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Protein

Protein RER1

Gene

RER1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the retrieval of endoplasmic reticulum membrane proteins from the early Golgi compartment.By similarity

GO - Biological processi

Complete GO annotation...

Protein family/group databases

TCDBi9.B.82.1.2. endoplasmic reticulum retrieval protein1 (putative heavy metal transporter) (rer1) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein RER1
Gene namesi
Name:RER1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:30309. RER1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei41 – 6121HelicalSequence analysisAdd
BLAST
Transmembranei63 – 8321HelicalSequence analysisAdd
BLAST
Transmembranei140 – 16021HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134901074.

Polymorphism and mutation databases

BioMutaiRER1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 196195Protein RER1PRO_0000207589Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei2 – 21PhosphoserineBy similarity
Modified residuei6 – 61PhosphoserineCombined sources
Modified residuei95 – 951PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO15258.
PaxDbiO15258.
PRIDEiO15258.

PTM databases

iPTMnetiO15258.
PhosphoSiteiO15258.
SwissPalmiO15258.

Expressioni

Gene expression databases

BgeeiO15258.
CleanExiHS_RER1.
ExpressionAtlasiO15258. baseline and differential.
GenevisibleiO15258. HS.

Organism-specific databases

HPAiCAB037240.
HPA051400.

Interactioni

Protein-protein interaction databases

BioGridi116262. 34 interactions.
IntActiO15258. 10 interactions.
MINTiMINT-4726643.
STRINGi9606.ENSP00000302088.

Structurei

3D structure databases

ProteinModelPortaliO15258.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the RER1 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1688. Eukaryota.
COG5249. LUCA.
HOVERGENiHBG002871.
InParanoidiO15258.
OrthoDBiEOG7QRQVV.
PhylomeDBiO15258.
TreeFamiTF300029.

Family and domain databases

InterProiIPR004932. Rer1.
[Graphical view]
PANTHERiPTHR10743. PTHR10743. 1 hit.
PfamiPF03248. Rer1. 1 hit.
[Graphical view]
PIRSFiPIRSF016013. AtER_Rer1p. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O15258-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEGDSVGES VHGKPSVVYR FFTRLGQIYQ SWLDKSTPYT AVRWVVTLGL
60 70 80 90 100
SFVYMIRVYL LQGWYIVTYA LGIYHLNLFI AFLSPKVDPS LMEDSDDGPS
110 120 130 140 150
LPTKQNEEFR PFIRRLPEFK FWHAATKGIL VAMVCTFFDA FNVPVFWPIL
160 170 180 190
VMYFIMLFCI TMKRQIKHMI KYRYIPFTHG KRRYRGKEDA GKAFAS
Length:196
Mass (Da):22,958
Last modified:January 1, 1998 - v1
Checksum:i0FF7F3CDC9F88A69
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti123 – 19674HAATK…KAFAS → DASVCGDGRCSCKAGGGRQC PVLAADAALTFSPHLKACGY QGHPCGYGLYFLRRFQRPGV LADSGDVLHHALLYHDEEAN QAHD in AAC72940 (Ref. 2) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001421 mRNA. Translation: CAA04754.1.
AF091071 mRNA. Translation: AAC72940.1.
BC004965 mRNA. Translation: AAH04965.1.
CCDSiCCDS41232.1.
RefSeqiNP_008964.3. NM_007033.4.
XP_006710369.1. XM_006710306.2.
XP_011538844.1. XM_011540542.1.
XP_011538845.1. XM_011540543.1.
UniGeneiHs.525527.

Genome annotation databases

EnsembliENST00000488353; ENSP00000464222; ENSG00000157916.
ENST00000605895; ENSP00000475168; ENSG00000157916.
GeneIDi11079.
KEGGihsa:11079.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ001421 mRNA. Translation: CAA04754.1.
AF091071 mRNA. Translation: AAC72940.1.
BC004965 mRNA. Translation: AAH04965.1.
CCDSiCCDS41232.1.
RefSeqiNP_008964.3. NM_007033.4.
XP_006710369.1. XM_006710306.2.
XP_011538844.1. XM_011540542.1.
XP_011538845.1. XM_011540543.1.
UniGeneiHs.525527.

3D structure databases

ProteinModelPortaliO15258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116262. 34 interactions.
IntActiO15258. 10 interactions.
MINTiMINT-4726643.
STRINGi9606.ENSP00000302088.

Protein family/group databases

TCDBi9.B.82.1.2. endoplasmic reticulum retrieval protein1 (putative heavy metal transporter) (rer1) family.

PTM databases

iPTMnetiO15258.
PhosphoSiteiO15258.
SwissPalmiO15258.

Polymorphism and mutation databases

BioMutaiRER1.

Proteomic databases

EPDiO15258.
PaxDbiO15258.
PRIDEiO15258.

Protocols and materials databases

DNASUi11079.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000488353; ENSP00000464222; ENSG00000157916.
ENST00000605895; ENSP00000475168; ENSG00000157916.
GeneIDi11079.
KEGGihsa:11079.

Organism-specific databases

CTDi11079.
GeneCardsiRER1.
HGNCiHGNC:30309. RER1.
HPAiCAB037240.
HPA051400.
neXtProtiNX_O15258.
PharmGKBiPA134901074.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1688. Eukaryota.
COG5249. LUCA.
HOVERGENiHBG002871.
InParanoidiO15258.
OrthoDBiEOG7QRQVV.
PhylomeDBiO15258.
TreeFamiTF300029.

Miscellaneous databases

ChiTaRSiRER1. human.
GenomeRNAii11079.
PROiO15258.

Gene expression databases

BgeeiO15258.
CleanExiHS_RER1.
ExpressionAtlasiO15258. baseline and differential.
GenevisibleiO15258. HS.

Family and domain databases

InterProiIPR004932. Rer1.
[Graphical view]
PANTHERiPTHR10743. PTHR10743. 1 hit.
PfamiPF03248. Rer1. 1 hit.
[Graphical view]
PIRSFiPIRSF016013. AtER_Rer1p. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Human Rer1 is localized to the Golgi apparatus and complements the deletion of the homologous Rer1 protein of Saccharomyces cerevisiae."
    Fuellekrug J., Boehm J., Roettger S., Nilsson T., Mieskes G., Schmitt H.
    Eur. J. Cell Biol. 74:31-40(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary cancer.
  2. "Full-insert sequence of mapped XREF EST."
    Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.
    Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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: Skin.
  4. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6 AND SER-95, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRER1_HUMAN
AccessioniPrimary (citable) accession number: O15258
Secondary accession number(s): O95322
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 134 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, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. 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.