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Q9BS26 (ERP44_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endoplasmic reticulum resident protein 44

Short name=ER protein 44
Short name=ERp44
Alternative name(s):
Thioredoxin domain-containing protein 4
Gene names
Name:ERP44
Synonyms:KIAA0573, TXNDC4
ORF Names:UNQ532/PRO1075
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1L and ERO1LB in the endoplasmic reticulum. Ref.1 Ref.7

Subunit structure

Forms mixed disulfides with both ERO1L and ERO1LB and cargo folding intermediates. Directly interacts with ITPR1 in a pH-, redox state- and calcium-dependent manner, but not with ITPR2 or ITPR3. The strength of this interaction inversely correlates with calcium concentration By similarity. Ref.1 Ref.9

Subcellular location

Endoplasmic reticulum lumen.

Induction

Up-regulated by inducers of the unfolded protein response (UPR), including tunicamycin and dithiothreitol. Ref.1

Sequence similarities

Contains 1 thioredoxin domain.

Sequence caution

The sequence BAA25499.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LMAN1P492573EBI-541644,EBI-1057738

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929
Chain30 – 406377Endoplasmic reticulum resident protein 44
PRO_0000034180

Regions

Domain30 – 138109Thioredoxin
Region236 – 28550Interaction with ITPR1 By similarity
Motif403 – 4064Prevents secretion from ER Potential

Amino acid modifications

Disulfide bond58Interchain (with ERO1L) Ref.1 Ref.11
Disulfide bond189 ↔ 241 Ref.1 Ref.11
Disulfide bond301 ↔ 318 Ref.1 Ref.11

Experimental info

Sequence conflict351D → A in AAQ89407. Ref.3

Secondary structure

............................................................... 406
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BS26 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 3865DCF3811BC263

FASTA40646,971
        10         20         30         40         50         60 
MHPAVFLSLP DLRCSLLLLV TWVFTPVTTE ITSLDTENID EILNNADVAL VNFYADWCRF 

        70         80         90        100        110        120 
SQMLHPIFEE ASDVIKEEFP NENQVVFARV DCDQHSDIAQ RYRISKYPTL KLFRNGMMMK 

       130        140        150        160        170        180 
REYRGQRSVK ALADYIRQQK SDPIQEIRDL AEITTLDRSK RNIIGYFEQK DSDNYRVFER 

       190        200        210        220        230        240 
VANILHDDCA FLSAFGDVSK PERYSGDNII YKPPGHSAPD MVYLGAMTNF DVTYNWIQDK 

       250        260        270        280        290        300 
CVPLVREITF ENGEELTEEG LPFLILFHMK EDTESLEIFQ NEVARQLISE KGTINFLHAD 

       310        320        330        340        350        360 
CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD LHSGKLHREF 

       370        380        390        400 
HHGPDPTDTA PGEQAQDVAS SPPESSFQKL APSEYRYTLL RDRDEL 

« Hide

References

« Hide 'large scale' references
[1]"ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family."
Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A., Sitia R.
EMBO J. 21:835-844(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 149-158 AND 314-327, FUNCTION, INTERACTION WITH ERO1L AND ERO1LB, MIXED DISULFIDE BOND FORMATION, INDUCTION.
Tissue: Cervix.
[2]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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. expand/collapse author list , 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].
[5]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
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].
Tissue: Liver.
[7]"Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44."
Anelli T., Alessio M., Bachi A., Bergamelli L., Bertoli G., Camerini S., Mezghrani A., Ruffato E., Simmen T., Sitia R.
EMBO J. 22:5015-5022(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Towards complete analysis of the platelet proteome."
O'Neill E.E., Brock C.J., von Kriegsheim A.F., Pearce A.C., Dwek R.A., Watson S.P., Hebestreit H.F.
Proteomics 2:288-305(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Platelet.
[9]"Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44."
Higo T., Hattori M., Nakamura T., Natsume T., Michikawa T., Mikoshiba K.
Cell 120:85-98(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITPR1.
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail."
Wang L., Wang L., Vavassori S., Li S., Ke H., Anelli T., Degano M., Ronzoni R., Sitia R., Sun F., Wang C.-C.
EMBO Rep. 9:642-647(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 25-406, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ344330 mRNA. Translation: CAC87611.1.
AB011145 mRNA. Translation: BAA25499.1. Different initiation.
AY359048 mRNA. Translation: AAQ89407.1.
AK075024 mRNA. Translation: BAG52054.1.
AL360084, AL137072, AL358937 Genomic DNA. Translation: CAH70308.1.
AL137072, AL358937, AL360084 Genomic DNA. Translation: CAH72172.1.
AL358937, AL137072, AL360084 Genomic DNA. Translation: CAI95319.1.
BC005374 mRNA. Translation: AAH05374.1.
RefSeqNP_055866.1. NM_015051.1.
UniGeneHs.154023.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2R2JX-ray2.60A30-406[»]
ProteinModelPortalQ9BS26.
SMRQ9BS26. Positions 32-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116704. 28 interactions.
IntActQ9BS26. 14 interactions.
MINTMINT-2816102.
STRING9606.ENSP00000262455.

Polymorphism databases

DMDM31077035.

2D gel databases

REPRODUCTION-2DPAGEIPI00401264.

Proteomic databases

PaxDbQ9BS26.
PeptideAtlasQ9BS26.
PRIDEQ9BS26.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262455; ENSP00000262455; ENSG00000023318.
GeneID23071.
KEGGhsa:23071.
UCSCuc004bam.3. human.

Organism-specific databases

CTD23071.
GeneCardsGC09M102742.
HGNCHGNC:18311. ERP44.
HPAHPA001318.
MIM609170. gene.
neXtProtNX_Q9BS26.
PharmGKBPA164719295.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0526.
HOGENOMHOG000007707.
InParanoidQ9BS26.
KOK17264.
OMARHMYLFP.
OrthoDBEOG718KCX.
PhylomeDBQ9BS26.
TreeFamTF106378.

Gene expression databases

BgeeQ9BS26.
CleanExHS_TXNDC4.
GenevestigatorQ9BS26.

Family and domain databases

Gene3D3.40.30.10. 2 hits.
InterProIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 3 hits.
PROSITEPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSERP44. human.
EvolutionaryTraceQ9BS26.
GeneWikiERP44.
GenomeRNAi23071.
NextBio44171.
PROQ9BS26.
SOURCESearch...

Entry information

Entry nameERP44_HUMAN
AccessionPrimary (citable) accession number: Q9BS26
Secondary accession number(s): O60319 expand/collapse secondary AC list , Q4VXC1, Q5VWZ7, Q6UW14, Q8WX67
Entry history
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM