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

Protein CREG1

Gene

Creg1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

May contribute to the transcriptional control of cell growth and differentiation. Antagonizes transcriptional activation and cellular transformation by the adenovirus E1A protein. The transcriptional control activity of cell growth requires interaction with IGF2R (By similarity).By similarity

GO - Molecular functioni

  1. FMN binding Source: InterPro
  2. oxidoreductase activity Source: InterPro
  3. transcription factor binding Source: MGI

GO - Biological processi

  1. regulation of growth Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: MGI
Complete GO annotation...

Keywords - Biological processi

Growth regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein CREG1
Alternative name(s):
Cellular repressor of E1A-stimulated genes 1
Gene namesi
Name:Creg1
Synonyms:Creg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:1344382. Creg1.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
  2. transcription factor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 220189Protein CREG1PRO_0000006204Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi160 – 1601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi216 – 2161N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.By similarity

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO88668.
PaxDbiO88668.
PRIDEiO88668.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Developmental stagei

Found at low level from E7 embryo and increased during embryonic development.1 Publication

Inductioni

Induced during differentiation.1 Publication

Gene expression databases

BgeeiO88668.
CleanExiMM_CREG1.
ExpressionAtlasiO88668. baseline and differential.
GenevestigatoriO88668.

Interactioni

Subunit structurei

Homodimer. Interacts with IGF2R; the interaction is dependent on glycosylation (By similarity).By similarity

Protein-protein interaction databases

IntActiO88668. 1 interaction.
MINTiMINT-1846777.

Structurei

3D structure databases

ProteinModelPortaliO88668.
SMRiO88668. Positions 49-218.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the CREG family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG294476.
GeneTreeiENSGT00390000005914.
HOGENOMiHOG000239875.
HOVERGENiHBG051115.
InParanoidiO88668.
OMAiEYYNATF.
OrthoDBiEOG7ZWD33.
PhylomeDBiO88668.
TreeFamiTF324680.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR014631. CREG.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PIRSFiPIRSF036911. CREG. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.

Sequencei

Sequence statusi: Complete.

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

O88668-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARAPELAR SLLAALLAPA LVALLVSPAS GRGGRDHGDW DVDRRLPPLP
60 70 80 90 100
PREDGPRVAR FVTHVSDWGS LATISTIKEV RGWPFADIIS ISDGPPGEGT
110 120 130 140 150
GEPYMYLSPL QQAVSDLQEN PEATLTMSLA QTVYCRNHGF DPQSPLCVHI
160 170 180 190 200
MMSGTVTKVN KTEEDYARDS LFVRHPEMKH WPSSHNWFFA KLKISRIWVL
210 220
DYFGGPKVVT PEEYFNVTLQ
Length:220
Mass (Da):24,452
Last modified:October 31, 1998 - v1
Checksum:iEF3A8CFD3186163D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621V → M in BAC39549 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084524 mRNA. Translation: AAC34862.1.
AK005388 mRNA. Translation: BAB23994.1.
AK010947 mRNA. Translation: BAB27285.1.
AK085844 mRNA. Translation: BAC39549.1.
AK144101 mRNA. Translation: BAE25699.1.
BC027426 mRNA. Translation: AAH27426.1.
CCDSiCCDS35759.1.
RefSeqiNP_035934.1. NM_011804.2.
XP_006496993.1. XM_006496930.1.
UniGeneiMm.294885.
Mm.468745.

Genome annotation databases

EnsembliENSMUST00000111432; ENSMUSP00000107060; ENSMUSG00000040713.
GeneIDi433375.
KEGGimmu:433375.
UCSCiuc007djm.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084524 mRNA. Translation: AAC34862.1.
AK005388 mRNA. Translation: BAB23994.1.
AK010947 mRNA. Translation: BAB27285.1.
AK085844 mRNA. Translation: BAC39549.1.
AK144101 mRNA. Translation: BAE25699.1.
BC027426 mRNA. Translation: AAH27426.1.
CCDSiCCDS35759.1.
RefSeqiNP_035934.1. NM_011804.2.
XP_006496993.1. XM_006496930.1.
UniGeneiMm.294885.
Mm.468745.

3D structure databases

ProteinModelPortaliO88668.
SMRiO88668. Positions 49-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO88668. 1 interaction.
MINTiMINT-1846777.

Proteomic databases

MaxQBiO88668.
PaxDbiO88668.
PRIDEiO88668.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000111432; ENSMUSP00000107060; ENSMUSG00000040713.
GeneIDi433375.
KEGGimmu:433375.
UCSCiuc007djm.1. mouse.

Organism-specific databases

CTDi8804.
MGIiMGI:1344382. Creg1.

Phylogenomic databases

eggNOGiNOG294476.
GeneTreeiENSGT00390000005914.
HOGENOMiHOG000239875.
HOVERGENiHBG051115.
InParanoidiO88668.
OMAiEYYNATF.
OrthoDBiEOG7ZWD33.
PhylomeDBiO88668.
TreeFamiTF324680.

Miscellaneous databases

ChiTaRSiCreg1. mouse.
NextBioi408624.
PROiO88668.
SOURCEiSearch...

Gene expression databases

BgeeiO88668.
CleanExiMM_CREG1.
ExpressionAtlasiO88668. baseline and differential.
GenevestigatoriO88668.

Family and domain databases

Gene3Di2.30.110.10. 1 hit.
InterProiIPR014631. CREG.
IPR012349. Split_barrel_FMN-bd.
[Graphical view]
PIRSFiPIRSF036911. CREG. 1 hit.
SUPFAMiSSF50475. SSF50475. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A cellular repressor of E1A-stimulated genes that inhibits activation by E2F."
    Veal E., Eisenstein M., Tseng Z.H., Gill G.
    Mol. Cell. Biol. 18:5032-5041(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Heart, Kidney, Liver and Placenta.
  3. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and FVB/N.
    Tissue: Mammary tumor.
  4. "The secreted glycoprotein CREG enhances differentiation of NTERA-2 human embryonal carcinoma cells."
    Veal E., Groisman R., Eisenstein M., Gill G.
    Oncogene 19:2120-2128(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiCREG1_MOUSE
AccessioniPrimary (citable) accession number: O88668
Secondary accession number(s): Q3UNP8, Q8C3I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 14, 2005
Last sequence update: October 31, 1998
Last modified: February 3, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.