S39A8_HUMAN - dbPTM
S39A8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID S39A8_HUMAN
UniProt AC Q9C0K1
Protein Name Zinc transporter ZIP8
Gene Name SLC39A8
Organism Homo sapiens (Human).
Sequence Length 460
Subcellular Localization Membrane
Multi-pass membrane protein . Associated with the lysosomal/endosomal compartment following transfection.
Protein Description Acts as a manganese and zinc influx transporter. [PubMed: 12504855]
Protein Sequence MAPGRAVAGLLLLAAAGLGGVAEGPGLAFSEDVLSVFGANLSLSAAQLQHLLEQMGAASRVGVPEPGQLHFNQCLTAEEIFSLHGFSNATQITSSKFSVICPAVLQQLNFHPCEDRPKHKTRPSHSEVWGYGFLSVTIINLASLLGLILTPLIKKSYFPKILTFFVGLAIGTLFSNAIFQLIPEAFGFDPKVDSYVEKAVAVFGGFYLLFFFERMLKMLLKTYGQNGHTHFGNDNFGPQEKTHQPKALPAINGVTCYANPAVTEANGHIHFDNVSVVSLQDGKKEPSSCTCLKGPKLSEIGTIAWMITLCDALHNFIDGLAIGASCTLSLLQGLSTSIAILCEEFPHELGDFVILLNAGMSTRQALLFNFLSACSCYVGLAFGILVGNNFAPNIIFALAGGMFLYISLADMFPEMNDMLREKVTGRKTDFTFFMIQNAGMLTGFTAILLITLYAGEIELE
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
15 (in isoform 2)Phosphorylation-11.3024043423
20 (in isoform 2)Phosphorylation-22.0924043423
23 (in isoform 2)Phosphorylation-64.6124043423
26 (in isoform 2)Phosphorylation-40.2624043423
27 (in isoform 2)Phosphorylation-4.9724043423
28 (in isoform 2)Phosphorylation-16.3124043423
40N-linked_GlycosylationVLSVFGANLSLSAAQ
HHHHHCCCCCCCHHH		30.46-
88N-linked_GlycosylationFSLHGFSNATQITSS
HHHHCCCCCCCCCCC		44.75-
150PhosphorylationSLLGLILTPLIKKSY
HHHHHHHHHHHHHHC		14.7324719451
255PhosphorylationLPAINGVTCYANPAV
CCCCCCEEEECCHHH		10.9527251275
257PhosphorylationAINGVTCYANPAVTE
CCCCEEEECCHHHEE		10.4727251275
263PhosphorylationCYANPAVTEANGHIH
EECCHHHEECCCEEE		31.3329449344
273N-linked_GlycosylationNGHIHFDNVSVVSLQ
CCEEEECCEEEEECC		27.33UniProtKB CARBOHYD
275PhosphorylationHIHFDNVSVVSLQDG
EEEECCEEEEECCCC		24.0525159151
278PhosphorylationFDNVSVVSLQDGKKE
ECCEEEEECCCCCCC		20.3925159151
284UbiquitinationVSLQDGKKEPSSCTC
EECCCCCCCCCCCEE		79.13-
287PhosphorylationQDGKKEPSSCTCLKG
CCCCCCCCCCEECCC		38.8528122231
288PhosphorylationDGKKEPSSCTCLKGP
CCCCCCCCCEECCCC		24.9421815630
290PhosphorylationKKEPSSCTCLKGPKL
CCCCCCCEECCCCCH		23.8728122231
424PhosphorylationDMLREKVTGRKTDFT
HHHHHHHHCCCCCCE		42.1922817900
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 S39A8_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of S39A8_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 S39A8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TAOK2_HUMANTAOK2physical
28514442
GPDM_HUMANGPD2physical
28514442
RMD2_HUMANRMDN2physical
28514442
SL9A6_HUMANSLC9A6physical
28514442
LEMD2_HUMANLEMD2physical
28514442
C1GLC_HUMANC1GALT1C1physical
28514442
CA043_HUMANC1orf43physical
28514442
ERGI2_HUMANERGIC2physical
28514442
ZDH17_HUMANZDHHC17physical
28514442
EXTL2_HUMANEXTL2physical
28514442
VAPB_HUMANVAPBphysical
28514442
EDA_HUMANEDAphysical
28514442
ST7L_HUMANST7Lphysical
28514442
SGPP1_HUMANSGPP1physical
28514442
MGT5A_HUMANMGAT5physical
28514442
HMOX1_HUMANHMOX1physical
28514442
SPPL3_HUMANSPPL3physical
28514442
STX4_HUMANSTX4physical
28514442
S22AI_HUMANSLC22A18physical
28514442
ERGI3_HUMANERGIC3physical
28514442
T179B_HUMANTMEM179Bphysical
28514442
TMPPE_HUMANTMPPEphysical
28514442
VANG2_HUMANVANGL2physical
28514442
TMX2_HUMANTMX2physical
28514442
B3A2_HUMANSLC4A2physical
28514442
GP1BB_HUMANGP1BBphysical
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 S39A8_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-288, AND MASSSPECTROMETRY.

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