SMC1B_HUMAN - dbPTM
SMC1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMC1B_HUMAN
UniProt AC Q8NDV3
Protein Name Structural maintenance of chromosomes protein 1B
Gene Name SMC1B
Organism Homo sapiens (Human).
Sequence Length 1235
Subcellular Localization Nucleus . Chromosome . Chromosome, centromere . Associates with chromatin. In prophase I stage of meiosis, localizes along the AE of synaptonemal complexes. In late-pachytene-diplotene, the bulk of protein dissociates from the chromosome arms probabl
Protein Description Meiosis-specific component of cohesin complex. Required for the maintenance of meiotic cohesion, but not, or only to a minor extent, for its establishment. Contributes to axial element (AE) formation and the organization of chromatin loops along the AE. Plays a key role in synapsis, recombination and chromosome movements. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The meiosis-specific cohesin complex probably replaces mitosis specific cohesin complex when it dissociates from chromatin during prophase I (By similarity)..
Protein Sequence MAHLELLLVENFKSWRGRQVIGPFRRFTCIIGPNGSGKSNVMDALSFVMGEKIANLRVKNIQELIHGAHIGKPISSSASVKIIYVEESGEEKTFARIIRGGCSEFRFNDNLVSRSVYIAELEKIGIIVKAQNCLVFQGTVESISVKKPKERTQFFEEISTSGELIGEYEEKKRKLQKAEEDAQFNFNKKKNIAAERRQAKLEKEEAERYQSLLEELKMNKIQLQLFQLYHNEKKIHLLNTKLEHVNRDLSVKRESLSHHENIVKARKKEHGMLTRQLQQTEKELKSVETLLNQKRPQYIKAKENTSHHLKKLDVAKKSIKDSEKQCSKQEDDIKALETELADLDAAWRSFEKQIEEEILHKKRDIELEASQLDRYKELKEQVRKKVATMTQQLEKLQWEQKTDEERLAFEKRRHGEVQGNLKQIKEQIEDHKKRIEKLEEYTKTCMDCLKEKKQQEETLVDEIEKTKSRMSEFNEELNLIRSELQNAGIDTHEGKRQQKRAEVLEHLKRLYPDSVFGRLFDLCHPIHKKYQLAVTKVFGRFITAIVVASEKVAKDCIRFLKEERAEPETFLALDYLDIKPINERLRELKGCKMVIDVIKTQFPQLKKVIQFVCGNGLVCETMEEARHIALSGPERQKTVALDGTLFLKSGVISGGSSDLKYKARCWDEKELKNLRDRRSQKIQELKGLMKTLRKETDLKQIQTLIQGTQTRLKYSQNELEMIKKKHLVAFYQEQSQLQSELLNIESQCIMLSEGIKERQRRIKEFQEKIDKVEDDIFQHFCEEIGVENIREFENKHVKRQQEIDQKRYFYKKMLTRLNVQLEYSRSHLKKKLNKINTLKETIQKGSEDIDHLKKAEENCLQTVNELMAKQQQLKDIRVTQNSSAEKVQTQIEEERKKFLAVDREVGKLQKEVVSIQTSLEQKRLEKHNLLLDCKVQDIEIILLSGSLDDIIEVEMGTEAESTQATIDIYEKEEAFEIDYSSLKEDLKALQSDQEIEAHLRLLLQQVASQEDILLKTAAPNLRALENLKTVRDKFQESTDAFEASRKEARLCRQEFEQVKKRRYDLFTQCFEHVSISIDQIYKKLCRNNSAQAFLSPENPEEPYLEGISYNCVAPGKRFMPMDNLSGGEKCVAALALLFAVHSFRPAPFFVLDEVDAALDNTNIGKVSSYIKEQTQDQFQMIVISLKEEFYSRADALIGIYPEYDDCMFSRVLTLDLSQYPDTEGQESSKRHGESR
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
38UbiquitinationIGPNGSGKSNVMDAL
ECCCCCCHHHHHHHH		40.32-
84PhosphorylationSASVKIIYVEESGEE
CCEEEEEEEECCCCC		12.7928270605
88PhosphorylationKIIYVEESGEEKTFA
EEEEEECCCCCEEHH		37.6928270605
92UbiquitinationVEESGEEKTFARIIR
EECCCCCEEHHHHHC		44.64-
113PhosphorylationRFNDNLVSRSVYIAE
CCCCCHHCCEEEEHH		23.2327251275
115PhosphorylationNDNLVSRSVYIAELE
CCCHHCCEEEEHHHH		16.2727251275
142PhosphorylationVFQGTVESISVKKPK
EEECEEEEEEECCCH		18.8124719451
177UbiquitinationEKKRKLQKAEEDAQF
HHHHHHHHHHHHHCC		69.10-
188UbiquitinationDAQFNFNKKKNIAAE
HHCCCCCHHHHHHHH		62.07-
190UbiquitinationQFNFNKKKNIAAERR
CCCCCHHHHHHHHHH		56.02-
211PhosphorylationEEAERYQSLLEELKM
HHHHHHHHHHHHHHH		26.4518452278
233UbiquitinationFQLYHNEKKIHLLNT
HHHHCCHHHHHHHHH		63.4530230243
234UbiquitinationQLYHNEKKIHLLNTK
HHHCCHHHHHHHHHH		29.2229967540
234AcetylationQLYHNEKKIHLLNTK
HHHCCHHHHHHHHHH		29.2220167786
241AcetylationKIHLLNTKLEHVNRD
HHHHHHHHHHHHCCC		51.2920167786
252AcetylationVNRDLSVKRESLSHH
HCCCCHHCHHHHCCC		47.2620167786
268UbiquitinationNIVKARKKEHGMLTR
HHHHHHHHHHCHHHH		49.76-
285UbiquitinationQQTEKELKSVETLLN
HHHHHHHHHHHHHHH		54.25-
294UbiquitinationVETLLNQKRPQYIKA
HHHHHHCCCCHHHHC		66.04-
294AcetylationVETLLNQKRPQYIKA
HHHHHHCCCCHHHHC		66.0425953088
322PhosphorylationAKKSIKDSEKQCSKQ
HHHHCHHHHHHHHCC		41.5129759185
324SumoylationKSIKDSEKQCSKQED
HHCHHHHHHHHCCHH		61.63-
327PhosphorylationKDSEKQCSKQEDDIK
HHHHHHHHCCHHHHH		34.5729759185
388PhosphorylationQVRKKVATMTQQLEK
HHHHHHHHHHHHHHH		24.6024043423
390PhosphorylationRKKVATMTQQLEKLQ
HHHHHHHHHHHHHHH		14.6024043423
395UbiquitinationTMTQQLEKLQWEQKT
HHHHHHHHHHHHHCC		55.35-
466PhosphorylationLVDEIEKTKSRMSEF
HHHHHHHHHHHHHHH		22.8221406692
468PhosphorylationDEIEKTKSRMSEFNE
HHHHHHHHHHHHHHH		38.1521406692
471PhosphorylationEKTKSRMSEFNEELN
HHHHHHHHHHHHHHH		37.6226270265
495UbiquitinationGIDTHEGKRQQKRAE
CCCCCHHHHHHHHHH		44.0129967540
495AcetylationGIDTHEGKRQQKRAE
CCCCCHHHHHHHHHH		44.0125953088
508UbiquitinationAEVLEHLKRLYPDSV
HHHHHHHHHHCCCCH		42.12-
511PhosphorylationLEHLKRLYPDSVFGR
HHHHHHHCCCCHHHH		14.7128152594
514PhosphorylationLKRLYPDSVFGRLFD
HHHHCCCCHHHHHHH		18.1628152594
529UbiquitinationLCHPIHKKYQLAVTK
HHCHHHHHHHHHHHH		24.8629967540
543PhosphorylationKVFGRFITAIVVASE
HHHHHHHHHHHHCCH		13.9721406692
579UbiquitinationALDYLDIKPINERLR
EHHHCCCHHHHHHHH		39.2429967540
638PhosphorylationSGPERQKTVALDGTL
CCCHHHCEEEECCEE		11.59-
644PhosphorylationKTVALDGTLFLKSGV
CEEEECCEEEEECCC		17.63-
648AcetylationLDGTLFLKSGVISGG
ECCEEEEECCCCCCC		37.52-
661PhosphorylationGGSSDLKYKARCWDE
CCCCCHHHHHCCCCH		19.71-
691PhosphorylationELKGLMKTLRKETDL
HHHHHHHHHHHHCCH		20.17-
713AcetylationQGTQTRLKYSQNELE
HHHHHHHHCCHHHHH		39.29-
815O-linked_GlycosylationYFYKKMLTRLNVQLE
HHHHHHHHHHHHHHH		29.6130379171
815PhosphorylationYFYKKMLTRLNVQLE
HHHHHHHHHHHHHHH		29.61-
882PhosphorylationDIRVTQNSSAEKVQT
CCCCCCCCCHHHHHH		22.5517924679
883PhosphorylationIRVTQNSSAEKVQTQ
CCCCCCCCHHHHHHH		48.2517924679
961PhosphorylationEMGTEAESTQATIDI
ECCCCCCCCEEEEEE		32.63-
965PhosphorylationEAESTQATIDIYEKE
CCCCCEEEEEEHHCH		14.90-
1028UbiquitinationLRALENLKTVRDKFQ
HHHHHCHHHHHHHHH		57.4629967540
1033AcetylationNLKTVRDKFQESTDA
CHHHHHHHHHHCHHH		38.08-
1063PhosphorylationEQVKKRRYDLFTQCF
HHHHHHHHHHHHHHH		22.4926074081
1125PhosphorylationFMPMDNLSGGEKCVA
CCCCCCCCHHHHHHH		51.51-
1184PhosphorylationQFQMIVISLKEEFYS
HHHHEEHHCHHHHHH		23.6124719451
1203PhosphorylationLIGIYPEYDDCMFSR
HCCCCCCCCCCCEEE		16.75-
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 SMC1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMC1B_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 SMC1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD21_HUMANRAD21physical
26344197
SMC3_HUMANSMC3physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMC1B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882 AND SER-883, ANDMASS SPECTROMETRY.

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