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Protein

Erlin-2

Gene

ERLIN2

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) such as ITPR1 (PubMed:19240031, PubMed:17502376). Promotes sterol-accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin ligase complex (PubMed:21343306). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. May promote ER retention of the SCAP-SREBF complex (PubMed:24217618).4 Publications

GO - Molecular functioni

  • cholesterol binding Source: GO_Central
  • protein tyrosine kinase activity Source: Reactome
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

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

Enzyme and pathway databases

ReactomeiR-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-8853336. Signaling by plasma membrane FGFR1 fusions.

Names & Taxonomyi

Protein namesi
Recommended name:
Erlin-2
Alternative name(s):
Endoplasmic reticulum lipid raft-associated protein 2
Stomatin-prohibitin-flotillin-HflC/K domain-containing protein 2
Short name:
SPFH domain-containing protein 2
Gene namesi
Name:ERLIN2
Synonyms:C8orf2, SPFH2
ORF Names:UNQ2441/PRO5003/PRO9924
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:1356. ERLIN2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 33CytoplasmicSequence analysis
Transmembranei4 – 2421HelicalSequence analysisAdd
BLAST
Topological domaini25 – 339315LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: HPA
  • endoplasmic reticulum Source: LIFEdb
  • endoplasmic reticulum membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
  • membrane raft Source: UniProtKB
  • plasma membrane Source: HPA
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Spastic paraplegia 18, autosomal recessive (SPG18)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of spastic paraplegia, a neurodegenerative disorder characterized by a slow, gradual, progressive weakness and spasticity of the lower limbs. Rate of progression and the severity of symptoms are quite variable. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. SPG18 is a severe form with onset in early childhood. Most affected individuals have severe psychomotor retardation. Some may develop significant joint contractures.
See also OMIM:611225

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi106 – 1061N → Q: Loss of glycosylation. 1 Publication

Keywords - Diseasei

Hereditary spastic paraplegia, Neurodegeneration

Organism-specific databases

MalaCardsiERLIN2.
MIMi611225. phenotype.
Orphaneti209951. Autosomal recessive spastic paraplegia type 18.
247604. Juvenile primary lateral sclerosis.
280384. Recessive intellectual disability - motor dysfunction - multiple joint contractures.
PharmGKBiPA25961.

Polymorphism and mutation databases

BioMutaiERLIN2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339Erlin-2PRO_0000002787Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi106 – 1061N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

EPDiO94905.
MaxQBiO94905.
PaxDbiO94905.
PeptideAtlasiO94905.
PRIDEiO94905.

PTM databases

iPTMnetiO94905.
PhosphoSiteiO94905.
SwissPalmiO94905.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiO94905.
CleanExiHS_ERLIN2.
ExpressionAtlasiO94905. baseline and differential.
GenevisibleiO94905. HS.

Organism-specific databases

HPAiCAB014894.
HPA002025.

Interactioni

Subunit structurei

Forms a heteromeric complex with ERLIN1. In complex with ERLIN1, interacts with RNF170 (PubMed:19240031, PubMed:21610068). Interacts with activated ITPR1, independently of the degree of ITPR1 polyubiquitination (By similarity). Interacts with SCAP, INSIG1, SREBF1 and SREBF2 under cholesterol sufficiency conditions; indicative for an association with the SCAP-SREBP-INSIG complex (PubMed:24217618). Probably part of an AMFR/gp78 and INSIG1-containing ubiquitin ligase complex involved in ERAD of HMGCR. Interacts with TMUB1; TMUB1 bridges the association with AMFR. Interacts with SYVN1 and RNF139 (PubMed:21343306). Interacts with TMEM259 (By similarity).By similarity1 Publication4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AMFRQ9UKV58EBI-4400770,EBI-1046367
HMGCRP003472EBI-4400770,EBI-11426687From a different organism.
TMUB1Q9BVT85EBI-4400770,EBI-11425701

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi116331. 103 interactions.
IntActiO94905. 53 interactions.
MINTiMINT-3035811.
STRINGi9606.ENSP00000276461.

Structurei

3D structure databases

ProteinModelPortaliO94905.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 309133Interaction with ERLIN1Add
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2962. Eukaryota.
ENOG410XQSH. LUCA.
GeneTreeiENSGT00390000014666.
HOVERGENiHBG050934.
InParanoidiO94905.
OMAiNMFVDSA.
OrthoDBiEOG7Z69D1.
PhylomeDBiO94905.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O94905-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAQLGAVVAV ASSFFCASLF SAVHKIEEGH IGVYYRGGAL LTSTSGPGFH
60 70 80 90 100
LMLPFITSYK SVQTTLQTDE VKNVPCGTSG GVMIYFDRIE VVNFLVPNAV
110 120 130 140 150
YDIVKNYTAD YDKALIFNKI HHELNQFCSV HTLQEVYIEL FDQIDENLKL
160 170 180 190 200
ALQQDLTSMA PGLVIQAVRV TKPNIPEAIR RNYELMESEK TKLLIAAQKQ
210 220 230 240 250
KVVEKEAETE RKKALIEAEK VAQVAEITYG QKVMEKETEK KISEIEDAAF
260 270 280 290 300
LAREKAKADA ECYTAMKIAE ANKLKLTPEY LQLMKYKAIA SNSKIYFGKD
310 320 330
IPNMFMDSAG SVSKQFEGLA DKLSFGLEDE PLETATKEN
Length:339
Mass (Da):37,840
Last modified:May 1, 1999 - v1
Checksum:i3CF322548FD58DB0
GO
Isoform 2 (identifier: O94905-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     142-152: DQIDENLKLAL → GLENDFSQESS
     153-339: Missing.

Show »
Length:152
Mass (Da):16,814
Checksum:i13EE2B91F5293642
GO
Isoform 3 (identifier: O94905-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     142-206: DQIDENLKLA...AQKQKVVEKE → GKKVSPEHAV...RMLIAMQQDP
     207-339: Missing.

Show »
Length:206
Mass (Da):22,939
Checksum:iC585C9F7DB01A671
GO

Sequence cautioni

The sequence AAH50611.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 611S → P in AAH05950 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711V → A.
Corresponds to variant rs2032066 [ dbSNP | Ensembl ].
VAR_059140

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei142 – 20665DQIDE…VVEKE → GKKVSPEHAVLKQGSWNPAS LHCLKPGCLQGVMVTYGQEM LKNLVLRSWSQRSSWRMLIA MQQDP in isoform 3. 2 PublicationsVSP_013940Add
BLAST
Alternative sequencei142 – 15211DQIDENLKLAL → GLENDFSQESS in isoform 2. 2 PublicationsVSP_008713Add
BLAST
Alternative sequencei153 – 339187Missing in isoform 2. 2 PublicationsVSP_008714Add
BLAST
Alternative sequencei207 – 339133Missing in isoform 3. 2 PublicationsVSP_013941Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018790 Genomic DNA. Translation: BAA36845.1.
AL442077 mRNA. Translation: CAC09443.1.
AY358108 mRNA. Translation: AAQ88475.1.
AY358851 mRNA. Translation: AAQ89210.1.
AK291394 mRNA. Translation: BAF84083.1.
AK297279 mRNA. Translation: BAG59750.1.
CH471080 Genomic DNA. Translation: EAW63365.1.
CH471080 Genomic DNA. Translation: EAW63366.1.
BC005950 mRNA. Translation: AAH05950.1. Different termination.
BC048308 mRNA. Translation: AAH48308.1.
BC050611 mRNA. Translation: AAH50611.1. Different initiation.
BC067765 mRNA. Translation: AAH67765.1.
CCDSiCCDS34879.1. [O94905-2]
CCDS6095.1. [O94905-1]
RefSeqiNP_001003790.1. NM_001003790.3. [O94905-2]
NP_001003791.1. NM_001003791.2. [O94905-2]
NP_009106.1. NM_007175.6. [O94905-1]
XP_005273449.1. XM_005273392.1. [O94905-1]
UniGeneiHs.705490.

Genome annotation databases

EnsembliENST00000276461; ENSP00000276461; ENSG00000147475. [O94905-1]
ENST00000335171; ENSP00000335220; ENSG00000147475. [O94905-2]
ENST00000397228; ENSP00000380405; ENSG00000147475. [O94905-2]
ENST00000518586; ENSP00000427847; ENSG00000147475. [O94905-3]
ENST00000519638; ENSP00000428112; ENSG00000147475. [O94905-1]
ENST00000523107; ENSP00000473292; ENSG00000147475. [O94905-3]
ENST00000523887; ENSP00000429903; ENSG00000147475. [O94905-3]
GeneIDi11160.
KEGGihsa:11160.
UCSCiuc003xkc.5. human. [O94905-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB018790 Genomic DNA. Translation: BAA36845.1.
AL442077 mRNA. Translation: CAC09443.1.
AY358108 mRNA. Translation: AAQ88475.1.
AY358851 mRNA. Translation: AAQ89210.1.
AK291394 mRNA. Translation: BAF84083.1.
AK297279 mRNA. Translation: BAG59750.1.
CH471080 Genomic DNA. Translation: EAW63365.1.
CH471080 Genomic DNA. Translation: EAW63366.1.
BC005950 mRNA. Translation: AAH05950.1. Different termination.
BC048308 mRNA. Translation: AAH48308.1.
BC050611 mRNA. Translation: AAH50611.1. Different initiation.
BC067765 mRNA. Translation: AAH67765.1.
CCDSiCCDS34879.1. [O94905-2]
CCDS6095.1. [O94905-1]
RefSeqiNP_001003790.1. NM_001003790.3. [O94905-2]
NP_001003791.1. NM_001003791.2. [O94905-2]
NP_009106.1. NM_007175.6. [O94905-1]
XP_005273449.1. XM_005273392.1. [O94905-1]
UniGeneiHs.705490.

3D structure databases

ProteinModelPortaliO94905.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116331. 103 interactions.
IntActiO94905. 53 interactions.
MINTiMINT-3035811.
STRINGi9606.ENSP00000276461.

PTM databases

iPTMnetiO94905.
PhosphoSiteiO94905.
SwissPalmiO94905.

Polymorphism and mutation databases

BioMutaiERLIN2.

Proteomic databases

EPDiO94905.
MaxQBiO94905.
PaxDbiO94905.
PeptideAtlasiO94905.
PRIDEiO94905.

Protocols and materials databases

DNASUi11160.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000276461; ENSP00000276461; ENSG00000147475. [O94905-1]
ENST00000335171; ENSP00000335220; ENSG00000147475. [O94905-2]
ENST00000397228; ENSP00000380405; ENSG00000147475. [O94905-2]
ENST00000518586; ENSP00000427847; ENSG00000147475. [O94905-3]
ENST00000519638; ENSP00000428112; ENSG00000147475. [O94905-1]
ENST00000523107; ENSP00000473292; ENSG00000147475. [O94905-3]
ENST00000523887; ENSP00000429903; ENSG00000147475. [O94905-3]
GeneIDi11160.
KEGGihsa:11160.
UCSCiuc003xkc.5. human. [O94905-1]

Organism-specific databases

CTDi11160.
GeneCardsiERLIN2.
HGNCiHGNC:1356. ERLIN2.
HPAiCAB014894.
HPA002025.
MalaCardsiERLIN2.
MIMi611225. phenotype.
611605. gene.
neXtProtiNX_O94905.
Orphaneti209951. Autosomal recessive spastic paraplegia type 18.
247604. Juvenile primary lateral sclerosis.
280384. Recessive intellectual disability - motor dysfunction - multiple joint contractures.
PharmGKBiPA25961.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2962. Eukaryota.
ENOG410XQSH. LUCA.
GeneTreeiENSGT00390000014666.
HOVERGENiHBG050934.
InParanoidiO94905.
OMAiNMFVDSA.
OrthoDBiEOG7Z69D1.
PhylomeDBiO94905.
TreeFamiTF313059.

Enzyme and pathway databases

ReactomeiR-HSA-5655302. Signaling by FGFR1 in disease.
R-HSA-8853336. Signaling by plasma membrane FGFR1 fusions.

Miscellaneous databases

GeneWikiiERLIN2.
GenomeRNAii11160.
PROiO94905.
SOURCEiSearch...

Gene expression databases

BgeeiO94905.
CleanExiHS_ERLIN2.
ExpressionAtlasiO94905. baseline and differential.
GenevisibleiO94905. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a novel gene (C8orf2), a human representative of a novel gene family with homology to C. elegans C42.C1.9."
    Ikegawa S., Isomura M., Koshizuka Y., Nakamura Y.
    Cytogenet. Cell Genet. 85:227-231(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph node.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Brain and Fetal brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-338 (ISOFORM 1).
    Tissue: Duodenum, Prostate and Testis.
  7. "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 ERLIN1.
  8. "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.
  9. "SPFH2 mediates the endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors and other substrates in mammalian cells."
    Pearce M.M., Wang Y., Kelley G.G., Wojcikiewicz R.J.H.
    J. Biol. Chem. 282:20104-20115(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-106, MUTAGENESIS OF ASN-106.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "A frameshift mutation of ERLIN2 in recessive intellectual disability, motor dysfunction and multiple joint contractures."
    Yildirim Y., Orhan E.K., Iseri S.A., Serdaroglu-Oflazer P., Kara B., Solakoglu S., Tolun A.
    Hum. Mol. Genet. 20:1886-1892(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SPG18.
  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: FUNCTION, INTERACTION WITH AMFR; SYVN1; RNF139 AND TMUB1, SUBUNIT.
  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, INTERACTION WITH SCAP; INSIG1; SREBF1 AND SREBF2.
  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 nameiERLN2_HUMAN
AccessioniPrimary (citable) accession number: O94905
Secondary accession number(s): A0JLQ1
, A8K5S9, B4DM38, D3DSW0, Q6NW21, Q86VS6, Q86W49
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: May 1, 1999
Last modified: July 6, 2016
This is version 130 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.