F1712_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: F1712_HUMAN
• UniProt AC: A8MVW0
• Protein Name: Protein FAM171A2
• Gene Name: FAM171A2
• Organism: Homo sapiens (Human).
• Sequence Length: 826
• Subcellular Localization: Membrane ; Single-pass type I membrane protein .
• Protein Sequence: MPPASGPSVLARLLPLLGLLLGSASRAPGKSPPEPPSPQEILIKVQVYVSGELVPLARASVDVFGNRTLLAAGTTDSEGVATLPLSYRLGTWVLVTAARPGFLTNSVPWRVDKLPLYASVSLYLLPERPATLILYEDLVHILLGSPGARSQPLVQFQRRAARLPVSSTYSQLWASLTPASTQQEMRAFPAFLGTEASSSGNGSWLELMPLTAVSVHLLTGNGTEVPLSGPIHLSLPVPSETRALTVGTSIPAWRFDPKSGLWVRNGTGVIRKEGRQLYWTFVSPQLGYWVAAMASPTAGLVTITSGIQDIGTYHTIFLLTILAALALLVLILLCLLIYYCRRRCLKPRQQHRKLQLSGPSDGNKRDQATSMSQLHLICGGPLEPAPSGDPEAPPPGPLHSAFSSSRDLASSRDDFFRTKPRSASRPAAEPSGARGGESAGLKGARSAEGPGGLEPGLEEHRRGPSGAAAFLHEPPSPPPPFDHYLGHKGAAEGKTPDFLLSQSVDQLARPPSLGQAGQLIFCGSIDHLKDNVYRNVMPTLVIPAHYVRLGGEAGAAGVGDEPAPPEGTAPGPARAFPQPDPQRPQMPGHSGPGGEGGGGGGEGWGAGRAAPVSGSVTIPVLFNESTMAQLNGELQALTEKKLLELGVKPHPRAWFVSLDGRSNSQVRHSYIDLQAGGGARSTDASLDSGVDVHEARPARRRPAREERERAPPAAPPPPPAPPRLALSEDTEPSSSESRTGLCSPEDNSLTPLLDEVAAPEGRAATVPRGRGRSRGDSSRSSASELRRDSLTSPEDELGAEVGDEAGDKKSPWQRREERPLMVFNVK

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
66	N-linked_Glycosylation	ASVDVFGNRTLLAAG EEEEEECCEEEEECC	23.46	19349973
74	Ubiquitination	RTLLAAGTTDSEGVA EEEEECCCCCCCCCE	23.78	21890473
121	Phosphorylation	LPLYASVSLYLLPER CCCEEEEEEEECCCC	14.59	25332170
201	N-linked_Glycosylation	TEASSSGNGSWLELM CCCCCCCCCCEEEEE	43.18	UniProtKB CARBOHYD
221	N-linked_Glycosylation	SVHLLTGNGTEVPLS EEEEECCCCCCCCCC	49.32	UniProtKB CARBOHYD
258	Ubiquitination	PAWRFDPKSGLWVRN CCEEECCCCCEEEEC	60.03	21890473
265	N-linked_Glycosylation	KSGLWVRNGTGVIRK CCCEEEECCCEEEEE	42.64	UniProtKB CARBOHYD
353	Ubiquitination	KPRQQHRKLQLSGPS CHHHHHHCCCCCCCC	38.16	29901268
357	Phosphorylation	QHRKLQLSGPSDGNK HHHCCCCCCCCCCCH	35.38	20363803
360	Phosphorylation	KLQLSGPSDGNKRDQ CCCCCCCCCCCHHHH	62.77	25002506
369	Phosphorylation	GNKRDQATSMSQLHL CCHHHHCCCHHHEEE	21.23	29116813
370	Phosphorylation	NKRDQATSMSQLHLI CHHHHCCCHHHEEEH	21.32	29116813
372	Phosphorylation	RDQATSMSQLHLICG HHHCCCHHHEEEHHC	29.38	26471730
387	Phosphorylation	GPLEPAPSGDPEAPP CCCCCCCCCCCCCCC	58.91	29116813
400	Phosphorylation	PPPGPLHSAFSSSRD CCCCCCCHHCCCCHH	38.40	29116813
410	Phosphorylation	SSSRDLASSRDDFFR CCCHHHHHCCHHHHC	32.95	30266825
411	Phosphorylation	SSRDLASSRDDFFRT CCHHHHHCCHHHHCC	33.84	30266825
418	Phosphorylation	SRDDFFRTKPRSASR CCHHHHCCCCCCCCC	40.00	24719451
422	Phosphorylation	FFRTKPRSASRPAAE HHCCCCCCCCCCCCC	38.84	28348404
424	Phosphorylation	RTKPRSASRPAAEPS CCCCCCCCCCCCCCC	39.79	23312004
431	Phosphorylation	SRPAAEPSGARGGES CCCCCCCCCCCCCCC	36.27	23312004
446	Phosphorylation	AGLKGARSAEGPGGL CCCCCCCCCCCCCCC	30.09	30266825
476	Phosphorylation	AFLHEPPSPPPPFDH HHCCCCCCCCCCCHH	61.83	29523821
512	Phosphorylation	DQLARPPSLGQAGQL HHHHCCCCCCCCCEE	48.06	-
533	Phosphorylation	DHLKDNVYRNVMPTL HHHHCCCHHHHCCCE	11.61	-
546	Phosphorylation	TLVIPAHYVRLGGEA CEEEECCEEECCCCC	6.86	28796482
648	Ubiquitination	KLLELGVKPHPRAWF HHHHCCCCCCCCEEE	35.49	33845483
657	Phosphorylation	HPRAWFVSLDGRSNS CCCEEEEEECCCCCC	15.98	30576142
662	Phosphorylation	FVSLDGRSNSQVRHS EEEECCCCCCCCEEE	46.49	23312004
664	Phosphorylation	SLDGRSNSQVRHSYI EECCCCCCCCEEEEE	31.16	28555341
669	Phosphorylation	SNSQVRHSYIDLQAG CCCCCEEEEEEEECC	17.14	28796482
670	Phosphorylation	NSQVRHSYIDLQAGG CCCCEEEEEEEECCC	7.73	25884760
730	Phosphorylation	RLALSEDTEPSSSES CCCCCCCCCCCCCCC	45.82	27732954
733	Phosphorylation	LSEDTEPSSSESRTG CCCCCCCCCCCCCCC	40.02	27732954
734	Phosphorylation	SEDTEPSSSESRTGL CCCCCCCCCCCCCCC	49.17	27732954
735	Phosphorylation	EDTEPSSSESRTGLC CCCCCCCCCCCCCCC	43.88	27732954
737	Phosphorylation	TEPSSSESRTGLCSP CCCCCCCCCCCCCCC	36.77	27732954
739	Phosphorylation	PSSSESRTGLCSPED CCCCCCCCCCCCCCC	43.73	29978859
743	Phosphorylation	ESRTGLCSPEDNSLT CCCCCCCCCCCCCCH	36.04	29978859
748	Phosphorylation	LCSPEDNSLTPLLDE CCCCCCCCCHHHHHH	46.04	29978859
750	Phosphorylation	SPEDNSLTPLLDEVA CCCCCCCHHHHHHHC	16.23	29978859
765	Phosphorylation	APEGRAATVPRGRGR CCCCCCCCCCCCCCC	30.02	24719451
780	Phosphorylation	SRGDSSRSSASELRR CCCCCCCCCHHHHHH	32.00	23403867
781	Phosphorylation	RGDSSRSSASELRRD CCCCCCCCHHHHHHH	34.40	24719451
783	Phosphorylation	DSSRSSASELRRDSL CCCCCCHHHHHHHCC	38.83	26699800
789	Phosphorylation	ASELRRDSLTSPEDE HHHHHHHCCCCCHHH	31.56	23401153
791	Phosphorylation	ELRRDSLTSPEDELG HHHHHCCCCCHHHHH	46.30	30266825
792	Phosphorylation	LRRDSLTSPEDELGA HHHHCCCCCHHHHHC	31.42	29255136

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of F1712_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of F1712_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of F1712_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of F1712_HUMAN !!

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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-66, AND MASS SPECTROMETRY.
PubMed: 19349973