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Q9BS26

- ERP44_HUMAN

UniProt

Q9BS26 - ERP44_HUMAN

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
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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 binding Source: IntAct
    2. 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

    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

    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.
    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

    MHPAVFLSLP DLRCSLLLLV TWVFTPVTTE ITSLDTENID EILNNADVAL    50
    VNFYADWCRF SQMLHPIFEE ASDVIKEEFP NENQVVFARV DCDQHSDIAQ 100
    RYRISKYPTL KLFRNGMMMK REYRGQRSVK ALADYIRQQK SDPIQEIRDL 150
    AEITTLDRSK RNIIGYFEQK DSDNYRVFER VANILHDDCA FLSAFGDVSK 200
    PERYSGDNII YKPPGHSAPD MVYLGAMTNF DVTYNWIQDK CVPLVREITF 250
    ENGEELTEEG LPFLILFHMK EDTESLEIFQ NEVARQLISE KGTINFLHAD 300
    CDKFRHPLLH IQKTPADCPV IAIDSFRHMY VFGDFKDVLI PGKLKQFVFD 350
    LHSGKLHREF HHGPDPTDTA PGEQAQDVAS SPPESSFQKL APSEYRYTLL 400
    RDRDEL 406
    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.
    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

    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 1, 2014
    This is version 127 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