SCC3_YEAST - dbPTM
SCC3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SCC3_YEAST
UniProt AC P40541
Protein Name Cohesin subunit SCC3
Gene Name IRR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1150
Subcellular Localization Nucleus . Chromosome . Chromosome, centromere . Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin except at centromeres, where cohesin complexes rema
Protein Description Component of cohesin complex, a complex 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 MCD1/SCC1 subunit of the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis..
Protein Sequence MTAVRRSTRIRTKSQVIEEDYDDEQNTSAQHVESDKITAKTQHEEEEEQDTGESEESSSEDDYEDQDDDDYVDTATAKRKSRKRKPKSASNTSSKRQKKKPTSAQKSAVSHAPAYHRSKKDQDQYLEIAKDFQPTELFDILSTSEDVSIEELLREWLETYSENRDKFLQEFINLLLNCCGSVARVEDHDVHSNESSNETIGEIQLLFQRQKLHEFYLLISKENKKRKNFKMGPLYQNFAEFMTKLLEVANDLQLLYVESDEDDTQIVTGNLVLDLLTWLSSFSVCKIRCFRYISTLTLYLFQDYLTQQAVNLEKNYLAKLSKQLSLEEKKKRPNNKTLEKLESTIAETQGSKVVIDSIIDNIVKLCFVHRYKDVSDLIRSESMLHLSIWIKNYPEYFLKVTFLKYFGWLLSDNSVSVRLQVTKILPHLIIQNHNSKSTDNSAIRQVFERFKTKILEVAIRDVNLDVRIHSIQVLTEASSLGYLDDSEILIISSLMFDEEFDPFKTSSFNKRSKFLSTVAKFLARVIKEKFDEFIKTHEDLPKEVDGLEVGPVVQVGIFIKILNDSLIYHLKDCAEVDSRTKIRMLTQAAEFLSPYISTHLKTICNLLISDTESNELIQKLQNSANNNSDDEDVDDEELDITPLFPIDRNSTILYLNVFHGLCAGANNPKIQTKDSVKEIVLPLFYDLLNAASIESADILCPLLESFITFSLDDWISIGYETELKKITDKTIKAFMDSTIGNSKVDMKYDIFAKFIHHIHHFEKKELQEKFLNQIATLKIHLKKFLQEKMDPNNSRDDYKDLTCSLYELYINKLTILGRDYPIEVDEELLQLFLNNFVSRIPIMFQDFDDSTAQEINFKMLVLLATWNLEKWREIIEKVRDYENSISKDLRSVWKPIAAIIGRLNTLVISLAATNETFENINSLFYLKWSACTSLMDIIVAIKIFELKLPADATTWRYSMSEQFPFYLHDNASKVLLKIFLYLESLFAKQVDVQLERVADEDANLNDLPETGFFENIETEFLLFTVKLKGLMKLNILDERFASRVALNKEKLGPLFKKIVDDTIMENPEPNKKNIQKAKSNQTQREKAPLQPNSERETDHANTENNDPDIPMTIDLEPIEESSQNNSELAPIEEHPTVVDAIDNSDEITQD
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
12PhosphorylationRRSTRIRTKSQVIEE
HHCCCCCCHHHHCCC		32.4530377154
14PhosphorylationSTRIRTKSQVIEEDY
CCCCCCHHHHCCCCC		29.1220377248
21PhosphorylationSQVIEEDYDDEQNTS
HHHCCCCCCCCCCCC		28.6822369663
27PhosphorylationDYDDEQNTSAQHVES
CCCCCCCCCCHHHHH		25.7422369663
28PhosphorylationYDDEQNTSAQHVESD
CCCCCCCCCHHHHHH		33.2222369663
34PhosphorylationTSAQHVESDKITAKT
CCCHHHHHHHCEEEC		43.0222369663
36AcetylationAQHVESDKITAKTQH
CHHHHHHHCEEECCC		51.7622865919
38PhosphorylationHVESDKITAKTQHEE
HHHHHHCEEECCCHH		28.0424961812
51PhosphorylationEEEEEQDTGESEESS
HHHHCCCCCCCCCCC		42.4121551504
92PhosphorylationKPKSASNTSSKRQKK
CCCCCCCCCCHHHHC		31.7028889911
103PhosphorylationRQKKKPTSAQKSAVS
HHHCCCCHHHHHHHH		36.9127214570
343PhosphorylationKTLEKLESTIAETQG
HHHHHHHHHHHHHCC		35.2320190278
344PhosphorylationTLEKLESTIAETQGS
HHHHHHHHHHHHCCC		18.1630377154
451AcetylationRQVFERFKTKILEVA
HHHHHHHHHHHHHHH		55.9525381059
623PhosphorylationLIQKLQNSANNNSDD
HHHHHHHHHCCCCCC		21.2928889911
628PhosphorylationQNSANNNSDDEDVDD
HHHHCCCCCCCCCCH		48.8728152593
650PhosphorylationLFPIDRNSTILYLNV
CEECCCCCCEEEEEH		20.0930377154
727PhosphorylationETELKKITDKTIKAF
HHHHHHCCHHHHHHH		40.0828889911
865PhosphorylationKMLVLLATWNLEKWR
HHHHHHHHCCHHHHH		18.1728152593
881PhosphorylationIIEKVRDYENSISKD
HHHHHHHHHHHHCHH		13.3728889911
1093PhosphorylationKAPLQPNSERETDHA
HCCCCCCCHHHCCCC		44.7227214570
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 SCC3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SCC3_YEAST !!
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 SCC3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMB4_YEASTKAP123physical
11805826
LIN1_YEASTLIN1physical
12402242
STH1_YEASTSTH1physical
15023343
SCC1_YEASTMCD1physical
9990856
SMC1_YEASTSMC1physical
9990856
SMC3_YEASTSMC3physical
9990856
SCC2_YEASTSCC2physical
9990856
IST2_YEASTIST2genetic
12362983
NOG2_YEASTNOG2genetic
12362983
CBF3C_YEASTCTF13genetic
11782448
H2A2_YEASTHTA2physical
16554755
SCC1_YEASTMCD1physical
16554755
YRA1_YEASTYRA1physical
16554755
SMC3_YEASTSMC3physical
16554755
SCC1_YEASTMCD1physical
17660750
SMC1_YEASTSMC1physical
17660750
SMC3_YEASTSMC3physical
17660750
HOS1_YEASTHOS1physical
18719252
SCC1_YEASTMCD1physical
18617290
HSP71_YEASTSSA1physical
19536198
RAD61_YEASTRAD61physical
19328069
SCC1_YEASTMCD1physical
21441928
PDS5_YEASTPDS5physical
21441928
SMC1_YEASTSMC1physical
21441928
SMC3_YEASTSMC3physical
21441928
PDS5_YEASTPDS5physical
22912589
APC11_YEASTAPC11genetic
27708008
COG3_YEASTCOG3genetic
27708008
CDC20_YEASTCDC20genetic
27708008
DAM1_YEASTDAM1genetic
27708008
CBF3A_YEASTCBF2genetic
27708008
UTP9_YEASTUTP9genetic
27708008
RFC2_YEASTRFC2genetic
27708008
PRS7_YEASTRPT1genetic
27708008
YKT6_YEASTYKT6genetic
27708008
SED5_YEASTSED5genetic
27708008
VTI1_YEASTVTI1genetic
27708008
LTE1_YEASTLTE1genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
NU170_YEASTNUP170genetic
27708008
NPL4_YEASTNPL4genetic
27708008
SWC5_YEASTSWC5genetic
27708008
CHK1_YEASTCHK1genetic
27708008
SLX5_YEASTSLX5genetic
27708008
VPS41_YEASTVPS41genetic
27708008
NUM1_YEASTNUM1genetic
27708008
SAC3_YEASTSAC3genetic
27708008
ACL4_YEASTYDR161Wgenetic
27708008
MON1_YEASTMON1genetic
27708008
UBR1_YEASTUBR1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
PEP8_YEASTPEP8genetic
27708008
DAL5_YEASTDAL5genetic
27708008
ELM1_YEASTELM1genetic
27708008
FRMSR_YEASTYKL069Wgenetic
27708008
SAC1_YEASTSAC1genetic
27708008
DYHC_YEASTDYN1genetic
27708008
PAM17_YEASTPAM17genetic
27708008
LDB18_YEASTLDB18genetic
27708008
PUR91_YEASTADE16genetic
27708008
RIC1_YEASTRIC1genetic
27708008
YL053_YEASTYLR053Cgenetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
JNM1_YEASTJNM1genetic
27708008
DYN3_YEASTDYN3genetic
27708008
MKT1_YEASTMKT1genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
PFD4_YEASTGIM3genetic
27708008
TLG2_YEASTTLG2genetic
27708008
INO4_YEASTINO4genetic
27708008
BUB3_YEASTBUB3genetic
27708008
VHS3_YEASTVHS3genetic
27708008
BUD21_YEASTBUD21genetic
27708008
DIA2_YEASTDIA2genetic
27708008
RUD3_YEASTRUD3genetic
27708008
LIS1_YEASTPAC1genetic
27708008
RAD1_YEASTRAD1genetic
27708008
PMA2_YEASTPMA2genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
POC4_YEASTPOC4genetic
27708008
RU2A_YEASTLEA1genetic
27708008
ACM1_YEASTACM1genetic
27708008
KAR3_YEASTKAR3genetic
27708008
RT05_YEASTMRPS5physical
28077952
SCC2_YEASTSCC2physical
25748820
SCC1_YEASTMCD1physical
25748820
PDS5_YEASTPDS5physical
25748820
RAD61_YEASTRAD61physical
25748820
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SCC3_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-27; SER-28 AND SER-343,AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, AND MASSSPECTROMETRY.

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