TRFM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRFM_HUMAN
• UniProt AC: P08582
• Protein Name: Melanotransferrin {ECO:0000312|HGNC:HGNC:7037}
• Gene Name: MELTF {ECO:0000312|HGNC:HGNC:7037}
• Organism: Homo sapiens (Human).
• Sequence Length: 738
• Subcellular Localization: Isoform 1: Cell membrane; Lipid-anchor, GPI-anchor.
• Protein Description: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc..
• Protein Sequence: MRGPSGALWLLLALRTVLGGMEVRWCATSDPEQHKCGNMSEAFREAGIQPSLLCVRGTSADHCVQLIAAQEADAITLDGGAIYEAGKEHGLKPVVGEVYDQEVGTSYYAVAVVRRSSHVTIDTLKGVKSCHTGINRTVGWNVPVGYLVESGRLSVMGCDVLKAVSDYFGGSCVPGAGETSYSESLCRLCRGDSSGEGVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGKTLPSWGQALLSQDFELLCRDGSRADVTEWRQCHLARVPAHAVVVRADTDGGLIFRLLNEGQRLFSHEGSSFQMFSSEAYGQKDLLFKDSTSELVPIATQTYEAWLGHEYLHAMKGLLCDPNRLPPYLRWCVLSTPEIQKCGDMAVAFRRQRLKPEIQCVSAKSPQHCMERIQAEQVDAVTLSGEDIYTAGKTYGLVPAAGEHYAPEDSSNSYYVVAVVRRDSSHAFTLDELRGKRSCHAGFGSPAGWDVPVGALIQRGFIRPKDCDVLTAVSEFFNASCVPVNNPKNYPSSLCALCVGDEQGRNKCVGNSQERYYGYRGAFRCLVENAGDVAFVRHTTVFDNTNGHNSEPWAAELRSEDYELLCPNGARAEVSQFAACNLAQIPPHAVMVRPDTNIFTVYGLLDKAQDLFGDDHNKNGFKMFDSSNYHGQDLLFKDATVRAVPVGEKTTYRGWLGLDYVAALEGMSSQQCSGAAAPAPGAPLLPLLLPALAARLLPPAL

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
38	N-linked_Glycosylation	PEQHKCGNMSEAFRE HHHHCCCCHHHHHHH	40.03	UniProtKB CARBOHYD
51	Phosphorylation	REAGIQPSLLCVRGT HHCCCCCCEEEEECC	20.00	-
117	Phosphorylation	VAVVRRSSHVTIDTL EEEEECCCCCEECCC	21.84	24719451
135	N-linked_Glycosylation	KSCHTGINRTVGWNV CCCCCCCCCCCCCCC	34.61	UniProtKB CARBOHYD
146	Phosphorylation	GWNVPVGYLVESGRL CCCCCCEEEEECCCE	14.07	-
150	Phosphorylation	PVGYLVESGRLSVMG CCEEEEECCCEEEEC	23.02	-
207	Phosphorylation	DKSPLERYYDYSGAF CCCHHHHHCCCCCHH	7.42	-
208	Phosphorylation	KSPLERYYDYSGAFR CCHHHHHCCCCCHHH	18.02	-
210	Phosphorylation	PLERYYDYSGAFRCL HHHHHCCCCCHHHHH	7.90	-
211	Phosphorylation	LERYYDYSGAFRCLA HHHHCCCCCHHHHHH	22.28	-
266	Phosphorylation	DGSRADVTEWRQCHL CCCCCCCCCHHHHHH	30.31	-
461	Phosphorylation	VAVVRRDSSHAFTLD EEEEECCCCCCEEHH	23.39	27050516
462	Phosphorylation	AVVRRDSSHAFTLDE EEEECCCCCCEEHHH	24.11	15489334
515	N-linked_Glycosylation	TAVSEFFNASCVPVN HHHHHHHCCCCCCCC	35.94	UniProtKB CARBOHYD
709	GPI-anchor	EGMSSQQCSGAAAPA HCCCCCCCCCCCCCC	2.92	-

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
462	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRFM_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 TRFM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HPGDS_HUMAN	HPGDS	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956

Drug and Disease Associations

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