationLKKSFQDSLEDIKKR
HHHHHHHHHHHHHHH
22817900
19UbiquitinationQDSLEDIKKRMKEKR
HHHHHHHHHHHHHHH
-
23AcetylationEDIKKRMKEKRNKNL
HHHHHHHHHHHHHCH
24431335
25AcetylationIKKRMKEKRNKNLAE
HHHHHHHHHHHCHHH
24431343
38PhosphorylationAEIGKRRSFIAAPCQ
HHHHHHHHHHHHCEE
22617229
50PhosphorylationPCQIITNTSTLLKNY
CEEEEECHHHHHHHH
22210691
119PhosphorylationAQNQEICSSGMDPNS
HHCCHHHHCCCCCCC
26074081
120PhosphorylationQNQEICSSGMDPNSD
HCCHHHHCCCCCCCC
26074081
126PhosphorylationSSGMDPNSDDSSRNL
HCCCCCCCCCHHCCC
25262027
129PhosphorylationMDPNSDDSSRNLFVK
CCCCCCCHHCCCEEC
25627689
130PhosphorylationDPNSDDSSRNLFVKD
CCCCCCHHCCCEECC
25262027
167 (in isoform 3)Phosphorylation-28387310
167 (in isoform 5)Phosphorylation-28387310
185 (in isoform 5)Ubiquitination-21890473
185 (in isoform 3)Ubiquitination-21890473
190PhosphorylationNVLPRTVSVRSSLKK
CCCCCCHHHHHHHHH
20068231
193PhosphorylationPRTVSVRSSLKKHCN
CCCHHHHHHHHHHHC
25159151
194PhosphorylationRTVSVRSSLKKHCNS
CCHHHHHHHHHHHCC
25159151
201PhosphorylationSLKKHCNSICQFDSL
HHHHHHCCCCCCCCC
-
202 (in isoform 4)Ubiquitination-21890473
202 (in isoform 2)Ubiquitination-21890473
207PhosphorylationNSICQFDSLDDFETS
CCCCCCCCCCHHHHH
20068231
220PhosphorylationTSHLAGKSFEFERVG
HHHHCCCCEEEEECC
21815630
256PhosphorylationSKDQVNLSPKLIQPG
CHHHCCCCHHHCCCC
29255136
264PhosphorylationPKLIQPGTFTKTKED
HHHCCCCCCCCCHHH
26074081
266PhosphorylationLIQPGTFTKTKEDIL
HCCCCCCCCCHHHHH
26074081
268PhosphorylationQPGTFTKTKEDILES
CCCCCCCCHHHHHHC
26074081
335PhosphorylationSVSSNDAYNFNLEEG
CCCCCCCCCCCCCCC
28122231
346PhosphorylationLEEGVHLTPFRQKVS
CCCCCEECCCCCCCC
25159151
394PhosphorylationKYIQNPTSNSDRPVT
CCCCCCCCCCCCCCC
28555341
417PhosphorylationKYTDEKETEGSKPTK
HHCCCCCCCCCCCCC
26074081
420PhosphorylationDEKETEGSKPTKTPT
CCCCCCCCCCCCCCC
26074081
423PhosphorylationETEGSKPTKTPTTTP
CCCCCCCCCCCCCCC
26074081
425PhosphorylationEGSKPTKTPTTTPPE
CCCCCCCCCCCCCCC
25159151
427PhosphorylationSKPTKTPTTTPPETQ
CCCCCCCCCCCCCCC
28450419
428PhosphorylationKPTKTPTTTPPETQQ
CCCCCCCCCCCCCCC
28450419
429PhosphorylationPTKTPTTTPPETQQS
CCCCCCCCCCCCCCC
25159151
433PhosphorylationPTTTPPETQQSPHLS
CCCCCCCCCCCCCCC
30266825
436PhosphorylationTPPETQQSPHLSLKD
CCCCCCCCCCCCHHH
30266825
440PhosphorylationTQQSPHLSLKDITNV
CCCCCCCCHHHCCCC
23663014
445PhosphorylationHLSLKDITNVSLYPV
CCCHHHCCCCCEEEE
28555341
448PhosphorylationLKDITNVSLYPVVKI
HHHCCCCCEEEEEEE
28442448
450PhosphorylationDITNVSLYPVVKIRR
HCCCCCEEEEEEEEE
28152594
454 (in isoform 6)Ubiquitination-21890473
454 (in isoform 1)Ubiquitination-21890473
454UbiquitinationVSLYPVVKIRRLSLS
CCEEEEEEEEEECCC
21890473
459PhosphorylationVVKIRRLSLSPKKNK
EEEEEEECCCCCCCC
22167270
461PhosphorylationKIRRLSLSPKKNKAS
EEEEECCCCCCCCCC
30266825
463UbiquitinationRRLSLSPKKNKASPA
EEECCCCCCCCCCCC
-
464UbiquitinationRLSLSPKKNKASPAV
EECCCCCCCCCCCCC
-
466UbiquitinationSLSPKKNKASPAVAL
CCCCCCCCCCCCCCC
-
468PhosphorylationSPKKNKASPAVALPK
CCCCCCCCCCCCCCC
25159151
488PhosphorylationSVNYKEPTLASKLRR
CCCCCCCCHHHHHCC
29449344
491PhosphorylationYKEPTLASKLRRGDP
CCCCCHHHHHCCCCC
29449344
500PhosphorylationLRRGDPFTDLCFLNS
HCCCCCCCHHHCCCC
24732914
507PhosphorylationTDLCFLNSPIFKQKK
CHHHCCCCHHHHCHH
25159151
556PhosphorylationCRKCKLETHICLR--
HHHCCCEEEEECC--
29457462

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
14SPhosphorylationKinaseNEK2P51955
Uniprot
346TPhosphorylationKinaseCDK1P06493
PSP
507SPhosphorylationKinaseNEK2P51955
Uniprot
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:19015261

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SGO1_HUMAN !!

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 SGO1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INCE_HUMANINCENPphysical
17322402
AURKB_HUMANAURKBphysical
17322402
PLK1_HUMANPLK1physical
18331714
BOREA_HUMANCDCA8physical
20739936
NSL1_HUMANNSL1physical
20231385
CBX5_HUMANCBX5physical
20231385
BUB1B_HUMANBUB1Bphysical
22374677
AL1B1_HUMANALDH1B1physical
26496610
CATC_HUMANCTSCphysical
26496610
DNM3B_HUMANDNMT3Bphysical
26496610
ECH1_HUMANECH1physical
26496610
ROAA_HUMANHNRNPABphysical
26496610
LIMS1_HUMANLIMS1physical
26496610
PFD2_HUMANPFDN2physical
26496610
RAD51_HUMANRAD51physical
26496610
SET_HUMANSETphysical
26496610
SPT6H_HUMANSUPT6Hphysical
26496610
ELOC_HUMANTCEB1physical
26496610
DYSF_HUMANDYSFphysical
26496610
CHD1L_HUMANCHD1Lphysical
26496610
NCOR1_HUMANNCOR1physical
26496610
RBCC1_HUMANRB1CC1physical
26496610
KIF2C_HUMANKIF2Cphysical
26496610
HPS5_HUMANHPS5physical
26496610
UBR2_HUMANUBR2physical
26496610
KAT6B_HUMANKAT6Bphysical
26496610
CHM2B_HUMANCHMP2Bphysical
26496610
RNC_HUMANDROSHAphysical
26496610
IMPCT_HUMANIMPACTphysical
26496610
ZN768_HUMANZNF768physical
26496610
KLH36_HUMANKLHL36physical
26496610
WDCP_HUMANC2orf44physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SGO1_HUMAN

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Related Literatures of Post-Translational Modification

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