HYOU1

Protein identityUniProt · HPA

UniProt accession

Q9Y4L1

Gene

HYOU1

Ensembl

ENSG00000149428

Chromosome

11

Canonical length

999 aa

Protein class

Disease related genes, Human disease related genes, Plasma proteins, Potential drug targets, Predicted intracellular proteins, Transporters

Secretome location

Intracellular and membrane

OverviewNCBI Gene

The protein encoded by this gene belongs to the heat shock protein 70 family. This gene uses alternative transcription start sites. A cis-acting segment found in the 5' UTR is involved in stress-dependent induction, resulting in the accumulation of this protein in the endoplasmic reticulum (ER) under hypoxic conditions. The protein encoded by this gene is thought to play an important role in protein folding and secretion in the ER. Since suppression of the protein is associated with accelerated apoptosis, it is also suggested to have an important cytoprotective role in hypoxia-induced cellular perturbation. This protein has been shown to be up-regulated in tumors, especially in breast tumors, and thus it is associated with tumor invasiveness. This gene also has an alternative translation initiation site, resulting in a protein that lacks the N-terminal signal peptide. This signal peptide-lacking protein, which is only 3 amino acids shorter than the mature protein in the ER, is thought to have a housekeeping function in the cytosol. In rat, this protein localizes to both the ER by a carboxy-terminal peptide sequence and to mitochondria by an amino-terminal targeting signal. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Mar 2014]

Canonical amino-acid sequenceUniProt

999 residues, UniProt reviewed canonical sequence.

>Q9Y4L1|HYOU1
     1  MADKVRRQRP RRRVCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL
    61  NKESRRKTPV IVTLKENERF FGDSAASMAI KNPKATLRYF QHLLGKQADN PHVALYQARF
   121  PEHELTFDPQ RQTVHFQISS QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPVFF
   181  NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INTTAQNIMF YDMGSGSTVC
   241  TIVTYQMVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR ERLAGLFNEQ RKGQRAKDVR
   301  ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFERVP
   361  GPVQQALQSA EMSLDEIEQV ILVGGATRVP RVQEVLLKAV GKEELGKNIN ADEAAAMGAV
   421  YQAAALSKAF KVKPFVVRDA VVYPILVEFT REVEEEPGIH SLKHNKRVLF SRMGPYPQRK
   481  VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGDSFKK YPDYESKGIK
   541  AHFNLDESGV LSLDRVESVF ETLVEDSAEE ESTLTKLGNT ISSLFGGGTT PDAKENGTDT
   601  VQEEEESPAE GSKDEPGEQV ELKEEAEAPV EDGSQPPPPE PKGDATPEGE KATEKENGDK
   661  SEAQKPSEKA EAGPEGVAPA PEGEKKQKPA RKRRMVEEIG VELVVLDLPD LPEDKLAQSV
   721  QKLQDLTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSAAST
   781  WLEDEGVGAT TVMLKEKLAE LRKLCQGLFF RVEERKKWPE RLSALDNLLN HSSMFLKGAR
   841  LIPEMDQIFT EVEMTTLEKV INETWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
   901  EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASASDQGEK VIPPAGQTED AEPISEPEKV
   961  ETGSEPGDTE PLELGGPGAE PEQKEQSTGQ KRPLKNDEL

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against HYOU1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.35

Highest tissue expression

105 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about HYOU1.

Disease | AllUniProt

Conditions HYOU1 is implicated in, by any mechanism.

• Immunodeficiency 59 and hypoglycemia (IMD59) MIM:233600

Disease | GeneticClinVar

4 pathogenic / likely-pathogenic of 867 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Granulocytopenia with immunoglobulin abnormality

ReferencesPubMed · IEDB

Publications for HYOU1 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.33

gnomAD pLI

0.86

gnomAD missense Z

1.8

DepMap mean gene effect

-1.04

DepMap dependency class

common

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cellular response to hypoxia
• endoplasmic reticulum to Golgi vesicle-mediated transport
• negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway
• negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
• response to endoplasmic reticulum stress
• response to ischemia

Molecular functions

• adenyl-nucleotide exchange factor activity
• ATP binding
• ATP-dependent protein folding chaperone
• protein-folding chaperone binding
• unfolded protein binding

Cellular components

• endocytic vesicle lumen
• endoplasmic reticulum
• endoplasmic reticulum chaperone complex
• endoplasmic reticulum lumen
• extracellular exosome
• extracellular region
• focal adhesion
• membrane
• mitochondrion
• smooth endoplasmic reticulum

Protein domainsUniProt · Pfam · InterPro

• Heat shock protein 70 family
• Heat shock protein 70, conserved site
• Heat shock protein 70kD, peptide-binding domain superfamily
• Heat shock protein 70kD, C-terminal domain superfamily
• ATPase, nucleotide binding domain
• Hsp70 protein

KeywordsUniProt

• Acetylation
• ATP-binding
• Chaperone
• Endoplasmic reticulum
• Glycoprotein
• Nucleotide-binding
• Phosphoprotein
• Signal
• Stress response

InteractionsUniProt · HPA

Protein binding partners of HYOU1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• CANX
• HSPA5