Probably involved in the regulation of pre-mRNA splicing. (updated: June 2, 2021)

Protein identification was indicated in the following studies:

Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

Publication	Identification ¹	Uniprot mapping ²	Not mapped / Obsolete	TrEMBL	Swiss-Prot
Goodman (2013)	2289 (gene list)	2278	53	20599	2269
Lange (2014)	1234	1234	7	28	1224
Hegedus (2015)	2638	2622	0	235	2387
Wilson (2016)	1658	1528	170	291	1068
d'Alessandro (2017)	1826	1817	2	0	1815
Bryk (2017)	2090	2060	10	108	1942
Chu (2018)	1853	1804	55	362	1387

¹ as available in the article and/or in supplementary material
² uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Protein sequence (FASTA)

Protein coevolution profile (FreeContact)

Multiple Sequence Alignment (Muscle)

Total structural coverage: 69%

Model score: 0

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Variant	Description
	Likely benign variant
	Likely benign variant
	MRXSA; unknown pathological significance; does not affect FAM50A protein levels in patient cells; does not affect localization to the nucleus
	MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos; does not affect FAM50A protein levels
	MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos; does not affect localization to the n
	MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos
	MRXSA; hypomorphic variant; does not fully rescue craniofacial patterning defects in zebrafish morphant embryos

Biological Process

Chromatin organization

Spermatogenesis

Cellular Component

Nucleoplasm

Nucleus

Molecular Function

Poly(A) RNA binding

RNA binding

The reference OMIM entry for this protein is 300453

Family with sequence similarity 50, member a; fam50a
Xap5 gene
Dxs9928e
Hxc26
9f

CLONING

By screening a human skeletal muscle cDNA library with a cosmid fragment obtained from Xq28 by use of an enhanced promoter trap system, Toyoda et al. (1996) cloned a partial XAP5 cDNA, which they called HXC-26. Mazzarella et al. (1997) cloned a full-length XAP5 cDNA from a human teratocarcinoma cDNA library. The full-length cDNA encodes a deduced 339-amino acid soluble protein with a predicted molecular mass of approximately 40 kD. It contains 23% basic residues and an SV40 large T antigen nuclear localization signal. By Northern blot analysis, Mazzarella et al. (1997) detected a major 1.4-kb band in all tissues examined, with an additional 1.8-kb band detectable in some tissues. Expression was abundant in fetal brain, liver, and especially kidney, with little signal from the equivalent adult organs; expression was high in adult heart, skeletal muscle, spleen, thymus, prostate, and small intestine.

GENE STRUCTURE

The XAP5 gene contains 13 exons and spans 6.5 to 8 kb of genomic sequence (Toyoda et al., 1996; Mazzarella et al., 1997). Mazzarella et al. (1997) identified a polymorphic CCG repeat region in the 5-prime UTR of XAP5.

MOLECULAR GENETICS

By examination of 48 unrelated males with a PCR assay across the CCG repeat region of the XAP5 gene, Mazzarella et al. (1997) demonstrated that the longest CCG runs ranged from 8 to 12 repeats, with 9 repeats being the most frequent.

MAPPING

By genomic sequence analysis, Toyoda et al. (1996) and Mazzarella et al. (1997) identified the FAM50A gene at Xq28. ... More on the omim web site

Subscribe to this protein entry history

July 1, 2021: Protein entry updated
Automatic update: Entry updated from uniprot information.

May 12, 2019: Protein entry updated
Automatic update: model status changed

Nov. 17, 2018: Protein entry updated
Automatic update: model status changed

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Oct. 27, 2017: Protein entry updated
Automatic update: model status changed

March 25, 2017: Additional information
No protein expression data in P. Mayeux work for FAM50A

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 300453 was added.

Feb. 25, 2016: Protein entry updated
Automatic update: model status changed

Feb. 24, 2016: Protein entry updated
Automatic update: model status changed

Jan. 25, 2016: Protein entry updated
Automatic update: model status changed

Protein FAM50A (FAM50A)