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Protein

Erlin-1

Gene

ERLIN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. Binds cholesterol and may promote ER retention of the SCAP-SREBF complex (PubMed:24217618).2 Publications

GO - Molecular functioni

  • cholesterol binding Source: UniProtKB

GO - Biological processi

  • cholesterol metabolic process Source: UniProtKB-KW
  • ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
  • negative regulation of cholesterol biosynthetic process Source: UniProtKB
  • negative regulation of fatty acid biosynthetic process Source: UniProtKB
  • SREBP signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Erlin-1
Alternative name(s):
Endoplasmic reticulum lipid raft-associated protein 1
Protein KE04
Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 1
Short name:
SPFH domain-containing protein 1
Gene namesi
Name:ERLIN1
Synonyms:C10orf69, KE04, KEO4, SPFH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:16947. ERLIN1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 55CytoplasmicSequence analysis
Transmembranei6 – 2621HelicalSequence analysisAdd
BLAST
Topological domaini27 – 346320LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • endoplasmic reticulum Source: HPA
  • endoplasmic reticulum membrane Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

MalaCardsiERLIN1.
Orphaneti401785. Autosomal recessive spastic paraplegia type 62.
PharmGKBiPA162385299.

Polymorphism and mutation databases

BioMutaiERLIN1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346Erlin-1PRO_0000002784Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061N-linked (GlcNAc...)1 Publication
Modified residuei267 – 2671N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

EPDiO75477.
MaxQBiO75477.
PaxDbiO75477.
PRIDEiO75477.

PTM databases

iPTMnetiO75477.
SwissPalmiO75477.

Expressioni

Tissue specificityi

Expressed in heart, placenta, liver, kidney, pancreas, prostate, testis, ovary and small intestine.1 Publication

Gene expression databases

BgeeiO75477.
CleanExiHS_ERLIN1.
ExpressionAtlasiO75477. baseline and differential.
GenevisibleiO75477. HS.

Organism-specific databases

HPAiHPA011252.

Interactioni

Subunit structurei

Forms a heteromeric complex with ERLIN2 (PubMed:19240031). In complex with ERLIN2, interacts with RNF170 (PubMed:21610068). Interacts with AMFR and SYVN1 (PubMed:21343306).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
B2RDE63EBI-359299,EBI-10175845
AGR3Q8TD063EBI-359299,EBI-3925742
SEC22AQ96IW73EBI-359299,EBI-8652744
TMEM199Q8N5113EBI-359299,EBI-10265825

Protein-protein interaction databases

BioGridi115859. 53 interactions.
IntActiO75477. 31 interactions.
MINTiMINT-1140220.
STRINGi9606.ENSP00000384900.

Structurei

3D structure databases

ProteinModelPortaliO75477.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the band 7/mec-2 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2962. Eukaryota.
ENOG410XQSH. LUCA.
HOGENOMiHOG000251613.
HOVERGENiHBG050934.
InParanoidiO75477.
PhylomeDBiO75477.
TreeFamiTF313059.

Family and domain databases

InterProiIPR001107. Band_7.
IPR033294. Erlin1/2.
[Graphical view]
PANTHERiPTHR15351. PTHR15351. 1 hit.
PfamiPF01145. Band_7. 1 hit.
[Graphical view]
SMARTiSM00244. PHB. 1 hit.
[Graphical view]
SUPFAMiSSF117892. SSF117892. 1 hit.

Sequencei

Sequence statusi: Complete.

O75477-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTQARVLVAA VVGLVAVLLY ASIHKIEEGH LAVYYRGGAL LTSPSGPGYH
60 70 80 90 100
IMLPFITTFR SVQTTLQTDE VKNVPCGTSG GVMIYIDRIE VVNMLAPYAV
110 120 130 140 150
FDIVRNYTAD YDKTLIFNKI HHELNQFCSA HTLQEVYIEL FDQIDENLKQ
160 170 180 190 200
ALQKDLNLMA PGLTIQAVRV TKPKIPEAIR RNFELMEAEK TKLLIAAQKQ
210 220 230 240 250
KVVEKEAETE RKKAVIEAEK IAQVAKIRFQ QKVMEKETEK RISEIEDAAF
260 270 280 290 300
LAREKAKADA EYYAAHKYAT SNKHKLTPEY LELKKYQAIA SNSKIYFGSN
310 320 330 340
IPNMFVDSSC ALKYSDIRTG RESSLPSKEA LEPSGENVIQ NKESTG
Length:346
Mass (Da):38,926
Last modified:November 1, 1998 - v1
Checksum:iD703ACFD3328A27B
GO

Sequence cautioni

The sequence CAQ10515.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence EAW49846.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti257 – 2571K → R in BAD96200 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064093 mRNA. Translation: AAC26658.1.
AK222480 mRNA. Translation: BAD96200.1.
AL138921 Genomic DNA. Translation: CAQ10515.1. Different initiation.
CH471066 Genomic DNA. Translation: EAW49846.1. Different initiation.
BC031791 mRNA. Translation: AAH31791.1.
RefSeqiNP_001094096.1. NM_001100626.1.
NP_006450.2. NM_006459.3.
XP_005269499.1. XM_005269442.2.
UniGeneiHs.150087.

Genome annotation databases

EnsembliENST00000407654; ENSP00000384900; ENSG00000107566.
ENST00000421367; ENSP00000410964; ENSG00000107566.
GeneIDi10613.
KEGGihsa:10613.
UCSCiuc001kqn.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064093 mRNA. Translation: AAC26658.1.
AK222480 mRNA. Translation: BAD96200.1.
AL138921 Genomic DNA. Translation: CAQ10515.1. Different initiation.
CH471066 Genomic DNA. Translation: EAW49846.1. Different initiation.
BC031791 mRNA. Translation: AAH31791.1.
RefSeqiNP_001094096.1. NM_001100626.1.
NP_006450.2. NM_006459.3.
XP_005269499.1. XM_005269442.2.
UniGeneiHs.150087.

3D structure databases

ProteinModelPortaliO75477.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115859. 53 interactions.
IntActiO75477. 31 interactions.
MINTiMINT-1140220.
STRINGi9606.ENSP00000384900.

PTM databases

iPTMnetiO75477.
SwissPalmiO75477.

Polymorphism and mutation databases

BioMutaiERLIN1.

Proteomic databases

EPDiO75477.
MaxQBiO75477.
PaxDbiO75477.
PRIDEiO75477.

Protocols and materials databases

DNASUi10613.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000407654; ENSP00000384900; ENSG00000107566.
ENST00000421367; ENSP00000410964; ENSG00000107566.
GeneIDi10613.
KEGGihsa:10613.
UCSCiuc001kqn.5. human.

Organism-specific databases

CTDi10613.
GeneCardsiERLIN1.
HGNCiHGNC:16947. ERLIN1.
HPAiHPA011252.
MalaCardsiERLIN1.
MIMi611604. gene.
neXtProtiNX_O75477.
Orphaneti401785. Autosomal recessive spastic paraplegia type 62.
PharmGKBiPA162385299.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2962. Eukaryota.
ENOG410XQSH. LUCA.
HOGENOMiHOG000251613.
HOVERGENiHBG050934.
InParanoidiO75477.
PhylomeDBiO75477.
TreeFamiTF313059.

Miscellaneous databases

ChiTaRSiERLIN1. human.
GeneWikiiERLIN1.
GenomeRNAii10613.
PROiO75477.
SOURCEiSearch...

Gene expression databases

BgeeiO75477.
CleanExiHS_ERLIN1.
ExpressionAtlasiO75477. baseline and differential.
GenevisibleiO75477. HS.

Family and domain databases

InterProiIPR001107. Band_7.
IPR033294. Erlin1/2.
[Graphical view]
PANTHERiPTHR15351. PTHR15351. 1 hit.
PfamiPF01145. Band_7. 1 hit.
[Graphical view]
SMARTiSM00244. PHB. 1 hit.
[Graphical view]
SUPFAMiSSF117892. SSF117892. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a novel gene KE04 differentially expressed by activated human dendritic cells."
    Li N., Huang X., Zhao Z., Chen G., Zhang W., Cao X.
    Biochem. Biophys. Res. Commun. 279:487-493(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Dendritic cell.
  2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Adipose tissue.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "An endoplasmic reticulum (ER) membrane complex composed of SPFH1 and SPFH2 mediates the ER-associated degradation of inositol 1,4,5-trisphosphate receptors."
    Pearce M.M.P., Wormer D.B., Wilkens S., Wojcikiewicz R.J.H.
    J. Biol. Chem. 284:10433-10445(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION, INTERACTION WITH ERLIN2.
  7. "Erlin-1 and erlin-2 are novel members of the prohibitin family of proteins that define lipid-raft-like domains of the ER."
    Browman D.T., Resek M.E., Zajchowski L.D., Robbins S.M.
    J. Cell Sci. 119:3149-3160(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-106.
    Tissue: Liver.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-267, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Membrane-associated ubiquitin ligase complex containing gp78 mediates sterol-accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase."
    Jo Y., Sguigna P.V., DeBose-Boyd R.A.
    J. Biol. Chem. 286:15022-15031(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AMFR AND SYVN1.
  13. "RNF170 protein, an endoplasmic reticulum membrane ubiquitin ligase, mediates inositol 1,4,5-trisphosphate receptor ubiquitination and degradation."
    Lu J.P., Wang Y., Sliter D.A., Pearce M.M., Wojcikiewicz R.J.
    J. Biol. Chem. 286:24426-24433(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF170.
  14. "Erlins restrict SREBP activation in the ER and regulate cellular cholesterol homeostasis."
    Huber M.D., Vesely P.W., Datta K., Gerace L.
    J. Cell Biol. 203:427-436(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiERLN1_HUMAN
AccessioniPrimary (citable) accession number: O75477
Secondary accession number(s): B0QZ42, Q53HV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

This sequence contains two in frame methionine codon situated in atypical consensus Kozak sequence in the 5'terminus. By homolog comparison, the second ATG was supposed to be the start codon according to PubMed:11118313.Curated

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.