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Q9BS26

- ERP44_HUMAN

UniProt

Q9BS26 - ERP44_HUMAN

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Protein

Endoplasmic reticulum resident protein 44

Gene

ERP44

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

Functioni

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.2 Publications

GO - Molecular functioni

  1. protein disulfide isomerase activity Source: UniProtKB

GO - Biological processi

  1. cell redox homeostasis Source: UniProtKB
  2. glycoprotein metabolic process Source: UniProtKB
  3. protein folding Source: UniProtKB
  4. response to endoplasmic reticulum stress Source: UniProtKB
  5. response to unfolded protein Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Names & Taxonomyi

Protein namesi
Recommended name:
Endoplasmic reticulum resident protein 44
Short name:
ER protein 44
Short name:
ERp44
Alternative name(s):
Thioredoxin domain-containing protein 4
Gene namesi
Name:ERP44
Synonyms:KIAA0573, TXNDC4
ORF Names:UNQ532/PRO1075
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:18311. ERP44.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: MGI
  2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  3. endoplasmic reticulum lumen Source: UniProtKB
  4. endoplasmic reticulum membrane Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164719295.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Add
BLAST
Chaini30 – 406377Endoplasmic reticulum resident protein 44PRO_0000034180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 – 58Interchain (with ERO1L)1 Publication
Disulfide bondi189 ↔ 2411 Publication
Disulfide bondi301 ↔ 3181 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ9BS26.
PaxDbiQ9BS26.
PeptideAtlasiQ9BS26.
PRIDEiQ9BS26.

2D gel databases

REPRODUCTION-2DPAGEIPI00401264.

Expressioni

Inductioni

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

Gene expression databases

BgeeiQ9BS26.
CleanExiHS_TXNDC4.
GenevestigatoriQ9BS26.

Organism-specific databases

HPAiHPA001318.

Interactioni

Subunit structurei

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).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LMAN1P492573EBI-541644,EBI-1057738

Protein-protein interaction databases

BioGridi116704. 30 interactions.
IntActiQ9BS26. 14 interactions.
MINTiMINT-2816102.
STRINGi9606.ENSP00000262455.

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni36 – 383
Helixi39 – 457
Beta strandi47 – 548
Helixi59 – 7517
Beta strandi85 – 917
Turni92 – 943
Helixi96 – 1016
Beta strandi106 – 1149
Beta strandi117 – 1226
Helixi129 – 14012
Beta strandi145 – 1473
Beta strandi162 – 1687
Beta strandi170 – 1723
Helixi173 – 18513
Turni186 – 1883
Beta strandi190 – 1967
Beta strandi208 – 2125
Beta strandi214 – 2185
Helixi230 – 24112
Beta strandi244 – 2474
Helixi250 – 2578
Beta strandi263 – 2686
Helixi274 – 28613
Helixi288 – 2903
Turni291 – 2933
Beta strandi294 – 3007
Turni301 – 3044
Helixi305 – 3106
Helixi315 – 3173
Beta strandi319 – 3246
Beta strandi329 – 3313
Helixi336 – 3394
Helixi343 – 35311
Helixi387 – 3904
Turni394 – 3963

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R2JX-ray2.60A30-406[»]
ProteinModelPortaliQ9BS26.
SMRiQ9BS26. Positions 32-401.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BS26.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 138109ThioredoxinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 28550Interaction with ITPR1By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi403 – 4064Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Contains 1 thioredoxin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0526.
GeneTreeiENSGT00760000119201.
HOGENOMiHOG000007707.
InParanoidiQ9BS26.
KOiK17264.
OMAiENAPDMV.
OrthoDBiEOG718KCX.
PhylomeDBiQ9BS26.
TreeFamiTF106378.

Family and domain databases

Gene3Di3.40.30.10. 2 hits.
InterProiIPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view]
PfamiPF00085. Thioredoxin. 1 hit.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 3 hits.
PROSITEiPS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BS26-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHPAVFLSLP DLRCSLLLLV TWVFTPVTTE ITSLDTENID EILNNADVAL
60 70 80 90 100
VNFYADWCRF SQMLHPIFEE ASDVIKEEFP NENQVVFARV DCDQHSDIAQ
110 120 130 140 150
RYRISKYPTL KLFRNGMMMK REYRGQRSVK ALADYIRQQK SDPIQEIRDL
160 170 180 190 200
AEITTLDRSK RNIIGYFEQK DSDNYRVFER VANILHDDCA FLSAFGDVSK
210 220 230 240 250
PERYSGDNII YKPPGHSAPD MVYLGAMTNF DVTYNWIQDK CVPLVREITF
260 270 280 290 300
ENGEELTEEG LPFLILFHMK EDTESLEIFQ NEVARQLISE KGTINFLHAD
310 320 330 340 350
CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD
360 370 380 390 400
LHSGKLHREF HHGPDPTDTA PGEQAQDVAS SPPESSFQKL APSEYRYTLL

RDRDEL
Length:406
Mass (Da):46,971
Last modified:June 1, 2001 - v1
Checksum:i3865DCF3811BC263
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti35 – 351D → A in AAQ89407. (PubMed:12975309)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS35082.1.
RefSeqiNP_055866.1. NM_015051.1.
UniGeneiHs.154023.

Genome annotation databases

EnsembliENST00000262455; ENSP00000262455; ENSG00000023318.
GeneIDi23071.
KEGGihsa:23071.
UCSCiuc004bam.3. human.

Polymorphism databases

DMDMi31077035.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS35082.1.
RefSeqi NP_055866.1. NM_015051.1.
UniGenei Hs.154023.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2R2J X-ray 2.60 A 30-406 [» ]
ProteinModelPortali Q9BS26.
SMRi Q9BS26. Positions 32-401.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116704. 30 interactions.
IntActi Q9BS26. 14 interactions.
MINTi MINT-2816102.
STRINGi 9606.ENSP00000262455.

Polymorphism databases

DMDMi 31077035.

2D gel databases

REPRODUCTION-2DPAGE IPI00401264.

Proteomic databases

MaxQBi Q9BS26.
PaxDbi Q9BS26.
PeptideAtlasi Q9BS26.
PRIDEi Q9BS26.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262455 ; ENSP00000262455 ; ENSG00000023318 .
GeneIDi 23071.
KEGGi hsa:23071.
UCSCi uc004bam.3. human.

Organism-specific databases

CTDi 23071.
GeneCardsi GC09M102742.
HGNCi HGNC:18311. ERP44.
HPAi HPA001318.
MIMi 609170. gene.
neXtProti NX_Q9BS26.
PharmGKBi PA164719295.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0526.
GeneTreei ENSGT00760000119201.
HOGENOMi HOG000007707.
InParanoidi Q9BS26.
KOi K17264.
OMAi ENAPDMV.
OrthoDBi EOG718KCX.
PhylomeDBi Q9BS26.
TreeFami TF106378.

Miscellaneous databases

ChiTaRSi ERP44. human.
EvolutionaryTracei Q9BS26.
GeneWikii ERP44.
GenomeRNAii 23071.
NextBioi 44171.
PROi Q9BS26.
SOURCEi Search...

Gene expression databases

Bgeei Q9BS26.
CleanExi HS_TXNDC4.
Genevestigatori Q9BS26.

Family and domain databases

Gene3Di 3.40.30.10. 2 hits.
InterProi IPR012336. Thioredoxin-like_fold.
IPR013766. Thioredoxin_domain.
[Graphical view ]
Pfami PF00085. Thioredoxin. 1 hit.
[Graphical view ]
SUPFAMi SSF52833. SSF52833. 3 hits.
PROSITEi PS00014. ER_TARGET. 1 hit.
PS51352. THIOREDOXIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiERP44_HUMAN
AccessioniPrimary (citable) accession number: Q9BS26
Secondary accession number(s): O60319
, Q4VXC1, Q5VWZ7, Q6UW14, Q8WX67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 128 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3