Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Anterior gradient protein 2 homolog

Gene

AGR2

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

Functioni

Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth.By similarity1 Publication

GO - Molecular functioni

  1. dystroglycan binding Source: UniProtKB

GO - Biological processi

  1. lung goblet cell differentiation Source: Ensembl
  2. mucus secretion Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Anterior gradient protein 2 homolog
Short name:
AG-2
Short name:
hAG-2
Alternative name(s):
HPC8
Secreted cement gland protein XAG-2 homolog
Gene namesi
Name:AGR2
Synonyms:AG2
ORF Names:UNQ515/PRO1030
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:328. AGR2.

Subcellular locationi

  1. Secreted 1 Publication
  2. Endoplasmic reticulum By similarity

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. extracellular region Source: UniProtKB-SubCell
  3. mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi81 – 811C → S: Loss of interaction with MUC2. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA24625.

Polymorphism and mutation databases

BioMutaiAGR2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 20201 PublicationAdd
BLAST
Chaini21 – 175155Anterior gradient protein 2 homologPRO_0000001037Add
BLAST

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiO95994.
PaxDbiO95994.
PRIDEiO95994.

PTM databases

PhosphoSiteiO95994.

Expressioni

Tissue specificityi

Expressed strongly in trachea, lung, stomach, colon, prostate and small intestine. Expressed weakly in pituitary gland, salivary gland, mammary gland, bladder, appendix, ovary, fetal lung, uterus, pancreas, kidney, fetal kidney, testis, placenta, thyroid gland and in estrogen receptor (ER)-positive breast cancer cell lines.1 Publication

Gene expression databases

BgeeiO95994.
CleanExiHS_AGR2.
ExpressionAtlasiO95994. baseline and differential.
GenevestigatoriO95994.

Organism-specific databases

HPAiHPA007912.

Interactioni

Subunit structurei

Interacts with LYPD3 and DAG1 (alphaDAG1). Interacts with MUC2; disulfide-linked.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CATSPER1Q8NEC53EBI-712648,EBI-744545
FABP2P121043EBI-712648,EBI-3905109
KRT31Q153233EBI-712648,EBI-948001
NUP62CLQ9H1M03EBI-712648,EBI-751933
POM121Q96HA14EBI-712648,EBI-739990
UBQLN1Q9UMX03EBI-712648,EBI-741480
UBQLN1Q9UMX0-23EBI-712648,EBI-10173939

Protein-protein interaction databases

BioGridi115802. 20 interactions.
DIPiDIP-48825N.
IntActiO95994. 12 interactions.
MINTiMINT-2868509.
STRINGi9606.ENSP00000391490.

Structurei

Secondary structure

1
175
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi48 – 514Combined sources
Helixi58 – 669Combined sources
Turni67 – 693Combined sources
Beta strandi72 – 776Combined sources
Beta strandi79 – 813Combined sources
Helixi82 – 9110Combined sources
Helixi95 – 1028Combined sources
Beta strandi103 – 1053Combined sources
Beta strandi109 – 1113Combined sources
Turni116 – 1183Combined sources
Beta strandi127 – 1326Combined sources
Turni133 – 1353Combined sources
Turni146 – 1505Combined sources
Turni154 – 1563Combined sources
Helixi157 – 16711Combined sources
Beta strandi171 – 1733Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LNSNMR-A/B41-175[»]
2LNTNMR-A41-175[»]
ProteinModelPortaliO95994.
SMRiO95994. Positions 38-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AGR family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG78144.
HOGENOMiHOG000231100.
HOVERGENiHBG006516.
InParanoidiO95994.
OrthoDBiEOG7DNNX2.
PhylomeDBiO95994.
TreeFamiTF321449.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O95994-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKIPVSAFL LLVALSYTLA RDTTVKPGAK KDTKDSRPKL PQTLSRGWGD
60 70 80 90 100
QLIWTQTYEE ALYKSKTSNK PLMIIHHLDE CPHSQALKKV FAENKEIQKL
110 120 130 140 150
AEQFVLLNLV YETTDKHLSP DGQYVPRIMF VDPSLTVRAD ITGRYSNRLY
160 170
AYEPADTALL LDNMKKALKL LKTEL
Length:175
Mass (Da):19,979
Last modified:May 1, 1999 - v1
Checksum:iF271B1BD377BEE11
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007791 mRNA. Translation: AAC77358.1.
AF038451 mRNA. Translation: AAC82614.1.
AF088867 mRNA. Translation: AAF22484.1.
AF115926 mRNA. Translation: AAL54870.1.
AF087879 mRNA. Translation: AAP97179.1.
AY359009 mRNA. Translation: AAQ89368.1.
BT007048 mRNA. Translation: AAP35697.1.
AC073333 Genomic DNA. Translation: AAP22354.1.
BC015503 mRNA. Translation: AAH15503.1.
CCDSiCCDS5364.1.
PIRiJE0350.
RefSeqiNP_006399.1. NM_006408.3.
XP_005249638.1. XM_005249581.3.
UniGeneiHs.530009.

Genome annotation databases

EnsembliENST00000419304; ENSP00000391490; ENSG00000106541.
GeneIDi10551.
KEGGihsa:10551.
UCSCiuc003str.3. human.

Polymorphism and mutation databases

BioMutaiAGR2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007791 mRNA. Translation: AAC77358.1.
AF038451 mRNA. Translation: AAC82614.1.
AF088867 mRNA. Translation: AAF22484.1.
AF115926 mRNA. Translation: AAL54870.1.
AF087879 mRNA. Translation: AAP97179.1.
AY359009 mRNA. Translation: AAQ89368.1.
BT007048 mRNA. Translation: AAP35697.1.
AC073333 Genomic DNA. Translation: AAP22354.1.
BC015503 mRNA. Translation: AAH15503.1.
CCDSiCCDS5364.1.
PIRiJE0350.
RefSeqiNP_006399.1. NM_006408.3.
XP_005249638.1. XM_005249581.3.
UniGeneiHs.530009.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LNSNMR-A/B41-175[»]
2LNTNMR-A41-175[»]
ProteinModelPortaliO95994.
SMRiO95994. Positions 38-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115802. 20 interactions.
DIPiDIP-48825N.
IntActiO95994. 12 interactions.
MINTiMINT-2868509.
STRINGi9606.ENSP00000391490.

PTM databases

PhosphoSiteiO95994.

Polymorphism and mutation databases

BioMutaiAGR2.

Proteomic databases

MaxQBiO95994.
PaxDbiO95994.
PRIDEiO95994.

Protocols and materials databases

DNASUi10551.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000419304; ENSP00000391490; ENSG00000106541.
GeneIDi10551.
KEGGihsa:10551.
UCSCiuc003str.3. human.

Organism-specific databases

CTDi10551.
GeneCardsiGC07M016831.
HGNCiHGNC:328. AGR2.
HPAiHPA007912.
MIMi606358. gene.
neXtProtiNX_O95994.
PharmGKBiPA24625.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG78144.
HOGENOMiHOG000231100.
HOVERGENiHBG006516.
InParanoidiO95994.
OrthoDBiEOG7DNNX2.
PhylomeDBiO95994.
TreeFamiTF321449.

Miscellaneous databases

ChiTaRSiAGR2. human.
GeneWikiiAGR2.
GenomeRNAii10551.
NextBioi40021.
PROiO95994.
SOURCEiSearch...

Gene expression databases

BgeeiO95994.
CleanExiHS_AGR2.
ExpressionAtlasiO95994. baseline and differential.
GenevestigatoriO95994.

Family and domain databases

Gene3Di3.40.30.10. 1 hit.
InterProiIPR012336. Thioredoxin-like_fold.
[Graphical view]
SUPFAMiSSF52833. SSF52833. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "hAG-2, the human homologue of the Xenopus laevis cement gland gene XAG-2, is coexpressed with estrogen receptor in breast cancer cell lines."
    Thompson D.A., Weigel R.J.
    Biochem. Biophys. Res. Commun. 251:111-116(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Mammary gland.
  2. "Identification of human homolog of XAG-2 over-expressed in tumors."
    Zhang J.S., Smith D.I.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Prostatic carcinoma.
  3. "Cloning and expression of a novel human cDNA homology to murine GOB-4 mRNA."
    Fan Y.X., Yu L., Zhang X.N., Wan W.C., Wang X.K., Zhao S.Y.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [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].
    Tissue: Colon.
  8. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
    Zhang Z., Henzel W.J.
    Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-35.
  9. "hAG-2 and hAG-3, human homologues of genes involved in differentiation, are associated with oestrogen receptor-positive breast tumours and interact with metastasis gene C4.4a and dystroglycan."
    Fletcher G.C., Patel S., Tyson K., Adam P.J., Schenker M., Loader J.A., Daviet L., Legrain P., Parekh R., Harris A.L., Terrett J.A.
    Br. J. Cancer 88:579-585(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LYPD3 AND DAG1.
  10. "AGR2, an androgen-inducible secretory protein overexpressed in prostate cancer."
    Zhang J.-S., Gong A., Cheville J.C., Smith D.I., Young C.Y.F.
    Genes Chromosomes Cancer 43:249-259(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  11. "The adenocarcinoma-associated antigen, AGR2, promotes tumor growth, cell migration, and cellular transformation."
    Wang Z., Hao Y., Lowe A.W.
    Cancer Res. 68:492-497(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The protein disulfide isomerase AGR2 is essential for production of intestinal mucus."
    Park S.-W., Zhen G., Verhaeghe C., Nakagami Y., Nguyenvu L.T., Barczak A.J., Killeen N., Erle D.J.
    Proc. Natl. Acad. Sci. U.S.A. 106:6950-6955(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MUC2, MUTAGENESIS OF CYS-81.

Entry informationi

Entry nameiAGR2_HUMAN
AccessioniPrimary (citable) accession number: O95994
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 1, 1999
Last modified: April 29, 2015
This is version 108 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 7
    Human chromosome 7: 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

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 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.