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Q15011 (HERP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein
Alternative name(s):
Methyl methanesulfonate (MMF)-inducible fragment protein 1
Gene names
Name:HERPUD1
Synonyms:HERP, KIAA0025, MIF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the endoplasmic reticulum quality control (ERQC) system also called ER-associated degradation (ERAD) involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Could enhance presenilin-mediated beta-amyloid protein 40 generation. Ref.10

Subunit structure

Interacts with PSEN1 and PSEN2. Interacts with SYVN1 and UBXN6. Ref.8 Ref.10 Ref.12

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.1.

Tissue specificity

Widely expressed; in the brain, expression seems to be restricted to neurons and vascular smooth muscle cells. Present in activated microglia in senile plaques in the brain of patients with Alzheimer disease.

Induction

Up-regulated by endoplasmic reticulum stress and CREB3. Ref.1 Ref.11

Miscellaneous

Although the precise topology is not known, experimental data suggest that both the N- and C-termini face the cytosol.

Sequence similarities

Contains 1 ubiquitin-like domain.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q15011-1)

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.
Isoform 2 (identifier: Q15011-2)

The sequence of this isoform differs from the canonical sequence as follows:
     76-76: Missing.
Isoform 3 (identifier: Q15011-3)

The sequence of this isoform differs from the canonical sequence as follows:
     76-76: Missing.
     145-302: Missing.
Isoform 4 (identifier: Q15011-4)

The sequence of this isoform differs from the canonical sequence as follows:
     75-99: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 391391Homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein
PRO_0000114920

Regions

Topological domain1 – 263263Cytoplasmic Potential
Transmembrane264 – 28421Helical; Potential
Topological domain285 – 2895Lumenal Potential
Transmembrane290 – 31021Helical; Potential
Topological domain311 – 39181Cytoplasmic Potential
Domain10 – 7263Ubiquitin-like

Amino acid modifications

Modified residue11N-acetylmethionine Ref.14

Natural variations

Alternative sequence75 – 9925Missing in isoform 4.
VSP_047333
Alternative sequence761Missing in isoform 2 and isoform 3.
VSP_006708
Alternative sequence145 – 302158Missing in isoform 3.
VSP_006709
Natural variant501R → H.
Corresponds to variant rs2217332 [ dbSNP | Ensembl ].
VAR_024277

Secondary structure

..................... 391
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 3CA827DC7EF0ED22

FASTA39143,720
        10         20         30         40         50         60 
MESETEPEPV TLLVKSPNQR HRDLELSGDR GWSVGHLKAH LSRVYPERPR PEDQRLIYSG 

        70         80         90        100        110        120 
KLLLDHQCLR DLLPKQEKRH VLHLVCNVKS PSKMPEINAK VAESTEEPAG SNRGQYPEDS 

       130        140        150        160        170        180 
SSDGLRQREV LRNLSSPGWE NISRPEAAQQ AFQGLGPGFS GYTPYGWLQL SWFQQIYARQ 

       190        200        210        220        230        240 
YYMQYLAATA ASGAFVPPPS AQEIPVVSAP APAPIHNQFP AENQPANQNA APQVVVNPGA 

       250        260        270        280        290        300 
NQNLRMNAQG GPIVEEDDEI NRDWLDWTYS AATFSVFLSI LYFYSSLSRF LMVMGATVVM 

       310        320        330        340        350        360 
YLHHVGWFPF RPRPVQNFPN DGPPPDVVNQ DPNNNLQEGT DPETEDPNHL PPDRDVLDGE 

       370        380        390 
QTSPSFMSTA WLVFKTFFAS LLPEGPPAIA N 

« Hide

Isoform 2 [UniParc].

Checksum: 7BCA8854403C71AF
Show »

FASTA39043,592
Isoform 3 [UniParc].

Checksum: BE916EB3E3CD79C0
Show »

FASTA23226,220
Isoform 4 [UniParc].

Checksum: DD39A053E4D46626
Show »

FASTA36640,851

References

« Hide 'large scale' references
[1]"Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress."
Kokame K., Agarwala K.L., Kato H., Miyata T.
J. Biol. Chem. 275:32846-32853(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
Tissue: Umbilical vein endothelial cell.
[2]"Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Bone marrow.
[3]Yu W., Gibbs R.A.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[4]"Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response."
Kokame K., Kato H., Miyata T.
J. Biol. Chem. 276:9199-9205(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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 1 AND 3).
Tissue: Brain, Eye, Placenta and Testis.
[8]"Endoplasmic reticulum stress-inducible protein, Herp, enhances presenilin-mediated generation of amyloid beta-protein."
Sai X., Kawamura Y., Kokame K., Yamaguchi H., Shiraishi H., Suzuki R., Suzuki T., Kawaichi M., Miyata T., Kitamura T., De Strooper B., Yanagisawa K., Komano H.
J. Biol. Chem. 277:12915-12920(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSEN1 AND PSEN2.
[9]"The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded protein response pathway."
van Laar T., Schouten T., Hoogervorst E., van Eck M., van der Eb A.J., Terleth C.
FEBS Lett. 469:123-131(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
Tissue: Skin fibroblast.
[10]"The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway."
Schulze A., Standera S., Buerger E., Kikkert M., van Voorden S., Wiertz E., Koning F., Kloetzel P.-M., Seeger M.
J. Mol. Biol. 354:1021-1027(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SYVN1.
[11]"Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element."
Liang G., Audas T.E., Li Y., Cockram G.P., Dean J.D., Martyn A.C., Kokame K., Lu R.
Mol. Cell. Biol. 26:7999-8010(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[12]"Ubxd1 is a novel co-factor of the human p97 ATPase."
Madsen L., Andersen K.M., Prag S., Moos T., Semple C.A., Seeger M., Hartmann-Petersen R.
Int. J. Biochem. Cell Biol. 40:2927-2942(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBXN6.
[13]"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].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Solution structure of the UBL-domain of HERP."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2004) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 10-90.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB034989 mRNA. Translation: BAB07891.1.
D14695 mRNA. Translation: BAA03521.1.
AF055001 mRNA. Translation: AAC09355.1.
AF055003 mRNA. Translation: AAC09357.1.
AB034990 Genomic DNA. Translation: BAB19010.1.
CR457116 mRNA. Translation: CAG33397.1.
AC012181 Genomic DNA. No translation available.
BC000086 mRNA. Translation: AAH00086.1.
BC008320 mRNA. Translation: AAH08320.1.
BC009739 mRNA. Translation: AAH09739.1.
BC032673 mRNA. Translation: AAH32673.1.
RefSeqNP_001010989.1. NM_001010989.2.
NP_001259032.1. NM_001272103.1.
NP_055500.1. NM_014685.3.
UniGeneHs.146393.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGDNMR-A10-90[»]
ProteinModelPortalQ15011.
SMRQ15011. Positions 10-90.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115060. 26 interactions.
DIPDIP-46662N.
IntActQ15011. 10 interactions.
MINTMINT-2867283.
STRING9606.ENSP00000300302.

PTM databases

PhosphoSiteQ15011.

Polymorphism databases

DMDM3123034.

Proteomic databases

PaxDbQ15011.
PRIDEQ15011.

Protocols and materials databases

DNASU9709.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000300302; ENSP00000300302; ENSG00000051108. [Q15011-2]
ENST00000344114; ENSP00000340931; ENSG00000051108. [Q15011-3]
ENST00000379792; ENSP00000369118; ENSG00000051108. [Q15011-4]
ENST00000439977; ENSP00000409555; ENSG00000051108. [Q15011-1]
GeneID9709.
KEGGhsa:9709.
UCSCuc002eke.2. human. [Q15011-1]
uc002ekf.2. human. [Q15011-2]
uc031qwh.1. human. [Q15011-3]

Organism-specific databases

CTD9709.
GeneCardsGC16P056965.
HGNCHGNC:13744. HERPUD1.
HPACAB037041.
CAB037104.
HPA040754.
HPA041219.
MIM608070. gene.
neXtProtNX_Q15011.
PharmGKBPA29252.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259558.
HOGENOMHOG000252989.
HOVERGENHBG051899.
InParanoidQ15011.
KOK14027.
OMALSGDRSW.
OrthoDBEOG7QRQWK.
PhylomeDBQ15011.
TreeFamTF324319.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ15011.
BgeeQ15011.
CleanExHS_HERPUD1.
GenevestigatorQ15011.

Family and domain databases

InterProIPR000626. Ubiquitin-like.
[Graphical view]
PfamPF00240. ubiquitin. 1 hit.
[Graphical view]
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHERPUD1. human.
EvolutionaryTraceQ15011.
GeneWikiHERPUD1.
GenomeRNAi9709.
NextBio36487.
PROQ15011.
SOURCESearch...

Entry information

Entry nameHERP1_HUMAN
AccessionPrimary (citable) accession number: Q15011
Secondary accession number(s): E9PGD1 expand/collapse secondary AC list , O60644, Q6IAN8, Q96D92
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 136 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM