OLFM4
entrez
10562
canonical
uniprot
Q6UX06
canonical
ensembl
ENSG00000102837
resolver
ensp
ENSP00000219022
resolver
enst
ENST00000219022
resolver
genesymbol
OLFM4
resolver
genesymbol_syn
GW112
resolver
hgnc
HGNC:17190
resolver
uniprot
O95362
resolver
uniprot
Q5VWG0
resolver
uniprot
Q86T22
resolver
uniprot_entry
OLFM4_HUMAN
resolver
uniprot_sec
O95362
resolver
uniprot_sec
Q5VWG0
resolver
uniprot_sec
Q86T22
resolver
amino_acid_sequence
MRPGLSFLLALLFFLGQAAGDLGDVGPPIPSPGFSSFPGVDSSSSFSSSSRSGSSSSRSLGSGGSVSQLFSNFTGSVDDRGTCQCSVSLPDTTFPVDRVERLEFTAHVLSQKFEKELSKVREYVQLISVYEKKLLNLTVRIDIMEKDTISYTELDFELIKVEVKEMEKLVIQLKESFGGSSEIVDQLEVEIRNMTLLVEKLETLDKNNVLAIRREIVALKTKLKECEASKDQNTPVVHPPPTPGSCGHGGVVNISKPSVVQLNWRGFSYLYGAWGRDYSPQHPNKGLYWVAPLNTDGRLLEYYRLYNTLDDLLLYINARELRITYGQGSGTAVYNNNMYVNMYNTGNIARVNLTTNTIAVTQTLPNAAYNNRFSYANVAWQDIDFAVDENGLWVIYSTEASTGNMVISKLNDTTLQVLNTWYTKQYKPSASNAFMVCGVLYATRTMNTRTEEIFYYYDTNTGKEGKLDIVMHKMQEKVQSINYNPFDQKLYVYNDGYLLNYDLSVLQKPQ
uniprot
proteins
function
FUNCTION: May promote proliferation of pancreatic cancer cells by favoring the transition from the S to G2/M phase. In myeloid leukemic cell lines, inhibits cell growth and induces cell differentiation and apoptosis. May play a role in the inhibition of EIF4EBP1 phosphorylation/deactivation. Facilitates cell adhesion, most probably through interaction with cell surface lectins and cadherin. {ECO:0000269|PubMed:16566923, ECO:0000269|PubMed:17270022, ECO:0000269|PubMed:20724538}.
uniprot
proteins
mass_dalton
57280
uniprot
proteins
mutagenesis
MUTAGEN 83; /note="C->A: Abolishes secretion. No effect on multimer formation."; /evidence="ECO:0000269|PubMed:16566923"; MUTAGEN 85; /note="C->A: Abolishes secretion. No effect on multimer formation."; /evidence="ECO:0000269|PubMed:16566923"; MUTAGEN 226; /note="C->A: No effect on secretion. Affects multimer formation."; /evidence="ECO:0000269|PubMed:16566923"; MUTAGEN 246; /note="C->A: Abolishes secretion. No effect on multimer formation."; /evidence="ECO:0000269|PubMed:16566923"; MUTAGEN 437; /note="C->A: Abolishes secretion. No effect on multimer formation."; /evidence="ECO:0000269|PubMed:16566923
uniprot
proteins
post_translational_modification
PTM: N-glycosylated.
uniprot
proteins
pubmed
11867215
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15059901
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16566923
uniprot
proteins
pubmed
17270022
uniprot
proteins
pubmed
20724538
uniprot
proteins
sequence_length
510
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space. Mitochondrion. Note=Subcellular location is not clearly defined: has been shown to be secreted (PubMed:16566923), but also in the mitochondrion (PubMed:15059901, PubMed:20724538), cytoplasm and plasma membrane (PubMed:20724538) and in the nucleus (PubMed:15059901). {ECO:0000269|PubMed:15059901, ECO:0000269|PubMed:16566923, ECO:0000269|PubMed:20724538}.
uniprot
proteins