SPS1_HUMAN - dbPTM
SPS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPS1_HUMAN
UniProt AC P49903
Protein Name Selenide, water dikinase 1
Gene Name SEPHS1
Organism Homo sapiens (Human).
Sequence Length 392
Subcellular Localization Isoform 1: Cell membrane. Nucleus membrane.
Isoform 2: Cytoplasm.
Isoform 3: Cytoplasm.
Isoform 4: Cytoplasm.
Protein Description Synthesizes selenophosphate from selenide and ATP..
Protein Sequence MSTRESFNPESYELDKSFRLTRFTELKGTGCKVPQDVLQKLLESLQENHFQEDEQFLGAVMPRLGIGMDTCVIPLRHGGLSLVQTTDYIYPIVDDPYMMGRIACANVLSDLYAMGVTECDNMLMLLGVSNKMTDRERDKVMPLIIQGFKDAAEEAGTSVTGGQTVLNPWIVLGGVATTVCQPNEFIMPDNAVPGDVLVLTKPLGTQVAVAVHQWLDIPEKWNKIKLVVTQEDVELAYQEAMMNMARLNRTAAGLMHTFNAHAATDITGFGILGHAQNLAKQQRNEVSFVIHNLPVLAKMAAVSKACGNMFGLMHGTCPETSGGLLICLPREQAARFCAEIKSPKYGEGHQAWIIGIVEKGNRTARIIDKPRIIEVAPQVATQNVNPTPGATS
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
2Acetylation------MSTRESFNP
------CCCCCCCCH		35.8519413330
2Phosphorylation------MSTRESFNP
------CCCCCCCCH		35.8523663014
3Phosphorylation-----MSTRESFNPE
-----CCCCCCCCHH		36.8423663014
6Phosphorylation--MSTRESFNPESYE
--CCCCCCCCHHHHH		27.3423663014
11PhosphorylationRESFNPESYELDKSF
CCCCCHHHHHHCCCE		25.7623663014
12PhosphorylationESFNPESYELDKSFR
CCCCHHHHHHCCCEE		20.8923663014
162-HydroxyisobutyrylationPESYELDKSFRLTRF
HHHHHHCCCEEEEEE		65.21-
16UbiquitinationPESYELDKSFRLTRF
HHHHHHCCCEEEEEE		65.2123000965
17PhosphorylationESYELDKSFRLTRFT
HHHHHCCCEEEEEEE		18.4422210691
27AcetylationLTRFTELKGTGCKVP
EEEEEECCCCCCCCC		48.4723749302
27UbiquitinationLTRFTELKGTGCKVP
EEEEEECCCCCCCCC		48.4733845483
32UbiquitinationELKGTGCKVPQDVLQ
ECCCCCCCCCHHHHH		59.2929967540
68SulfoxidationMPRLGIGMDTCVIPL
HHHCCCCCCEEEEEE		3.4921406390
70PhosphorylationRLGIGMDTCVIPLRH
HCCCCCCEEEEEECC		10.3629083192
72UbiquitinationGIGMDTCVIPLRHGG
CCCCCEEEEEECCCC		5.6921890473
139UbiquitinationMTDRERDKVMPLIIQ
CCHHHHHCHHHHHHH		46.8021890473
139AcetylationMTDRERDKVMPLIIQ
CCHHHHHCHHHHHHH		46.8025953088
139UbiquitinationMTDRERDKVMPLIIQ
CCHHHHHCHHHHHHH		46.8021890473
139UbiquitinationMTDRERDKVMPLIIQ
CCHHHHHCHHHHHHH		46.8023000965
270UbiquitinationATDITGFGILGHAQN
CCCCCCCHHHHHHHH		18.6333845483
274UbiquitinationTGFGILGHAQNLAKQ
CCCHHHHHHHHHHHH		22.2433845483
341UbiquitinationARFCAEIKSPKYGEG
HHHHHHCCCCCCCCC		52.8133845483
341AcetylationARFCAEIKSPKYGEG
HHHHHHCCCCCCCCC		52.8120167786
342PhosphorylationRFCAEIKSPKYGEGH
HHHHHCCCCCCCCCC		32.0828348404
345PhosphorylationAEIKSPKYGEGHQAW
HHCCCCCCCCCCEEE		24.6417360941
387PhosphorylationATQNVNPTPGATS--
CCCCCCCCCCCCC--		29.2025159151
391PhosphorylationVNPTPGATS------
CCCCCCCCC------		40.6730576142
392PhosphorylationNPTPGATS-------
CCCCCCCC-------		37.3830278072
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 SPS1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPS1_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 SPS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPS1_HUMANSEPHS1physical
16189514
SACA9_HUMANC9orf9physical
16169070
GBP2_HUMANGBP2physical
16169070
S35F6_HUMANSLC35F6physical
16169070
IGS21_HUMANIGSF21physical
16169070
U119A_HUMANUNC119physical
16169070
ERG28_HUMANC14orf1physical
16169070
DPYL1_HUMANCRMP1physical
16169070
XPO7_HUMANXPO7physical
22939629
TPD52_HUMANTPD52physical
22939629
WDR12_HUMANWDR12physical
22939629
SPS1_HUMANSEPHS1physical
25416956
QRIC1_HUMANQRICH1physical
25416956
ACADS_HUMANACADSphysical
26344197
CRKL_HUMANCRKLphysical
26344197
DD19A_HUMANDDX19Aphysical
26344197
G6PD_HUMANG6PDphysical
26344197
HSPB1_HUMANHSPB1physical
26344197
MCFD2_HUMANMCFD2physical
26344197
PDCD6_HUMANPDCD6physical
26344197
PUR4_HUMANPFASphysical
26344197
RTCB_HUMANRTCBphysical
26344197
SEC13_HUMANSEC13physical
26344197
SGT1_HUMANSUGT1physical
26344197
EFTU_HUMANTUFMphysical
26344197
WDR12_HUMANWDR12physical
26344197
CDCA4_HUMANCDCA4physical
21516116
SPS1_HUMANSEPHS1physical
21516116
ZBT25_HUMANZBTB25physical
21516116
DEPD7_HUMANDEPDC7physical
21516116
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 SPS1_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-392, AND MASSSPECTROMETRY.

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