SAS6_HUMAN - dbPTM
SAS6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAS6_HUMAN
UniProt AC Q6UVJ0
Protein Name Spindle assembly abnormal protein 6 homolog
Gene Name SASS6
Organism Homo sapiens (Human).
Sequence Length 657
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole . Component of the deuterosome, a structure that promotes de novo centriole amplification in multicilia
Protein Description Central scaffolding component of the centrioles ensuring their 9-fold symmetry. Required for centrosome biogenesis and duplication: required both for mother-centriole-dependent centriole duplication and deuterosome-dependent centriole amplification in multiciliated cells. Overexpression results in excess foci-bearing centriolar markers. Required for the recruitment of STIL to the procentriole and for STIL-mediated centriole amplification. [PubMed: 22020124]
Protein Sequence MSQVLFHQLVPLQVKCKDCEERRVSIRMSIELQSVSNPVHRKDLVIRLTDDTDPFFLYNLVISEEDFQSLKFQQGLLVDFLAFPQKFIDLLQQCTQEHAKEIPRFLLQLVSPAAILDNSPAFLNVVETNPFKHLTHLSLKLLPGNDVEIKKFLAGCLKCSKEEKLSLMQSLDDATKQLDFTRKTLAEKKQELDKLRNEWASHTAALTNKHSQELTNEKEKALQAQVQYQQQHEQQKKDLEILHQQNIHQLQNRLSELEAANKDLTERKYKGDSTIRELKAKLSGVEEELQRTKQEVLSLRRENSTLDVECHEKEKHVNQLQTKVAVLEQEIKDKDQLVLRTKEAFDTIQEQKVVLEENGEKNQVQLGKLEATIKSLSAELLKANEIIKKLQGDLKTLMGKLKLKNTVTIQQEKLLAEKEEKLQKEQKELQDVGQSLRIKEQEVCKLQEQLEATVKKLEESKQLLKNNEKLITWLNKELNENQLVRKQDVLGPSTTPPAHSSSNTIRSGISPNLNVVDGRLTYPTCGIGYPVSSAFAFQNTFPHSISAKNTSHPGSGTKVQFNLQFTKPNASLGDVQSGATISMPCSTDKENGENVGLESKYLKKREDSIPLRGLSQNLFSNSDHQRDGTLGALHTSSKPTALPSASSAYFPGQLPNS
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
2Phosphorylation------MSQVLFHQL
------CCCHHHHHE		29.0624043423
15UbiquitinationQLVPLQVKCKDCEER
HEECEEEECCCCHHC		23.70-
17AcetylationVPLQVKCKDCEERRV
ECEEEECCCCHHCEE		60.7520167786
49PhosphorylationKDLVIRLTDDTDPFF
CCEEEEECCCCCCCH		23.2120068231
52PhosphorylationVIRLTDDTDPFFLYN
EEEECCCCCCCHHEE		48.6720068231
58PhosphorylationDTDPFFLYNLVISEE
CCCCCHHEEEEECHH		10.9920068231
63PhosphorylationFLYNLVISEEDFQSL
HHEEEEECHHHHHHC		27.7020068231
69PhosphorylationISEEDFQSLKFQQGL
ECHHHHHHCCCCCCC		33.2620068231
95PhosphorylationIDLLQQCTQEHAKEI
HHHHHHHHHHHHHHH		32.43-
100UbiquitinationQCTQEHAKEIPRFLL
HHHHHHHHHHHHHHH		59.07-
100AcetylationQCTQEHAKEIPRFLL
HHHHHHHHHHHHHHH		59.0726051181
138PhosphorylationFKHLTHLSLKLLPGN
CCCHHHEEEEECCCC		18.8224719451
140UbiquitinationHLTHLSLKLLPGNDV
CHHHEEEEECCCCCH		44.60-
158UbiquitinationKFLAGCLKCSKEEKL
HHHHHHHHCCHHHHH		40.31-
164UbiquitinationLKCSKEEKLSLMQSL
HHCCHHHHHHHHHHH		44.46-
166PhosphorylationCSKEEKLSLMQSLDD
CCHHHHHHHHHHHHH		32.6328842319
168SulfoxidationKEEKLSLMQSLDDAT
HHHHHHHHHHHHHHH		1.9821406390
170PhosphorylationEKLSLMQSLDDATKQ
HHHHHHHHHHHHHHH		21.5728842319
175PhosphorylationMQSLDDATKQLDFTR
HHHHHHHHHHCHHHH		26.7328842319
209UbiquitinationHTAALTNKHSQELTN
HHHHHHHHHHHHHCH		39.12-
237UbiquitinationQQHEQQKKDLEILHQ
HHHHHHHHHHHHHHH		64.31-
269PhosphorylationKDLTERKYKGDSTIR
HHHHHCHHCCCHHHH		26.82-
273PhosphorylationERKYKGDSTIRELKA
HCHHCCCHHHHHHHH		34.11-
274PhosphorylationRKYKGDSTIRELKAK
CHHCCCHHHHHHHHH		28.88-
304PhosphorylationLSLRRENSTLDVECH
HHHHHHCCCCCEEHH		26.1230624053
305PhosphorylationSLRRENSTLDVECHE
HHHHHCCCCCEEHHH		38.2625884760
455AcetylationEQLEATVKKLEESKQ
HHHHHHHHHHHHHHH		47.4925953088
455MalonylationEQLEATVKKLEESKQ
HHHHHHHHHHHHHHH		47.4930639696
486UbiquitinationNENQLVRKQDVLGPS
CCCCCCCCCCCCCCC		43.29-
493PhosphorylationKQDVLGPSTTPPAHS
CCCCCCCCCCCCCCC		43.0125159151
494PhosphorylationQDVLGPSTTPPAHSS
CCCCCCCCCCCCCCC		46.5924732914
495PhosphorylationDVLGPSTTPPAHSSS
CCCCCCCCCCCCCCC		31.4525159151
500PhosphorylationSTTPPAHSSSNTIRS
CCCCCCCCCCCCCCC		37.2524732914
500O-linked_GlycosylationSTTPPAHSSSNTIRS
CCCCCCCCCCCCCCC		37.2530059200
501PhosphorylationTTPPAHSSSNTIRSG
CCCCCCCCCCCCCCC		20.1024732914
502PhosphorylationTPPAHSSSNTIRSGI
CCCCCCCCCCCCCCC		40.7924732914
504PhosphorylationPAHSSSNTIRSGISP
CCCCCCCCCCCCCCC		21.5124732914
507PhosphorylationSSSNTIRSGISPNLN
CCCCCCCCCCCCCCC		36.3125159151
510PhosphorylationNTIRSGISPNLNVVD
CCCCCCCCCCCCEEC		15.9725159151
533O-linked_GlycosylationGIGYPVSSAFAFQNT
CCCCCCCHHHHCCCC		27.8630059200
548UbiquitinationFPHSISAKNTSHPGS
CCCCEECCCCCCCCC		54.70-
551PhosphorylationSISAKNTSHPGSGTK
CEECCCCCCCCCCCE		36.7620068231
555PhosphorylationKNTSHPGSGTKVQFN
CCCCCCCCCCEEEEE		47.9820068231
557PhosphorylationTSHPGSGTKVQFNLQ
CCCCCCCCEEEEEEE		29.7320068231
566PhosphorylationVQFNLQFTKPNASLG
EEEEEEECCCCCCCC		32.4125690035
600UbiquitinationENVGLESKYLKKRED
CCCCCCHHHHHHCCC		45.27-
608PhosphorylationYLKKREDSIPLRGLS
HHHHCCCCCCCCHHC		22.7323186163
615PhosphorylationSIPLRGLSQNLFSNS
CCCCCHHCCCCCCCC		21.6123917254
622PhosphorylationSQNLFSNSDHQRDGT
CCCCCCCCCCCCCCC		34.9628555341
649PhosphorylationLPSASSAYFPGQLPN
CCCCCCCCCCCCCCC		16.5627642862
657PhosphorylationFPGQLPNS-------
CCCCCCCC-------		39.3925159151
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
-KUbiquitinationE3 ubiquitin ligaseFBXW5Q969U6
PMID:21725316
-KUbiquitinationE3 ubiquitin ligaseFZR1Q9UM11
PMID:17681132
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAS6_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 SAS6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBXW5_HUMANFBXW5physical
21725316
STIL_HUMANSTILphysical
22349698
ABRAL_HUMANABRACLphysical
26638075
ALMS1_HUMANALMS1physical
26638075
APC_HUMANAPCphysical
26638075
CP131_HUMANCEP131physical
26638075
CC138_HUMANCCDC138physical
26638075
CP110_HUMANCCP110physical
26638075
CE152_HUMANCEP152physical
26638075
CE170_HUMANCEP170physical
26638075
CEP97_HUMANCEP97physical
26638075
DLG5_HUMANDLG5physical
26638075
DVL2_HUMANDVL2physical
26638075
RB6I2_HUMANERC1physical
26638075
WAC2A_HUMANFAM21Aphysical
26638075
FR1OP_HUMANFGFR1OPphysical
26638075
GPTC1_HUMANGPATCH1physical
26638075
HAUS1_HUMANHAUS1physical
26638075
HAUS2_HUMANHAUS2physical
26638075
HAUS3_HUMANHAUS3physical
26638075
HAUS4_HUMANHAUS4physical
26638075
HAUS5_HUMANHAUS5physical
26638075
HAUS6_HUMANHAUS6physical
26638075
HAUS7_HUMANHAUS7physical
26638075
HAUS8_HUMANHAUS8physical
26638075
ISOC1_HUMANISOC1physical
26638075
K1671_HUMANKIAA1671physical
26638075
LRC49_HUMANLRRC49physical
26638075
MED4_HUMANMED4physical
26638075
MTPN_HUMANMTPNphysical
26638075
NEDD1_HUMANNEDD1physical
26638075
NRBF2_HUMANNRBF2physical
26638075
OFD1_HUMANOFD1physical
26638075
PCM1_HUMANPCM1physical
26638075
PIBF1_HUMANPIBF1physical
26638075
RAE1L_HUMANRAE1physical
26638075
RGPD1_HUMANRGPD1physical
26638075
SDCG3_HUMANSDCCAG3physical
26638075
SQSTM_HUMANSQSTM1physical
26638075
SRSF2_HUMANSRSF2physical
26638075
ADIP_HUMANSSX2IPphysical
26638075
TARB1_HUMANTARBP1physical
26638075
TBK1_HUMANTBK1physical
26638075
ZO1_HUMANTJP1physical
26638075
TNR6B_HUMANTNRC6Bphysical
26638075
TTC28_HUMANTTC28physical
26638075
UBR4_HUMANUBR4physical
26638075
UN45A_HUMANUNC45Aphysical
26638075
WRP73_HUMANWRAP73physical
26638075
CENPJ_HUMANCENPJphysical
26638075
ALAT1_HUMANGPTphysical
26496610
SMBP2_HUMANIGHMBP2physical
26496610
NFIB_HUMANNFIBphysical
26496610
C2CD5_HUMANC2CD5physical
26496610
RTEL1_HUMANRTEL1physical
26496610
EFL1_HUMANEFTUD1physical
26496610
RT4I1_HUMANRTN4IP1physical
26496610
NIPA_HUMANZC3HC1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616402Microcephaly 14, primary, autosomal recessive (MCPH14)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAS6_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-510 AND SER-657, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory