FSD1_HUMAN - dbPTM
FSD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FSD1_HUMAN
UniProt AC Q9BTV5
Protein Name Fibronectin type III and SPRY domain-containing protein 1
Gene Name FSD1
Organism Homo sapiens (Human).
Sequence Length 496
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus. Cytoplasm. Cleavage furrow. Cell-cycle-dependent association with the centrosome. Colocalizes with a subpopulation of microtubules. Does not associates with microtubules dur
Protein Description May be involved in microtubule organization and stabilization..
Protein Sequence MEEQREALRKIIKTLAVKNEEIQSFIYSLKQMLLNVEANSAKVQEDLEAEFQSLFSLLEELKEGMLMKIKQDRASRTYELQNQLAACTRALESSEELLETANQTLQAMDSEDFPQAAKQIKDGVTMAPAFRLSLKAKVSDNMSHLMVDFAQERQMLQALKFLPVPSAPVIDLAESLVADNCVTLVWRMPDEDSKIDHYVLEYRRTNFEGPPRLKEDQPWMVIEGIRQTEYTLTGLKFDMKYMNFRVKACNKAVAGEFSEPVTLETPAFMFRLDASTSHQNLRVDDLSVEWDAMGGKVQDIKAREKDGKGRTASPINSPARGTPSPKRMPSGRGGRDRFTAESYTVLGDTLIDGGEHYWEVRYEPDSKAFGVGVAYRSLGRFEQLGKTAASWCLHVNNWLQVSFTAKHANKVKVLDAPVPDCLGVHCDFHQGLLSFYNARTKQVLHTFKTRFTQPLLPAFTVWCGSFQVTTGLQVPSAVRCLQKRGSATSSSNTSLT
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
13UbiquitinationEALRKIIKTLAVKNE
HHHHHHHHHHHHCCH		40.7421890473
28PhosphorylationEIQSFIYSLKQMLLN
HHHHHHHHHHHHHHH		25.0324719451
118UbiquitinationEDFPQAAKQIKDGVT
CCCHHHHHHHCCCCC		56.42-
126SulfoxidationQIKDGVTMAPAFRLS
HHCCCCCCCHHHHHH		3.8021406390
193PhosphorylationWRMPDEDSKIDHYVL
EECCCCCCCCCEEEE		29.48-
198PhosphorylationEDSKIDHYVLEYRRT
CCCCCCEEEEEECCC		11.72-
202PhosphorylationIDHYVLEYRRTNFEG
CCEEEEEECCCCCCC		10.96-
214UbiquitinationFEGPPRLKEDQPWMV
CCCCCCCCCCCCCEE		61.60-
240UbiquitinationTGLKFDMKYMNFRVK
ECEEEECEECCEEEH		43.10-
241PhosphorylationGLKFDMKYMNFRVKA
CEEEECEECCEEEHH		7.2230631047
258PhosphorylationKAVAGEFSEPVTLET
HHHCCCCCCCEEEEC		36.3723898821
301AcetylationGGKVQDIKAREKDGK
CCCEEEEHHHCCCCC		50.0819807531
305AcetylationQDIKAREKDGKGRTA
EEEHHHCCCCCCCCC		67.2519807539
310MethylationREKDGKGRTASPINS
HCCCCCCCCCCCCCC		30.52-
311PhosphorylationEKDGKGRTASPINSP
CCCCCCCCCCCCCCC		39.9126055452
313PhosphorylationDGKGRTASPINSPAR
CCCCCCCCCCCCCCC		26.2126055452
317PhosphorylationRTASPINSPARGTPS
CCCCCCCCCCCCCCC		22.2126055452
320MethylationSPINSPARGTPSPKR
CCCCCCCCCCCCCCC		53.5624129315
322PhosphorylationINSPARGTPSPKRMP
CCCCCCCCCCCCCCC		18.2923663014
324PhosphorylationSPARGTPSPKRMPSG
CCCCCCCCCCCCCCC		42.7821712546
332MethylationPKRMPSGRGGRDRFT
CCCCCCCCCCCCCCE		49.05-
367UbiquitinationVRYEPDSKAFGVGVA
EEECCCCCCCCCEEH		55.93-
375PhosphorylationAFGVGVAYRSLGRFE
CCCCEEHHHHCCCHH		9.7923612710
452PhosphorylationHTFKTRFTQPLLPAF
HHHHHCCCCCCCCEE		26.45-
486PhosphorylationRCLQKRGSATSSSNT
HHHHHCCCCCCCCCC		32.1922617229
488PhosphorylationLQKRGSATSSSNTSL
HHHCCCCCCCCCCCC		30.7323403867
489PhosphorylationQKRGSATSSSNTSLT
HHCCCCCCCCCCCCC		31.3320363803
490PhosphorylationKRGSATSSSNTSLT-
HCCCCCCCCCCCCC-		24.2120363803
491PhosphorylationRGSATSSSNTSLT--
CCCCCCCCCCCCC--		43.8420363803
493PhosphorylationSATSSSNTSLT----
CCCCCCCCCCC----		27.3620363803
494PhosphorylationATSSSNTSLT-----
CCCCCCCCCC-----		33.9720363803
496PhosphorylationSSSNTSLT-------
CCCCCCCC-------		36.0123403867
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 FSD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FSD1_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 FSD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CYTSA_HUMANSPECC1Lphysical
26186194
TLDC1_HUMANTLDC1physical
26186194
AGFG1_HUMANAGFG1physical
26186194
PYGB_HUMANPYGBphysical
26186194
MIB1_HUMANMIB1physical
26186194
AIDA_HUMANAIDAphysical
26186194
SRC_HUMANSRCphysical
26186194
SYUA_HUMANSNCAphysical
26186194
BIRC2_HUMANBIRC2physical
26186194
UB2D2_HUMANUBE2D2physical
26186194
ILEU_HUMANSERPINB1physical
26186194
NAA50_HUMANNAA50physical
26186194
UB2E3_HUMANUBE2E3physical
26186194
ERF1_HUMANETF1physical
26186194
FBX46_HUMANFBXO46physical
26186194
ARPIN_HUMANARPINphysical
26186194
PAK2_HUMANPAK2physical
26186194
FAHD1_HUMANFAHD1physical
26186194
UBFD1_HUMANUBFD1physical
26186194
PTN11_HUMANPTPN11physical
26186194
UBCP1_HUMANUBLCP1physical
26186194
RHG01_HUMANARHGAP1physical
26186194
EFHD1_HUMANEFHD1physical
26186194
NCS1_HUMANNCS1physical
26186194
EEPD1_HUMANEEPD1physical
26186194
CGL_HUMANCTHphysical
26186194
VTA1_HUMANVTA1physical
26186194
TCEA1_HUMANTCEA1physical
26186194
DENR_HUMANDENRphysical
26186194
PRRC1_HUMANPRRC1physical
26186194
AR2BP_HUMANARL2BPphysical
26186194
BLVRB_HUMANBLVRBphysical
26186194
EHD4_HUMANEHD4physical
26186194
GBG5_HUMANGNG5physical
26186194
MCTS1_HUMANMCTS1physical
26186194
HMCS1_HUMANHMGCS1physical
26186194
TTL12_HUMANTTLL12physical
26186194
CHAC2_HUMANCHAC2physical
26186194
ARPIN_HUMANARPINphysical
28514442
UBFD1_HUMANUBFD1physical
28514442
EFHD1_HUMANEFHD1physical
28514442
UBCP1_HUMANUBLCP1physical
28514442
AIDA_HUMANAIDAphysical
28514442
SRC_HUMANSRCphysical
28514442
CHAC2_HUMANCHAC2physical
28514442
LZIC_HUMANLZICphysical
28514442
AR2BP_HUMANARL2BPphysical
28514442
ILEU_HUMANSERPINB1physical
28514442
UB2D2_HUMANUBE2D2physical
28514442
CGL_HUMANCTHphysical
28514442
FAHD1_HUMANFAHD1physical
28514442
RHG01_HUMANARHGAP1physical
28514442
PTN11_HUMANPTPN11physical
28514442
PAK2_HUMANPAK2physical
28514442
MCTS1_HUMANMCTS1physical
28514442
PAK1_HUMANPAK1physical
28514442
FTO_HUMANFTOphysical
28514442
EEPD1_HUMANEEPD1physical
28514442
CHRC1_HUMANCHRAC1physical
28514442
PRRC1_HUMANPRRC1physical
28514442
BLVRB_HUMANBLVRBphysical
28514442
FBX46_HUMANFBXO46physical
28514442
MIB1_HUMANMIB1physical
28514442
HMCS1_HUMANHMGCS1physical
28514442
HDHD2_HUMANHDHD2physical
28514442
TES_HUMANTESphysical
28514442
DENR_HUMANDENRphysical
28514442
EFHD2_HUMANEFHD2physical
28514442
VTA1_HUMANVTA1physical
28514442
CYTSA_HUMANSPECC1Lphysical
28514442
PMVK_HUMANPMVKphysical
28514442
GBG5_HUMANGNG5physical
28514442
DDAH1_HUMANDDAH1physical
28514442
PLSI_HUMANPLS1physical
28514442
GAMT_HUMANGAMTphysical
28514442
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 FSD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-317 ANDSER-324, AND MASS SPECTROMETRY.

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