SPNS1_HUMAN - dbPTM
SPNS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPNS1_HUMAN
UniProt AC Q9H2V7
Protein Name Protein spinster homolog 1
Gene Name SPNS1
Organism Homo sapiens (Human).
Sequence Length 528
Subcellular Localization Mitochondrion inner membrane
Multi-pass membrane protein . Colocalizes with SDHB.
Protein Description Sphingolipid transporter (By similarity). May be involved in necrotic or autophagic cell death..
Protein Sequence MAGSDTAPFLSQADDPDDGPVPGTPGLPGSTGNPKSEEPEVPDQEGLQRITGLSPGRSALIVAVLCYINLLNYMDRFTVAGVLPDIEQFFNIGDSSSGLIQTVFISSYMVLAPVFGYLGDRYNRKYLMCGGIAFWSLVTLGSSFIPGEHFWLLLLTRGLVGVGEASYSTIAPTLIADLFVADQRSRMLSIFYFAIPVGSGLGYIAGSKVKDMAGDWHWALRVTPGLGVVAVLLLFLVVREPPRGAVERHSDLPPLNPTSWWADLRALARNPSFVLSSLGFTAVAFVTGSLALWAPAFLLRSRVVLGETPPCLPGDSCSSSDSLIFGLITCLTGVLGVGLGVEISRRLRHSNPRADPLVCATGLLGSAPFLFLSLACARGSIVATYIFIFIGETLLSMNWAIVADILLYVVIPTRRSTAEAFQIVLSHLLGDAGSPYLIGLISDRLRRNWPPSFLSEFRALQFSLMLCAFVGALGGAAFLGTAIFIEADRRRAQLHVQGLLHEAGSTDDRIVVPQRGRSTRVPVASVLI
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------MAGSDTAPF
------CCCCCCCCC
26.6319413330
11PhosphorylationSDTAPFLSQADDPDD
CCCCCCCCCCCCCCC
24.5728122231
24PhosphorylationDDGPVPGTPGLPGST
CCCCCCCCCCCCCCC
14.2325850435
30PhosphorylationGTPGLPGSTGNPKSE
CCCCCCCCCCCCCCC
31.0721955146
31PhosphorylationTPGLPGSTGNPKSEE
CCCCCCCCCCCCCCC
47.0621955146
54PhosphorylationLQRITGLSPGRSALI
HHHHHCCCCCHHHHH
27.0124719451
78 (in isoform 3)Phosphorylation-15.44-
167PhosphorylationVGVGEASYSTIAPTL
CCCCCCCHHCCHHHH
19.5122817900
192PhosphorylationSRMLSIFYFAIPVGS
HHHHHHEEEEEECCC
7.1622817900
203PhosphorylationPVGSGLGYIAGSKVK
ECCCCCHHHCCCCHH
7.8222817900
223PhosphorylationWHWALRVTPGLGVVA
CHHHHHCCCCHHHHH
12.76-
287PhosphorylationFTAVAFVTGSLALWA
CCHHHHHHHHHHHHH
18.01-
301PhosphorylationAPAFLLRSRVVLGET
HHHHHHHCCEECCCC
29.42-
505PhosphorylationGLLHEAGSTDDRIVV
HHHHHCCCCCCEEEE
35.3925849741
506PhosphorylationLLHEAGSTDDRIVVP
HHHHCCCCCCEEEEC
40.7930266825
518PhosphorylationVVPQRGRSTRVPVAS
EECCCCCCCCCCEEE
24.3221712546
519PhosphorylationVPQRGRSTRVPVASV
ECCCCCCCCCCEEEE
34.0321712546
525PhosphorylationSTRVPVASVLI----
CCCCCEEEECC----
20.0724117733

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 SPNS1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPNS1_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 SPNS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCL2_HUMANBCL2physical
12815463
B2CL1_HUMANBCL2L1physical
12815463

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 SPNS1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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-518, AND MASSSPECTROMETRY.

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