SCAR5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SCAR5_HUMAN
• UniProt AC: Q6ZMJ2
• Protein Name: Scavenger receptor class A member 5 {ECO:0000255|HAMAP-Rule:MF_03070}
• Gene Name: SCARA5 {ECO:0000255|HAMAP-Rule:MF_03070}
• Organism: Homo sapiens (Human).
• Sequence Length: 495
• Subcellular Localization: Cell membrane ; Single-pass type II membrane protein .
• Protein Description: Ferritin receptor that mediates non-transferrin-dependent delivery of iron. Mediates cellular uptake of ferritin-bound iron by stimulating ferritin endocytosis from the cell surface with consequent iron delivery within the cell. Delivery of iron to cells by ferritin is required for the development of specific cell types, suggesting the existence of cell type-specific mechanisms of iron traffic in organogenesis, which alternatively utilize transferrin or non-transferrin iron delivery pathways. Ferritin mediates iron uptake in capsule cells of the developing kidney. Binds preferrentially ferritin light chain (FTL) compared to heavy chain (FTH1)..
• Protein Sequence: MENKAMYLHTVSDCDTSSICEDSFDGRSLSKLNLCEDGPCHKRRASICCTQLGSLSALKHAVLGLYLLVFLILVGIFILAVSRPRSSPDDLKALTRNVNRLNESFRDLQLRLLQAPLQADLTEQVWKVQDALQNQSDSLLALAGAVQRLEGALWGLQAQAVQTEQAVALLRDRTGQQSDTAQLELYQLQVESNSSQLLLRRHAGLLDGLARRVGILGEELADVGGVLRGLNHSLSYDVALHRTRLQDLRVLVSNASEDTRRLRLAHVGMELQLKQELAMLNAVTEDLRLKDWEHSIALRNISLAKGPPGPKGDQGDEGKEGRPGIPGLPGLRGLPGERGTPGLPGPKGDDGKLGATGPMGMRGFKGDRGPKGEKGEKGDRAGDASGVEAPMMIRLVNGSGPHEGRVEVYHDRRWGTVCDDGWDKKDGDVVCRMLGFRGVEEVYRTARFGQGTGRIWMDDVACKGTEETIFRCSFSKWGVTNCGHAEDASVTCNRH

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
7	Phosphorylation	-MENKAMYLHTVSDC -CCCCCEEEEECCCC	10.53	23312004
10	Phosphorylation	NKAMYLHTVSDCDTS CCCEEEEECCCCCCC	21.07	23312004
12	Phosphorylation	AMYLHTVSDCDTSSI CEEEEECCCCCCCHH	33.41	23312004
16	Phosphorylation	HTVSDCDTSSICEDS EECCCCCCCHHCCCC	30.61	23312004
17	Phosphorylation	TVSDCDTSSICEDSF ECCCCCCCHHCCCCC	12.40	23312004
18	Phosphorylation	VSDCDTSSICEDSFD CCCCCCCHHCCCCCC	33.09	23312004
28	Phosphorylation	EDSFDGRSLSKLNLC CCCCCCCCCHHCCCC	42.39	29214152
30	Phosphorylation	SFDGRSLSKLNLCED CCCCCCCHHCCCCCC	36.02	22617229
46	Phosphorylation	PCHKRRASICCTQLG CCCHHHHHHHCCCHH	17.85	23312004
50	Phosphorylation	RRASICCTQLGSLSA HHHHHHCCCHHHHHH	23.55	23312004
87	Phosphorylation	AVSRPRSSPDDLKAL HHCCCCCCHHHHHHH	33.36	21815630
102	N-linked_Glycosylation	TRNVNRLNESFRDLQ HHHHHHHCHHHHHHH	39.36	UniProtKB CARBOHYD
134	N-linked_Glycosylation	KVQDALQNQSDSLLA HHHHHHHCCCHHHHH	44.14	UniProtKB CARBOHYD
193	N-linked_Glycosylation	YQLQVESNSSQLLLR EEEHHHCCHHHHHHH	31.98	UniProtKB CARBOHYD
231	N-linked_Glycosylation	GGVLRGLNHSLSYDV HHHHHHHCCCCHHHH	26.06	UniProtKB CARBOHYD
254	N-linked_Glycosylation	DLRVLVSNASEDTRR HHHHHHCCCCHHHHH	39.75	UniProtKB CARBOHYD
284	Phosphorylation	LAMLNAVTEDLRLKD HHHHHCCCCHHHHCC	22.75	28355574
300	N-linked_Glycosylation	EHSIALRNISLAKGP CCHHHHHCEEECCCC	29.11	UniProtKB CARBOHYD
397	N-linked_Glycosylation	PMMIRLVNGSGPHEG CEEEEECCCCCCCCC	43.43	UniProtKB CARBOHYD
452	Phosphorylation	TARFGQGTGRIWMDD HHCCCCCCCCEEEEC	18.52	28348404
473	Phosphorylation	EETIFRCSFSKWGVT CCEEEEEEEECCCCC	28.44	24719451

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

Oops, there are no upstream regulatory protein records of SCAR5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SCAR5_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 SCAR5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HS3S2_HUMAN	HS3ST2	physical	28514442
GT252_HUMAN	COLGALT2	physical	28514442

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.