CUBN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CUBN_HUMAN
• UniProt AC: O60494
• Protein Name: Cubilin
• Gene Name: CUBN
• Organism: Homo sapiens (Human).
• Sequence Length: 3623
• Subcellular Localization: Apical cell membrane ; Peripheral membrane protein . Cell membrane ; Peripheral membrane protein . Membrane, coated pit . Endosome . Lysosome membrane; Peripheral membrane protein. Colocalizes with AMN and LRP2 in the endocytotic apparatus of epithel
• Protein Description: Cotransporter which plays a role in lipoprotein, vitamin and iron metabolism, by facilitating their uptake. Binds to ALB, MB, Kappa and lambda-light chains, TF, hemoglobin, GC, SCGB1A1, APOA1, high density lipoprotein, and the GIF-cobalamin complex. The binding of all ligands requires calcium. Serves as important transporter in several absorptive epithelia, including intestine, renal proximal tubules and embryonic yolk sac. Interaction with LRP2 mediates its trafficking throughout vesicles and facilitates the uptake of specific ligands like GC, hemoglobin, ALB, TF and SCGB1A1. Interaction with AMN controls its trafficking to the plasma membrane and facilitates endocytosis of ligands. May play an important role in the development of the peri-implantation embryo through internalization of APOA1 and cholesterol. Binds to LGALS3 at the maternal-fetal interface..
• Protein Sequence: MMNMSLPFLWSLLTLLIFAEVNGEAGELELQRQKRSINLQQPRMATERGNLVFLTGSAQNIEFRTGSLGKIKLNDEDLSECLHQIQKNKEDIIELKGSAIGLPQNISSQIYQLNSKLVDLERKFQGLQQTVDKKVCSSNPCQNGGTCLNLHDSFFCICPPQWKGPLCSADVNECEIYSGTPLSCQNGGTCVNTMGSYSCHCPPETYGPQCASKYDDCEGGSVARCVHGICEDLMREQAGEPKYSCVCDAGWMFSPNSPACTLDRDECSFQPGPCSTLVQCFNTQGSFYCGACPTGWQGNGYICEDINECEINNGGCSVAPPVECVNTPGSSHCQACPPGYQGDGRVCTLTDICSVSNGGCHPDASCSSTLGSLPLCTCLPGYTGNGYGPNGCVQLSNICLSHPCLNGQCIDTVSGYFCKCDSGWTGVNCTENINECLSNPCLNGGTCVDGVDSFSCECTRLWTGALCQVPQQVCGESLSGINGSFSYRSPDVGYVHDVNCFWVIKTEMGKVLRITFTFFRLESMDNCPHEFLQVYDGDSSSAFQLGRFCGSSLPHELLSSDNALYFHLYSEHLRNGRGFTVRWETQQPECGGILTGPYGSIKSPGYPGNYPPGRDCVWIVVTSPDLLVTFTFGTLSLEHHDDCNKDYLEIRDGPLYQDPLLGKFCTTFSVPPLQTTGPFARIHFHSDSQISDQGFHITYLTSPSDLRCGGNYTDPEGELFLPELSGPFTHTRQCVYMMKQPQGEQIQINFTHVELQCQSDSSQNYIEVRDGETLLGKVCGNGTISHIKSITNSVWIRFKIDASVEKASFRAVYQVACGDELTGEGVIRSPFFPNVYPGERTCRWTIHQPQSQVILLNFTVFEIGSSAHCETDYVEIGSSSILGSPENKKYCGTDIPSFITSVYNFLYVTFVKSSSTENHGFMAKFSAEDLACGEILTESTGTIQSPGHPNVYPHGINCTWHILVQPNHLIHLMFETFHLEFHYNCTNDYLEVYDTDSETSLGRYCGKSIPPSLTSSGNSLMLVFVTDSDLAYEGFLINYEAISAATACLQDYTDDLGTFTSPNFPNNYPNNWECIYRITVRTGQLIAVHFTNFSLEEAIGNYYTDFLEIRDGGYEKSPLLGIFYGSNLPPTIISHSNKLWLKFKSDQIDTRSGFSAYWDGSSTGCGGNLTTSSGTFISPNYPMPYYHSSECYWWLKSSHGSAFELEFKDFHLEHHPNCTLDYLAVYDGPSSNSHLLTQLCGDEKPPLIRSSGDSMFIKLRTDEGQQGRGFKAEYRQTCENVVIVNQTYGILESIGYPNPYSENQHCNWTIRATTGNTVNYTFLAFDLEHHINCSTDYLELYDGPRQMGRYCGVDLPPPGSTTSSKLQVLLLTDGVGRREKGFQMQWFVYGCGGELSGATGSFSSPGFPNRYPPNKECIWYIRTDPGSSIQLTIHDFDVEYHSRCNFDVLEIYGGPDFHSPRIAQLCTQRSPENPMQVSSTGNELAIRFKTDLSINGRGFNASWQAVTGGCGGIFQAPSGEIHSPNYPSPYRSNTDCSWVIRVDRNHRVLLNFTDFDLEPQDSCIMAYDGLSSTMSRLARTCGREQLANPIVSSGNSLFLRFQSGPSRQNRGFRAQFRQACGGHILTSSFDTVSSPRFPANYPNNQNCSWIIQAQPPLNHITLSFTHFELERSTTCARDFVEILDGGHEDAPLRGRYCGTDMPHPITSFSSALTLRFVSDSSISAGGFHTTVTASVSACGGTFYMAEGIFNSPGYPDIYPPNVECVWNIVSSPGNRLQLSFISFQLEDSQDCSRDFVEIREGNATGHLVGRYCGNSFPLNYSSIVGHTLWVRFISDGSGSGTGFQATFMKIFGNDNIVGTHGKVASPFWPENYPHNSNYQWTVNVNASHVVHGRILEMDIEEIQNCYYDKLRIYDGPSIHARLIGAYCGTQTESFSSTGNSLTFHFYSDSSISGKGFLLEWFAVDAPDGVLPTIAPGACGGFLRTGDAPVFLFSPGWPDSYSNRVDCTWLIQAPDSTVELNILSLDIESHRTCAYDSLVIRDGDNNLAQQLAVLCGREIPGPIRSTGEYMFIRFTSDSSVTRAGFNASFHKSCGGYLHADRGIITSPKYPETYPSNLNCSWHVLVQSGLTIAVHFEQPFQIPNGDSSCNQGDYLVLRNGPDICSPPLGPPGGNGHFCGSHASSTLFTSDNQMFVQFISDHSNEGQGFKIKYEAKSLACGGNVYIHDADSAGYVTSPNHPHNYPPHADCIWILAAPPETRIQLQFEDRFDIEVTPNCTSNYLELRDGVDSDAPILSKFCGTSLPSSQWSSGEVMYLRFRSDNSPTHVGFKAKYSIAQCGGRVPGQSGVVESIGHPTLPYRDNLFCEWHLQGLSGHYLTISFEDFNLQNSSGCEKDFVEIWDNHTSGNILGRYCGNTIPDSIDTSSNTAVVRFVTDGSVTASGFRLRFESSMEECGGDLQGSIGTFTSPNYPNPNPHGRICEWRITAPEGRRITLMFNNLRLATHPSCNNEHVIVFNGIRSNSPQLEKLCSSVNVSNEIKSSGNTMKVIFFTDGSRPYGGFTASYTSSEDAVCGGSLPNTPEGNFTSPGYDGVRNYSRNLNCEWTLSNPNQGNSSISIHFEDFYLESHQDCQFDVLEFRVGDADGPLMWRLCGPSKPTLPLVIPYSQVWIHFVTNERVEHIGFHAKYSFTDCGGIQIGDSGVITSPNYPNAYDSLTHCSSLLEAPQGHTITLTFSDFDIEPHTTCAWDSVTVRNGGSPESPIIGQYCGNSNPRTIQSGSNQLVVTFNSDHSLQGGGFYATWNTQTLGCGGIFHSDNGTIRSPHWPQNFPENSRCSWTAITHKSKHLEISFDNNFLIPSGDGQCQNSFVKVWAGTEEVDKALLATGCGNVAPGPVITPSNTFTAVFQSQEAPAQGFSASFVSRCGSNFTGPSGYIISPNYPKQYDNNMNCTYVIEANPLSVVLLTFVSFHLEARSAVTGSCVNDGVHIIRGYSVMSTPFATVCGDEMPAPLTIAGPVLLNFYSNEQITDFGFKFSYRIISCGGVFNFSSGIITSPAYSYADYPNDMHCLYTITVSDDKVIELKFSDFDVVPSTSCSHDYLAIYDGANTSDPLLGKFCGSKRPPNVKSSNNSMLLVFKTDSFQTAKGWKMSFRQTLGPQQGCGGYLTGSNNTFASPDSDSNGMYDKNLNCVWIIIAPVNKVIHLTFNTFALEAASTRQRCLYDYVKLYDGDSENANLAGTFCGSTVPAPFISSGNFLTVQFISDLTLEREGFNATYTIMDMPCGGTYNATWTPQNISSPNSSDPDVPFSICTWVIDSPPHQQVKITVWALQLTSQDCTQNYLQLQDSPQGHGNSRFQFCGRNASAVPVFYSSMSTAMVIFKSGVVNRNSRMSFTYQIADCNRDYHKAFGNLRSPGWPDNYDNDKDCTVTLTAPQNHTISLFFHSLGIENSVECRNDFLEVRNGSNSNSPLLGKYCGTLLPNPVFSQNNELYLRFKSDSVTSDRGYEIIWTSSPSGCGGTLYGDRGSFTSPGYPGTYPNNTYCEWVLVAPAGRLVTINFYFISIDDPGDCVQNYLTLYDGPNASSPSSGPYCGGDTSIAPFVASSNQVFIKFHADYARRPSAFRLTWDS

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
3	N-linked_Glycosylation	-----MMNMSLPFLW -----CCCCCHHHHH	28.84	UniProtKB CARBOHYD
105	N-linked_Glycosylation	SAIGLPQNISSQIYQ CCCCCCCCHHHHHHH	33.88	UniProtKB CARBOHYD
107	Phosphorylation	IGLPQNISSQIYQLN CCCCCCHHHHHHHHH	24.60	-
108	Phosphorylation	GLPQNISSQIYQLNS CCCCCHHHHHHHHHH	19.46	-
111	Phosphorylation	QNISSQIYQLNSKLV CCHHHHHHHHHHHHH	10.18	-
115	Phosphorylation	SQIYQLNSKLVDLER HHHHHHHHHHHHHHH	35.64	-
130	Phosphorylation	KFQGLQQTVDKKVCS HHCHHHHHCCHHHHC	20.08	28102081
428	N-linked_Glycosylation	DSGWTGVNCTENINE CCCCCCCCCCCCHHH	28.47	UniProtKB CARBOHYD
482	N-linked_Glycosylation	GESLSGINGSFSYRS CCCCCCCCCCCCCCC	43.51	UniProtKB CARBOHYD
669	Phosphorylation	GKFCTTFSVPPLQTT CCCCCEEECCCCCCC	31.46	-
688	O-linked_Glycosylation	RIHFHSDSQISDQGF EEEEECCCCCCCCCE	32.21	OGP
711	N-linked_Glycosylation	SDLRCGGNYTDPEGE HHCCCCCCCCCCCCC	23.09	UniProtKB CARBOHYD
736	Phosphorylation	THTRQCVYMMKQPQG CCCEEEEEEEECCCC	10.10	24043423
749	N-linked_Glycosylation	QGEQIQINFTHVELQ CCCEEEEEEEEEEEE	21.27	UniProtKB CARBOHYD
781	N-linked_Glycosylation	LLGKVCGNGTISHIK EEEEECCCCCHHHEE	39.03	UniProtKB CARBOHYD
791	Phosphorylation	ISHIKSITNSVWIRF HHHEEECCCEEEEEE	28.65	25690035
793	Phosphorylation	HIKSITNSVWIRFKI HEEECCCEEEEEEEE	15.35	25690035
803	Phosphorylation	IRFKIDASVEKASFR EEEEECCCCCHHHEE	27.36	24719451
857	N-linked_Glycosylation	QSQVILLNFTVFEIG CCEEEEEEEEEEEEC	27.39	UniProtKB CARBOHYD
890	Phosphorylation	GSPENKKYCGTDIPS CCCCCCCCCCCCHHH	9.56	23663014
893	Phosphorylation	ENKKYCGTDIPSFIT CCCCCCCCCHHHHHH	27.48	23663014
897	Phosphorylation	YCGTDIPSFITSVYN CCCCCHHHHHHHHHH	29.61	23663014
900	Phosphorylation	TDIPSFITSVYNFLY CCHHHHHHHHHHHHE	15.32	23663014
901	Phosphorylation	DIPSFITSVYNFLYV CHHHHHHHHHHHHEE	20.14	23663014
903	Phosphorylation	PSFITSVYNFLYVTF HHHHHHHHHHHEEEE	10.44	23663014
907	Phosphorylation	TSVYNFLYVTFVKSS HHHHHHHEEEEECCC	8.03	23663014
909	Phosphorylation	VYNFLYVTFVKSSST HHHHHEEEEECCCCC	14.78	23663014
913	Phosphorylation	LYVTFVKSSSTENHG HEEEEECCCCCCCCC	24.99	23663014
914	Phosphorylation	YVTFVKSSSTENHGF EEEEECCCCCCCCCE	35.25	23663014
915	Phosphorylation	VTFVKSSSTENHGFM EEEECCCCCCCCCEE	47.00	23663014
916	Phosphorylation	TFVKSSSTENHGFMA EEECCCCCCCCCEEE	42.63	23663014
957	N-linked_Glycosylation	NVYPHGINCTWHILV CCCCCCCEEEEEEEE	23.04	UniProtKB CARBOHYD
984	N-linked_Glycosylation	FHLEFHYNCTNDYLE EEEEEEECCCCCCEE	19.98	20237569
1079	Phosphorylation	WECIYRITVRTGQLI CEEEEEEEEECCCEE	8.57	-
1092	N-linked_Glycosylation	LIAVHFTNFSLEEAI EEEEEEECCCHHHHH	24.46	20237569
1168	N-linked_Glycosylation	SSTGCGGNLTTSSGT CCCCCCCCEECCCCE	21.35	20237569
1217	N-linked_Glycosylation	FHLEHHPNCTLDYLA EEHHCCCCCEEEEEE	27.35	20237569
1285	N-linked_Glycosylation	CENVVIVNQTYGILE CCCEEEEECCEEHHH	19.83	20237569
1307	N-linked_Glycosylation	YSENQHCNWTIRATT CCCCCCCCEEEEECC	36.48	20237569
1319	N-linked_Glycosylation	ATTGNTVNYTFLAFD ECCCCCEEEEEEEEE	28.26	20237569
1332	N-linked_Glycosylation	FDLEHHINCSTDYLE EEHHHEECCCCCCEE	14.88	20237569
1350	Phosphorylation	GPRQMGRYCGVDLPP CCCCCCCCCCCCCCC	6.45	24043423
1360	Phosphorylation	VDLPPPGSTTSSKLQ CCCCCCCCCCCCCEE	34.00	22210691
1361	Phosphorylation	DLPPPGSTTSSKLQV CCCCCCCCCCCCEEE	36.29	24043423
1362	Phosphorylation	LPPPGSTTSSKLQVL CCCCCCCCCCCEEEE	32.47	24043423
1363	Phosphorylation	PPPGSTTSSKLQVLL CCCCCCCCCCEEEEE	26.09	24043423
1364	Phosphorylation	PPGSTTSSKLQVLLL CCCCCCCCCEEEEEE	34.98	24043423
1372	Phosphorylation	KLQVLLLTDGVGRRE CEEEEEEECCCCCCC	30.58	22210691
1500	N-linked_Glycosylation	SINGRGFNASWQAVT EECCCCEEEEEEEHH	35.57	UniProtKB CARBOHYD
1551	N-linked_Glycosylation	RNHRVLLNFTDFDLE CCCEEEEEECCCCCC	33.34	UniProtKB CARBOHYD
1646	N-linked_Glycosylation	ANYPNNQNCSWIIQA CCCCCCCCCEEEEEE	24.74	UniProtKB CARBOHYD
1802	N-linked_Glycosylation	FVEIREGNATGHLVG EEEEECCCCCCCEEE	29.58	UniProtKB CARBOHYD
1819	N-linked_Glycosylation	CGNSFPLNYSSIVGH CCCCCCCCHHHCCCC	34.57	UniProtKB CARBOHYD
1885	N-linked_Glycosylation	YQWTVNVNASHVVHG CEEEEEECCHHEEEC	30.44	UniProtKB CARBOHYD
1909	"N6,N6-dimethyllysine"	IQNCYYDKLRIYDGP HHHHHHCCCEECCCC	24.44	-
1909	Methylation	IQNCYYDKLRIYDGP HHHHHHCCCEECCCC	24.44	23644510
1972	O-linked_Glycosylation	APDGVLPTIAPGACG CCCCCCCCCCCCCCC	26.13	OGP
2075	Phosphorylation	YMFIRFTSDSSVTRA EEEEEEECCCCCCCC	32.55	-
2077	Phosphorylation	FIRFTSDSSVTRAGF EEEEECCCCCCCCCC	26.86	-
2078	Phosphorylation	IRFTSDSSVTRAGFN EEEECCCCCCCCCCC	32.28	-
2085	N-linked_Glycosylation	SVTRAGFNASFHKSC CCCCCCCCEEEHHHH	33.48	UniProtKB CARBOHYD
2108	Phosphorylation	GIITSPKYPETYPSN CCEECCCCCCCCCCC	15.08	-
2117	N-linked_Glycosylation	ETYPSNLNCSWHVLV CCCCCCCCCEEEEEE	23.25	UniProtKB CARBOHYD
2274	N-linked_Glycosylation	FDIEVTPNCTSNYLE CCEECCCCCCCCCEE	32.12	UniProtKB CARBOHYD
2304	Phosphorylation	CGTSLPSSQWSSGEV CCCCCCHHHCCCCCE	33.46	24114839
2307	Phosphorylation	SLPSSQWSSGEVMYL CCCHHHCCCCCEEEE	22.34	24114839
2386	N-linked_Glycosylation	FEDFNLQNSSGCEKD EECCCCCCCCCCCCC	41.11	UniProtKB CARBOHYD
2400	N-linked_Glycosylation	DFVEIWDNHTSGNIL CEEEEECCCCCCCCC	25.91	UniProtKB CARBOHYD
2483	Phosphorylation	RICEWRITAPEGRRI CCEEEEEECCCCCCE	27.82	24719451
2531	N-linked_Glycosylation	EKLCSSVNVSNEIKS HHHHHCCCCCHHHHC	33.19	UniProtKB CARBOHYD
2581	N-linked_Glycosylation	LPNTPEGNFTSPGYD CCCCCCCCCCCCCCC	35.05	UniProtKB CARBOHYD
2592	N-linked_Glycosylation	PGYDGVRNYSRNLNC CCCCCCHHCCCCCCC	36.40	UniProtKB CARBOHYD
2610	N-linked_Glycosylation	LSNPNQGNSSISIHF ECCCCCCCCEEEEEE	23.87	UniProtKB CARBOHYD
2748	Phosphorylation	TCAWDSVTVRNGGSP EEEEECEEEECCCCC	20.07	24719451
2813	N-linked_Glycosylation	GGIFHSDNGTIRSPH CCEEECCCCCCCCCC	53.15	UniProtKB CARBOHYD
2904	O-linked_Glycosylation	TFTAVFQSQEAPAQG CEEEEECCCCCCCCC	20.65	OGP
2923	N-linked_Glycosylation	FVSRCGSNFTGPSGY HHHCCCCCCCCCCCE	24.63	UniProtKB CARBOHYD
2945	N-linked_Glycosylation	KQYDNNMNCTYVIEA CCCCCCCCEEEEEEC	19.66	UniProtKB CARBOHYD
3008	Phosphorylation	DEMPAPLTIAGPVLL CCCCCCCEEECCEEE	14.02	-
3042	N-linked_Glycosylation	ISCGGVFNFSSGIIT EECCCCEECCCCEEE	33.22	UniProtKB CARBOHYD
3103	N-linked_Glycosylation	LAIYDGANTSDPLLG EEEECCCCCCCCCHH	45.72	UniProtKB CARBOHYD
3115	Phosphorylation	LLGKFCGSKRPPNVK CHHHHCCCCCCCCCC	27.03	-
3125	N-linked_Glycosylation	PPNVKSSNNSMLLVF CCCCCCCCCCEEEEE	52.25	UniProtKB CARBOHYD
3127	Phosphorylation	NVKSSNNSMLLVFKT CCCCCCCCEEEEEEC	18.30	23532336
3134	Phosphorylation	SMLLVFKTDSFQTAK CEEEEEECCCCCCCC	25.97	23532336
3139	Phosphorylation	FKTDSFQTAKGWKMS EECCCCCCCCCEEEE	28.46	-
3146	Phosphorylation	TAKGWKMSFRQTLGP CCCCEEEEEECCCCC	17.35	24719451
3165	N-linked_Glycosylation	GGYLTGSNNTFASPD CCEECCCCCCCCCCC	53.56	UniProtKB CARBOHYD
3223	Phosphorylation	LYDYVKLYDGDSENA HHEEEEECCCCCCCC	16.50	19845377
3235	Phosphorylation	ENANLAGTFCGSTVP CCCCCCCCCCCCCCC	15.33	19845377
3240	Phosphorylation	AGTFCGSTVPAPFIS CCCCCCCCCCCCCCC	18.78	19845377
3261	Phosphorylation	VQFISDLTLEREGFN EEEEEECEECCCCCC	31.40	19845377
3268	N-linked_Glycosylation	TLEREGFNATYTIMD EECCCCCCEEEEEEE	42.08	UniProtKB CARBOHYD
3283	N-linked_Glycosylation	MPCGGTYNATWTPQN CCCCCEEECCCCCCC	30.63	UniProtKB CARBOHYD
3290	N-linked_Glycosylation	NATWTPQNISSPNSS ECCCCCCCCCCCCCC	36.99	UniProtKB CARBOHYD
3295	N-linked_Glycosylation	PQNISSPNSSDPDVP CCCCCCCCCCCCCCC	56.97	UniProtKB CARBOHYD
3357	N-linked_Glycosylation	RFQFCGRNASAVPVF CCEECCCCCCCCCEE	24.43	UniProtKB CARBOHYD
3430	N-linked_Glycosylation	VTLTAPQNHTISLFF EEEECCCCCEEEEEE	32.96	UniProtKB CARBOHYD
3457	N-linked_Glycosylation	NDFLEVRNGSNSNSP CCCEEECCCCCCCCC	64.52	UniProtKB CARBOHYD
3486	Phosphorylation	FSQNNELYLRFKSDS CCCCCEEEEEEECCC	6.94	-
3491	Phosphorylation	ELYLRFKSDSVTSDR EEEEEEECCCCCCCC	32.19	-
3493	Phosphorylation	YLRFKSDSVTSDRGY EEEEECCCCCCCCCC	34.09	-
3495	Phosphorylation	RFKSDSVTSDRGYEI EEECCCCCCCCCCEE	28.94	-
3500	Phosphorylation	SVTSDRGYEIIWTSS CCCCCCCCEEEEECC	12.59	-
3509	Phosphorylation	IIWTSSPSGCGGTLY EEEECCCCCCCCCCC	48.97	-
3516	Phosphorylation	SGCGGTLYGDRGSFT CCCCCCCCCCCCCCC	19.47	-
3533	N-linked_Glycosylation	GYPGTYPNNTYCEWV CCCCCCCCCCEEEEE	42.96	UniProtKB CARBOHYD
3576	N-linked_Glycosylation	LTLYDGPNASSPSSG EEEECCCCCCCCCCC	58.97	UniProtKB CARBOHYD
3591	O-linked_Glycosylation	PYCGGDTSIAPFVAS CCCCCCCCCCCEEEC	22.84	OGP

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CUBN_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 CUBN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IF_HUMAN	GIF	physical	9572993
CUBN_HUMAN	CUBN	physical	20237569
LRP1_HUMAN	LRP1	physical	17124247
PCLI1_HUMAN	PID1	physical	17124247

Drug and Disease Associations

• Kegg Disease
• H01277: Vitamin B12 deficiency anaemia, including: Hereditary intrinsic factor deficiency (IFD); Imerslund-G
• OMIM Disease
• 261100: Recessive hereditary megaloblastic anemia 1 (RH-MGA1)
• 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

"Structural basis for receptor recognition of vitamin-B(12)-intrinsicfactor complexes.";
Andersen C.B., Madsen M., Storm T., Moestrup S.K., Andersen G.R.;
Nature 464:445-448(2010).
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 932-1388 IN COMPLEX WITH GIFAND CALCIUM IONS, INTERACTION WITH GIF, IDENTIFICATION IN CUBAMCOMPLEX, SUBUNIT, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-984;ASN-1092; ASN-1168; ASN-1217; ASN-1285; ASN-1307; ASN-1319 ANDASN-1332.
PubMed: 20237569