CSMD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CSMD1_HUMAN
• UniProt AC: Q96PZ7
• Protein Name: CUB and sushi domain-containing protein 1
• Gene Name: CSMD1
• Organism: Homo sapiens (Human).
• Sequence Length: 3564
• Subcellular Localization: Membrane ; Single-pass type I membrane protein .
• Protein Description: Potential suppressor of squamous cell carcinomas..
• Protein Sequence: MTAWRRFQSLLLLLGLLVLCARLLTAAKGQNCGGLVQGPNGTIESPGFPHGYPNYANCTWIIITGERNRIQLSFHTFALEEDFDILSVYDGQPQQGNLKVRLSGFQLPSSIVSTGSILTLWFTTDFAVSAQGFKALYEVLPSHTCGNPGEILKGVLHGTRFNIGDKIRYSCLPGYILEGHAILTCIVSPGNGASWDFPAPFCRAEGACGGTLRGTSSSISSPHFPSEYENNADCTWTILAEPGDTIALVFTDFQLEEGYDFLEISGTEAPSIWLTGMNLPSPVISSKNWLRLHFTSDSNHRRKGFNAQFQVKKAIELKSRGVKMLPSKDGSHKNSVLSQGGVALVSDMCPDPGIPENGRRAGSDFRVGANVQFSCEDNYVLQGSKSITCQRVTETLAAWSDHRPICRARTCGSNLRGPSGVITSPNYPVQYEDNAHCVWVITTTDPDKVIKLAFEEFELERGYDTLTVGDAGKVGDTRSVLYVLTGSSVPDLIVSMSNQMWLHLQSDDSIGSPGFKAVYQEIEKGGCGDPGIPAYGKRTGSSFLHGDTLTFECPAAFELVGERVITCQQNNQWSGNKPSCVFSCFFNFTASSGIILSPNYPEEYGNNMNCVWLIISEPGSRIHLIFNDFDVEPQFDFLAVKDDGISDITVLGTFSGNEVPSQLASSGHIVRLEFQSDHSTTGRGFNITYTTFGQNECHDPGIPINGRRFGDRFLLGSSVSFHCDDGFVKTQGSESITCILQDGNVVWSSTVPRCEAPCGGHLTASSGVILPPGWPGYYKDSLHCEWIIEAKPGHSIKITFDRFQTEVNYDTLEVRDGPASSSPLIGEYHGTQAPQFLISTGNFMYLLFTTDNSRSSIGFLIHYESVTLESDSCLDPGIPVNGHRHGGDFGIRSTVTFSCDPGYTLSDDEPLVCERNHQWNHALPSCDALCGGYIQGKSGTVLSPGFPDFYPNSLNCTWTIEVSHGKGVQMIFHTFHLESSHDYLLITEDGSFSEPVARLTGSVLPHTIKAGLFGNFTAQLRFISDFSISYEGFNITFSEYDLEPCDDPGVPAFSRRIGFHFGVGDSLTFSCFLGYRLEGATKLTCLGGGRRVWSAPLPRCVAECGASVKGNEGTLLSPNFPSNYDNNHECIYKIETEAGKGIHLRTRSFQLFEGDTLKVYDGKDSSSRPLGTFTKNELLGLILNSTSNHLWLEFNTNGSDTDQGFQLTYTSFDLVKCEDPGIPNYGYRIRDEGHFTDTVVLYSCNPGYAMHGSNTLTCLSGDRRVWDKPLPSCIAECGGQIHAATSGRILSPGYPAPYDNNLHCTWIIEADPGKTISLHFIVFDTEMAHDILKVWDGPVDSDILLKEWSGSALPEDIHSTFNSLTLQFDSDFFISKSGFSIQFSTSIAATCNDPGMPQNGTRYGDSREAGDTVTFQCDPGYQLQGQAKITCVQLNNRFFWQPDPPTCIAACGGNLTGPAGVILSPNYPQPYPPGKECDWRVKVNPDFVIALIFKSFNMEPSYDFLHIYEGEDSNSPLIGSYQGSQAPERIESSGNSLFLAFRSDASVGLSGFAIEFKEKPREACFDPGNIMNGTRVGTDFKLGSTITYQCDSGYKILDPSSITCVIGADGKPSWDQVLPSCNAPCGGQYTGSEGVVLSPNYPHNYTAGQICLYSITVPKEFVVFGQFAYFQTALNDLAELFDGTHAQARLLSSLSGSHSGETLPLATSNQILLRFSAKSGASARGFHFVYQAVPRTSDTQCSSVPEPRYGRRIGSEFSAGSIVRFECNPGYLLQGSTALHCQSVPNALAQWNDTIPSCVVPCSGNFTQRRGTILSPGYPEPYGNNLNCIWKIIVTEGSGIQIQVISFATEQNWDSLEIHDGGDVTAPRLGSFSGTTVPALLNSTSNQLYLHFQSDISVAAAGFHLEYKTVGLAACQEPALPSNSIKIGDRYMVNDVLSFQCEPGYTLQGRSHISCMPGTVRRWNYPSPLCIATCGGTLSTLGGVILSPGFPGSYPNNLDCTWRISLPIGYGAHIQFLNFSTEANHDFLEIQNGPYHTSPMIGQFSGTDLPAALLSTTHETLIHFYSDHSQNRQGFKLAYQAYELQNCPDPPPFQNGYMINSDYSVGQSVSFECYPGYILIGHPVLTCQHGINRNWNYPFPRCDAPCGYNVTSQNGTIYSPGFPDEYPILKDCIWLITVPPGHGVYINFTLLQTEAVNDYIAVWDGPDQNSPQLGVFSGNTALETAYSSTNQVLLKFHSDFSNGGFFVLNFHAFQLKKCQPPPAVPQAEMLTEDDDFEIGDFVKYQCHPGYTLVGTDILTCKLSSQLQFEGSLPTCEAQCPANEVRTGSSGVILSPGYPGNYFNSQTCSWSIKVEPNYNITIFVDTFQSEKQFDALEVFDGSSGQSPLLVVLSGNHTEQSNFTSRSNQLYLRWSTDHATSKKGFKIRYAAPYCSLTHPLKNGGILNRTAGAVGSKVHYFCKPGYRMVGHSNATCRRNPLGMYQWDSLTPLCQAVSCGIPESPGNGSFTGNEFTLDSKVVYECHEGFKLESSQQATAVCQEDGLWSNKGKPPTCKPVACPSIEAQLSEHVIWRLVSGSLNEYGAQVLLSCSPGYYLEGWRLLRCQANGTWNIGDERPSCRVISCGSLSFPPNGNKIGTLTVYGATAIFTCNTGYTLVGSHVRECLANGLWSGSETRCLAGHCGSPDPIVNGHISGDGFSYRDTVVYQCNPGFRLVGTSVRICLQDHKWSGQTPVCVPITCGHPGNPAHGFTNGSEFNLNDVVNFTCNTGYLLQGVSRAQCRSNGQWSSPLPTCRVVNCSDPGFVENAIRHGQQNFPESFEYGMSILYHCKKGFYLLGSSALTCMANGLWDRSLPKCLAISCGHPGVPANAVLTGELFTYGAVVHYSCRGSESLIGNDTRVCQEDSHWSGALPHCTGNNPGFCGDPGTPAHGSRLGDDFKTKSLLRFSCEMGHQLRGSPERTCLLNGSWSGLQPVCEAVSCGNPGTPTNGMIVSSDGILFSSSVIYACWEGYKTSGLMTRHCTANGTWTGTAPDCTIISCGDPGTLANGIQFGTDFTFNKTVSYQCNPGYVMEAVTSATIRCTKDGRWNPSKPVCKAVLCPQPPPVQNGTVEGSDFRWGSSISYSCMDGYQLSHSAILSCEGRGVWKGEIPQCLPVFCGDPGIPAEGRLSGKSFTYKSEVFFQCKSPFILVGSSRRVCQADGTWSGIQPTCIDPAHNTCPDPGTPHFGIQNSSRGYEVGSTVFFRCRKGYHIQGSTTRTCLANLTWSGIQTECIPHACRQPETPAHADVRAIDLPTFGYTLVYTCHPGFFLAGGSEHRTCKADMKWTGKSPVCKSKGVREVNETVTKTPVPSDVFFVNSLWKGYYEYLGKRQPATLTVDWFNATSSKVNATFSEASPVELKLTGIYKKEEAHLLLKAFQIKGQADIFVSKFENDNWGLDGYVSSGLERGGFTFQGDIHGKDFGKFKLERQDPLNPDQDSSSHYHGTSSGSVAAAILVPFFALILSGFAFYLYKHRTRPKVQYNGYAGHENSNGQASFENPMYDTNLKPTEAKAVRFDTTLNTVCTVV

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
9	Phosphorylation	TAWRRFQSLLLLLGL CHHHHHHHHHHHHHH	20.48	-
40	N-linked_Glycosylation	GGLVQGPNGTIESPG CCCCCCCCCCCCCCC	68.04	UniProtKB CARBOHYD
57	N-linked_Glycosylation	HGYPNYANCTWIIIT CCCCCCCCEEEEEEE	17.25	UniProtKB CARBOHYD
109	Phosphorylation	LSGFQLPSSIVSTGS ECCCCCCCCEEECCC	41.09	22210691
113	Phosphorylation	QLPSSIVSTGSILTL CCCCCEEECCCEEEE	25.94	22210691
123	Phosphorylation	SILTLWFTTDFAVSA CEEEEEEECCHHHCC	17.55	22210691
327	Phosphorylation	RGVKMLPSKDGSHKN CCEEECCCCCCCCCC	39.14	24719451
363	Phosphorylation	ENGRRAGSDFRVGAN CCCCCCCCCCEECCE	34.20	22210691
366	Phosphorylation	RRAGSDFRVGANVQF CCCCCCCEECCEEEE	30.92	22210691
375	Phosphorylation	GANVQFSCEDNYVLQ CCEEEEEECCCEEEE	10.25	22210691
536	Phosphorylation	DPGIPAYGKRTGSSF CCCCCCCCCCCCCCC	20.16	-
587	N-linked_Glycosylation	CVFSCFFNFTASSGI EEEEEEEEECCCCCE	9.60	-
588	N-linked_Glycosylation	VFSCFFNFTASSGII EEEEEEEECCCCCEE	17.07	UniProtKB CARBOHYD
655	Phosphorylation	ITVLGTFSGNEVPSQ EEEEEEECCCCCCHH	9.27	24719451
656	Phosphorylation	TVLGTFSGNEVPSQL EEEEEECCCCCCHHH	40.31	24719451
686	N-linked_Glycosylation	STTGRGFNITYTTFG CCCCCEEEEEEEECC	6.03	-
687	N-linked_Glycosylation	TTGRGFNITYTTFGQ CCCCEEEEEEEECCC	28.63	UniProtKB CARBOHYD
690	Phosphorylation	RGFNITYTTFGQNEC CEEEEEEEECCCCCC	10.45	23403867
691	Phosphorylation	GFNITYTTFGQNECH EEEEEEEECCCCCCC	13.65	23403867
692	Phosphorylation	FNITYTTFGQNECHD EEEEEEECCCCCCCC	18.49	23403867
955	N-linked_Glycosylation	DFYPNSLNCTWTIEV CCCCCCCCEEEEEEE	8.51	-
956	N-linked_Glycosylation	FYPNSLNCTWTIEVS CCCCCCCEEEEEEEE	22.46	UniProtKB CARBOHYD
1001	Phosphorylation	EPVARLTGSVLPHTI CCHHHHHCCCCCCEE	23.12	-
1003	Phosphorylation	VARLTGSVLPHTIKA HHHHHCCCCCCEECC	18.42	-
1015	N-linked_Glycosylation	IKAGLFGNFTAQLRF ECCCCCCCEEEEEEE	33.12	-
1016	N-linked_Glycosylation	KAGLFGNFTAQLRFI CCCCCCCEEEEEEEE	24.62	UniProtKB CARBOHYD
1034	N-linked_Glycosylation	SISYEGFNITFSEYD EEEEECEEEEEEECC	3.90	-
1035	N-linked_Glycosylation	ISYEGFNITFSEYDL EEEECEEEEEEECCC	43.16	UniProtKB CARBOHYD
1068	Phosphorylation	FGVGDSLTFSCFLGY ECCCCCEEEEECCCC	7.16	24719451
1069	Phosphorylation	GVGDSLTFSCFLGYR CCCCCEEEEECCCCE	19.90	24719451
1081	Phosphorylation	GYRLEGATKLTCLGG CCEECCCEEEEEECC	7.68	24719451
1082	Phosphorylation	YRLEGATKLTCLGGG CEECCCEEEEEECCC	37.13	24719451
1095	Phosphorylation	GGRRVWSAPLPRCVA CCCEEECCCCCCCCH	19.70	22985185
1184	N-linked_Glycosylation	ELLGLILNSTSNHLW HHHHHHHCCCCCEEE	5.08	-
1185	N-linked_Glycosylation	LLGLILNSTSNHLWL HHHHHHCCCCCEEEE	35.93	UniProtKB CARBOHYD
1197	N-linked_Glycosylation	LWLEFNTNGSDTDQG EEEEEECCCCCCCCC	46.40	-
1198	N-linked_Glycosylation	WLEFNTNGSDTDQGF EEEEECCCCCCCCCE	49.42	UniProtKB CARBOHYD
1399	N-linked_Glycosylation	NDPGMPQNGTRYGDS CCCCCCCCCCCCCCC	52.68	-
1400	N-linked_Glycosylation	DPGMPQNGTRYGDSR CCCCCCCCCCCCCCC	48.18	UniProtKB CARBOHYD
1454	N-linked_Glycosylation	CIAACGGNLTGPAGV EEEECCCCCCCCCEE	26.34	-
1455	N-linked_Glycosylation	IAACGGNLTGPAGVI EEECCCCCCCCCEEE	21.51	UniProtKB CARBOHYD
1572	N-linked_Glycosylation	FDPGNIMNGTRVGTD CCCCCCCCCEEECCC	4.37	-
1573	N-linked_Glycosylation	DPGNIMNGTRVGTDF CCCCCCCCEEECCCC	44.91	UniProtKB CARBOHYD
1644	N-linked_Glycosylation	LSPNYPHNYTAGQIC ECCCCCCCCCCCCEE	29.57	-
1645	N-linked_Glycosylation	SPNYPHNYTAGQICL CCCCCCCCCCCCEEE	31.20	UniProtKB CARBOHYD
1657	Phosphorylation	ICLYSITVPKEFVVF EEEEEEECCHHEEEE	25.47	24719451
1740	Phosphorylation	VPRTSDTQCSSVPEP CCCCCCCCCCCCCCC	31.10	30576142
1743	Phosphorylation	TSDTQCSSVPEPRYG CCCCCCCCCCCCCCC	25.26	30576142
1792	N-linked_Glycosylation	PNALAQWNDTIPSCV CCHHHHCCCCCCCCE	10.08	-
1793	N-linked_Glycosylation	NALAQWNDTIPSCVV CHHHHCCCCCCCCEE	25.19	UniProtKB CARBOHYD
1805	N-linked_Glycosylation	CVVPCSGNFTQRRGT CEEECCCCCCCCCCC	39.73	-
1806	N-linked_Glycosylation	VVPCSGNFTQRRGTI EEECCCCCCCCCCCE	22.09	UniProtKB CARBOHYD
1813	Phosphorylation	FTQRRGTILSPGYPE CCCCCCCEECCCCCC	19.55	25247763
1882	N-linked_Glycosylation	TTVPALLNSTSNQLY CCHHHHHCCCCCCEE	5.30	-
1883	N-linked_Glycosylation	TVPALLNSTSNQLYL CHHHHHCCCCCCEEE	44.05	UniProtKB CARBOHYD
2018	N-linked_Glycosylation	GAHIQFLNFSTEANH CCEEEEEECCCCCCC	3.47	-
2019	N-linked_Glycosylation	AHIQFLNFSTEANHD CEEEEEECCCCCCCC	30.06	UniProtKB CARBOHYD
2149	N-linked_Glycosylation	CDAPCGYNVTSQNGT CCCCCCCCCCCCCCE	17.12	-
2150	N-linked_Glycosylation	DAPCGYNVTSQNGTI CCCCCCCCCCCCCEE	18.84	UniProtKB CARBOHYD
2154	N-linked_Glycosylation	GYNVTSQNGTIYSPG CCCCCCCCCEEECCC	42.90	-
2155	N-linked_Glycosylation	YNVTSQNGTIYSPGF CCCCCCCCEEECCCC	49.71	UniProtKB CARBOHYD
2187	N-linked_Glycosylation	PGHGVYINFTLLQTE CCCCEEEEEEEEEEC	2.96	-
2188	N-linked_Glycosylation	GHGVYINFTLLQTEA CCCEEEEEEEEEECC	13.23	UniProtKB CARBOHYD
2358	N-linked_Glycosylation	IKVEPNYNITIFVDT EEEECCCEEEEEEEC	20.75	-
2359	N-linked_Glycosylation	KVEPNYNITIFVDTF EEECCCEEEEEEECC	31.41	UniProtKB CARBOHYD
2394	N-linked_Glycosylation	LLVVLSGNHTEQSNF EEEEECCCCCCCCCC	26.27	-
2395	N-linked_Glycosylation	LVVLSGNHTEQSNFT EEEECCCCCCCCCCC	35.22	UniProtKB CARBOHYD
2397	Phosphorylation	VLSGNHTEQSNFTSR EECCCCCCCCCCCCC	39.45	30576142
2400	N-linked_Glycosylation	GNHTEQSNFTSRSNQ CCCCCCCCCCCCCCE	27.90	-
2401	N-linked_Glycosylation	NHTEQSNFTSRSNQL CCCCCCCCCCCCCEE	43.86	UniProtKB CARBOHYD
2403	Phosphorylation	TEQSNFTSRSNQLYL CCCCCCCCCCCEEEE	27.73	30576142
2404	Phosphorylation	EQSNFTSRSNQLYLR CCCCCCCCCCEEEEE	29.58	30576142
2406	Phosphorylation	SNFTSRSNQLYLRWS CCCCCCCCEEEEEEE	28.79	30177828
2410	Phosphorylation	SRSNQLYLRWSTDHA CCCCEEEEEEECCCC	5.62	30177828
2414	Phosphorylation	QLYLRWSTDHATSKK EEEEEEECCCCCCCC	19.95	30177828
2415	Phosphorylation	LYLRWSTDHATSKKG EEEEEECCCCCCCCC	25.50	30177828
2419	Phosphorylation	WSTDHATSKKGFKIR EECCCCCCCCCCEEE	37.34	30177828
2420	Phosphorylation	STDHATSKKGFKIRY ECCCCCCCCCCEEEE	32.90	30177828
2445	N-linked_Glycosylation	LKNGGILNRTAGAVG CCCCCCCCCCCCCCC	3.92	-
2446	N-linked_Glycosylation	KNGGILNRTAGAVGS CCCCCCCCCCCCCCC	37.02	UniProtKB CARBOHYD
2470	N-linked_Glycosylation	YRMVGHSNATCRRNP CCCCCCCCCCCCCCC	23.41	-
2471	N-linked_Glycosylation	RMVGHSNATCRRNPL CCCCCCCCCCCCCCC	33.33	UniProtKB CARBOHYD
2503	N-linked_Glycosylation	GIPESPGNGSFTGNE CCCCCCCCCCCCCCE	61.48	-
2504	N-linked_Glycosylation	IPESPGNGSFTGNEF CCCCCCCCCCCCCEE	46.44	UniProtKB CARBOHYD
2605	N-linked_Glycosylation	RLLRCQANGTWNIGD EEEEEECCCCEECCC	21.75	-
2606	N-linked_Glycosylation	LLRCQANGTWNIGDE EEEEECCCCEECCCC	23.65	UniProtKB CARBOHYD
2617	Phosphorylation	IGDERPSCRVISCGS CCCCCCCEEEEEECC	22.30	30631047
2625	Phosphorylation	RVISCGSLSFPPNGN EEEEECCEECCCCCC	25.76	30631047
2627	Phosphorylation	ISCGSLSFPPNGNKI EEECCEECCCCCCCE	37.09	30631047
2750	N-linked_Glycosylation	NPAHGFTNGSEFNLN CCCCCCCCCCCCCHH	43.17	-
2751	N-linked_Glycosylation	PAHGFTNGSEFNLND CCCCCCCCCCCCHHH	50.13	UniProtKB CARBOHYD
2761	N-linked_Glycosylation	FNLNDVVNFTCNTGY CCHHHEEEEEECCCH	5.63	-
2762	N-linked_Glycosylation	NLNDVVNFTCNTGYL CHHHEEEEEECCCHH	26.76	UniProtKB CARBOHYD
2795	N-linked_Glycosylation	LPTCRVVNCSDPGFV CCCEEEEECCCCCHH	2.86	-
2796	N-linked_Glycosylation	PTCRVVNCSDPGFVE CCEEEEECCCCCHHH	19.40	UniProtKB CARBOHYD
2851	Phosphorylation	NGLWDRSLPKCLAIS CCHHCCCCCCEEECC	46.69	24719451
2894	N-linked_Glycosylation	GSESLIGNDTRVCQE CCCHHCCCCCEECCC	31.11	-
2895	N-linked_Glycosylation	SESLIGNDTRVCQED CCHHCCCCCEECCCC	40.25	UniProtKB CARBOHYD
2897	Phosphorylation	SLIGNDTRVCQEDSH HHCCCCCEECCCCCC	29.06	-
2941	Phosphorylation	DDFKTKSLLRFSCEM CCCCCHHHHHHHHHH	37.56	24719451
2963	N-linked_Glycosylation	PERTCLLNGSWSGLQ CCCEEEECCCCCCCC	8.09	-
2964	N-linked_Glycosylation	ERTCLLNGSWSGLQP CCEEEECCCCCCCCC	29.51	UniProtKB CARBOHYD
3022	N-linked_Glycosylation	MTRHCTANGTWTGTA EEEEEECCCCEEECC	20.18	-
3023	N-linked_Glycosylation	TRHCTANGTWTGTAP EEEEECCCCEEECCC	30.21	UniProtKB CARBOHYD
3056	N-linked_Glycosylation	FGTDFTFNKTVSYQC ECCCCEECCEEEEEC	9.97	-
3057	N-linked_Glycosylation	GTDFTFNKTVSYQCN CCCCEECCEEEEECC	35.71	UniProtKB CARBOHYD
3062	Phosphorylation	FNKTVSYQCNPGYVM ECCEEEEECCCCCEE	16.85	30576142
3074	Phosphorylation	YVMEAVTSATIRCTK CEEEEEEEEEEEECC	21.49	22210691
3075	Phosphorylation	VMEAVTSATIRCTKD EEEEEEEEEEEECCC	19.47	22210691
3105	N-linked_Glycosylation	PQPPPVQNGTVEGSD CCCCCCCCCEECCCC	48.70	-
3106	N-linked_Glycosylation	QPPPVQNGTVEGSDF CCCCCCCCEECCCCC	48.62	UniProtKB CARBOHYD
3184	Phosphorylation	VFFQCKSPFILVGSS EEEEECCCEEEEECC	32.44	23403867
3191	Phosphorylation	PFILVGSSRRVCQAD CEEEEECCCCEEECC	17.13	-
3192	Phosphorylation	FILVGSSRRVCQADG EEEEECCCCEEECCC	20.41	23403867
3228	N-linked_Glycosylation	TPHFGIQNSSRGYEV CCCCCEECCCCCEEE	44.10	-
3229	N-linked_Glycosylation	PHFGIQNSSRGYEVG CCCCEECCCCCEEEC	39.78	UniProtKB CARBOHYD
3260	N-linked_Glycosylation	TTRTCLANLTWSGIQ CCEEEEEECCCCCCC	15.90	-
3261	N-linked_Glycosylation	TRTCLANLTWSGIQT CEEEEEECCCCCCCC	25.67	UniProtKB CARBOHYD
3339	N-linked_Glycosylation	SKGVREVNETVTKTP CCCCEEECCCCCCCC	5.70	-
3340	N-linked_Glycosylation	KGVREVNETVTKTPV CCCEEECCCCCCCCC	34.17	UniProtKB CARBOHYD
3379	N-linked_Glycosylation	TLTVDWFNATSSKVN EEEEEEEECCCCCEE	3.74	-
3380	N-linked_Glycosylation	LTVDWFNATSSKVNA EEEEEEECCCCCEEE	37.75	UniProtKB CARBOHYD
3386	N-linked_Glycosylation	NATSSKVNATFSEAS ECCCCCEEEEECCCC	6.78	-
3387	N-linked_Glycosylation	ATSSKVNATFSEASP CCCCCEEEEECCCCC	36.68	UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of CSMD1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CSMD1_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 CSMD1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of CSMD1_HUMAN !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.