IF_HUMAN - dbPTM
IF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF_HUMAN
UniProt AC P27352
Protein Name Gastric intrinsic factor
Gene Name GIF
Organism Homo sapiens (Human).
Sequence Length 417
Subcellular Localization Secreted.
Protein Description Promotes absorption of the essential vitamin cobalamin (Cbl) in the ileum. After interaction with CUBN, the GIF-cobalamin complex is internalized via receptor-mediated endocytosis..
Protein Sequence MAWFALYLLSLLWATAGTSTQTQSSCSVPSAQEPLVNGIQVLMENSVTSSAYPNPSILIAMNLAGAYNLKAQKLLTYQLMSSDNNDLTIGQLGLTIMALTSSCRDPGDKVSILQRQMENWAPSSPNAEASAFYGPSLAILALCQKNSEATLPIAVRFAKTLLANSSPFNVDTGAMATLALTCMYNKIPVGSEEGYRSLFGQVLKDIVEKISMKIKDNGIIGDIYSTGLAMQALSVTPEPSKKEWNCKKTTDMILNEIKQGKFHNPMSIAQILPSLKGKTYLDVPQVTCSPDHEVQPTLPSNPGPGPTSASNITVIYTINNQLRGVELLFNETINVSVKSGSVLLVVLEEAQRKNPMFKFETTMTSWGLVVSSINNIAENVNHKTYWQFLSGVTPLNEGVADYIPFNHEHITANFTQY
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
160PhosphorylationIAVRFAKTLLANSSP
HHHHHHHHHHHCCCC
24.4729083192
165PhosphorylationAKTLLANSSPFNVDT
HHHHHHCCCCCCCCH
33.5129083192
166PhosphorylationKTLLANSSPFNVDTG
HHHHHCCCCCCCCHH
33.0629083192
172PhosphorylationSSPFNVDTGAMATLA
CCCCCCCHHHHHHHH
23.6629083192
191PhosphorylationYNKIPVGSEEGYRSL
HCCCCCCCHHHHHHH
32.48-
274PhosphorylationSIAQILPSLKGKTYL
CHHHHHHHCCCCEEE
38.9924719451
297PhosphorylationPDHEVQPTLPSNPGP
CCCCCCCCCCCCCCC
33.92-
311N-linked_GlycosylationPGPTSASNITVIYTI
CCCCCCCCEEEEEEE
33.4020237569
317PhosphorylationSNITVIYTINNQLRG
CCEEEEEEECCEEEC
13.20-
330N-linked_GlycosylationRGVELLFNETINVSV
ECEEEEEECCEEEEE
45.53UniProtKB CARBOHYD
334N-linked_GlycosylationLLFNETINVSVKSGS
EEEECCEEEEECCCC
27.68UniProtKB CARBOHYD
413N-linked_GlycosylationNHEHITANFTQY---
CCCCCCCCCCCC---
31.6720237569

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 IF_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF_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 IF_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FBX2_HUMANFBXO2physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
261000Hereditary intrinsic factor deficiency (IFD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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 25-417 IN COMPLEX WITHCOBALAMIN AND CUBN, INTERACTION WITH CUBN, DISULFIDE BONDS, ANDGLYCOSYLATION AT ASN-311 AND ASN-413.
"Crystal structure of human intrinsic factor: cobalamin complex at2.6-A resolution.";
Mathews F.S., Gordon M.M., Chen Z., Rajashankar K.R., Ealick S.E.,Alpers D.H., Sukumar N.;
Proc. Natl. Acad. Sci. U.S.A. 104:17311-17316(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 19-417 IN COMPLEX WITHCOBALAMIN, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-413.

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