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Protein

BRCA1-associated protein

Gene

Brap

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

Functioni

Negatively regulates MAP kinase activation by limiting the formation of Raf/MEK complexes probably by inactivation of the KSR1 scaffold protein. Also acts as a Ras responsive E3 ubiquitin ligase that, on activation of Ras, is modified by auto-polyubiquitination resulting in the release of inhibition of Raf/MEK complex formation. May also act as a cytoplasmic retention protein with a role in regulating nuclear transport (By similarity).By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri263 – 30341RING-typePROSITE-ProRule annotationCuratedAdd
BLAST
Zinc fingeri314 – 37562UBP-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-5673000. RAF activation.
R-MMU-5675221. Negative regulation of MAPK pathway.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
BRCA1-associated protein (EC:6.3.2.-)
Alternative name(s):
BRAP2
Impedes mitogenic signal propagation
Short name:
IMP
Gene namesi
Name:BrapImported
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1919649. Brap.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 591591BRCA1-associated proteinPRO_0000055826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei118 – 1181PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99MP8.
MaxQBiQ99MP8.
PaxDbiQ99MP8.
PRIDEiQ99MP8.

PTM databases

iPTMnetiQ99MP8.
PhosphoSiteiQ99MP8.

Expressioni

Tissue specificityi

Isoform 2 is highly expressed in testis, lower levels in brain, heart, lung, stomach, colon, uterus, liver and kidney. Isoform 1 is only expressed in the testis. Isoform 2 is predominant over isoform 1 in both fetal and adult testis.1 Publication

Gene expression databases

BgeeiQ99MP8.
CleanExiMM_BRAP.
ExpressionAtlasiQ99MP8. baseline and differential.
GenevisibleiQ99MP8. MM.

Interactioni

Subunit structurei

Interacts with the nuclear localization signal of BRCA1 and with the N-terminal of KSR1. The C-terminal portion of BRCA1 interacts with DDB1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Akap3O889873EBI-10818333,EBI-9033539

GO - Molecular functioni

Protein-protein interaction databases

BioGridi215356. 8 interactions.
IntActiQ99MP8. 3 interactions.
STRINGi10090.ENSMUSP00000031414.

Structurei

3D structure databases

ProteinModelPortaliQ99MP8.
SMRiQ99MP8. Positions 255-307, 316-368.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili430 – 536107Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotationCurated
Contains 1 UBP-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri263 – 30341RING-typePROSITE-ProRule annotationCuratedAdd
BLAST
Zinc fingeri314 – 37562UBP-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG0804. Eukaryota.
ENOG410XSS2. LUCA.
GeneTreeiENSGT00500000044909.
HOGENOMiHOG000190616.
HOVERGENiHBG050729.
InParanoidiQ99MP8.
KOiK10632.
OMAiCLQRWED.
OrthoDBiEOG7XM2X9.
PhylomeDBiQ99MP8.
TreeFamiTF313622.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.30.70.330. 1 hit.
InterProiIPR011422. BRAP2.
IPR012677. Nucleotide-bd_a/b_plait.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF07576. BRAP2. 1 hit.
PF13639. zf-RING_2. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
ProDomiPD017029. BRAP2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00184. RING. 1 hit.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50089. ZF_RING_2. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 11 Publication (identifier: Q99MP8-1) [UniParc]FASTAAdd to basket

Also known as: alpha1 Publication

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.

« Hide

        10         20         30         40         50
MSVSLVVIRL ELAGHSPVPT DFGFSAAAGE MSDEEIKKKT LASAVACLEG
60 70 80 90 100
KSAGEKAAII HQHLGRREMT DVIIETMKAR ADEVRDTVEE KKPSAAPVSA
110 120 130 140 150
QRSREQSESV NTAPESPSKQ LPDQISFFSG NPSVEIVHGI MHLYKTNKMT
160 170 180 190 200
SLKEDVRRSA MLCVLTVPAT MTSHDLMKFV APFNDVIEQM KIIRDSTPNQ
210 220 230 240 250
YMVLIKFSAQ ADADSFYMAC NGRQFNSIED DVCQLVYVER AEVLKSEDGA
260 270 280 290 300
SLPVMDLTEL PKCTVCLERM DESVNGILTT LCNHSFHSQC LQRWDDTTCP
310 320 330 340 350
VCRYCQTPEP VEENKCFECG VQENLWICLI CGHIGCGRYV SRHAYKHFEE
360 370 380 390 400
TQHTYAMQLT NHRVWDYAGD NYVHRLVASK TDGKIVQYEC EGDTCQEEKI
410 420 430 440 450
DALQLEYSYL LTSQLESQRI YWENKIVRIE KDTAEEINNM KTKFKETIEK
460 470 480 490 500
CDSLELRLSD LLKEKQSVER KCTQLNTRVA KLSTELQEEQ ELNKCLRANQ
510 520 530 540 550
LVLQNQLKEE EKLLKETCAQ KDLQITEIQE QLRDVMFYLE TQQQISHLPA
560 570 580 590
ETRQEIQEGQ INIAMASAPN PPSSGAGGKL QSRKGRSKRG K
Length:591
Mass (Da):66,991
Last modified:June 1, 2001 - v1
Checksum:iDF925A28C0388E72
GO
Isoform 21 Publication (identifier: Q99MP8-2) [UniParc]FASTAAdd to basket

Also known as: beta1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.

Show »
Length:561
Mass (Da):63,951
Checksum:i54DBA485E084D520
GO
Isoform 3Curated (identifier: Q99MP8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-217: Missing.

Note: No experimental confirmation available.Curated
Show »
Length:374
Mass (Da):43,165
Checksum:iBC8C4F2F1E3EE012
GO

Sequence cautioni

The sequence BAB29036.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111N → I (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 217217Missing in isoform 3. 1 PublicationVSP_050762Add
BLAST
Alternative sequencei1 – 3030Missing in isoform 2. 1 PublicationVSP_050761Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF321920 mRNA. Translation: AAK28079.1.
AF321921 mRNA. Translation: AAK28080.1.
BC038490 mRNA. Translation: AAH38490.1.
AK013885 mRNA. Translation: BAB29036.1. Different initiation.
AK034212 mRNA. Translation: BAC28633.1.
CCDSiCCDS19640.1. [Q99MP8-1]
CCDS80389.1. [Q99MP8-2]
RefSeqiNP_001276473.1. NM_001289544.1. [Q99MP8-2]
NP_082503.2. NM_028227.3. [Q99MP8-1]
XP_006530532.1. XM_006530469.1.
XP_011246544.1. XM_011248242.1. [Q99MP8-2]
UniGeneiMm.153372.

Genome annotation databases

EnsembliENSMUST00000031414; ENSMUSP00000031414; ENSMUSG00000029458. [Q99MP8-1]
ENSMUST00000111765; ENSMUSP00000107395; ENSMUSG00000029458. [Q99MP8-2]
GeneIDi72399.
KEGGimmu:72399.
UCSCiuc008zkc.2. mouse. [Q99MP8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF321920 mRNA. Translation: AAK28079.1.
AF321921 mRNA. Translation: AAK28080.1.
BC038490 mRNA. Translation: AAH38490.1.
AK013885 mRNA. Translation: BAB29036.1. Different initiation.
AK034212 mRNA. Translation: BAC28633.1.
CCDSiCCDS19640.1. [Q99MP8-1]
CCDS80389.1. [Q99MP8-2]
RefSeqiNP_001276473.1. NM_001289544.1. [Q99MP8-2]
NP_082503.2. NM_028227.3. [Q99MP8-1]
XP_006530532.1. XM_006530469.1.
XP_011246544.1. XM_011248242.1. [Q99MP8-2]
UniGeneiMm.153372.

3D structure databases

ProteinModelPortaliQ99MP8.
SMRiQ99MP8. Positions 255-307, 316-368.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi215356. 8 interactions.
IntActiQ99MP8. 3 interactions.
STRINGi10090.ENSMUSP00000031414.

PTM databases

iPTMnetiQ99MP8.
PhosphoSiteiQ99MP8.

Proteomic databases

EPDiQ99MP8.
MaxQBiQ99MP8.
PaxDbiQ99MP8.
PRIDEiQ99MP8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031414; ENSMUSP00000031414; ENSMUSG00000029458. [Q99MP8-1]
ENSMUST00000111765; ENSMUSP00000107395; ENSMUSG00000029458. [Q99MP8-2]
GeneIDi72399.
KEGGimmu:72399.
UCSCiuc008zkc.2. mouse. [Q99MP8-1]

Organism-specific databases

CTDi8315.
MGIiMGI:1919649. Brap.

Phylogenomic databases

eggNOGiKOG0804. Eukaryota.
ENOG410XSS2. LUCA.
GeneTreeiENSGT00500000044909.
HOGENOMiHOG000190616.
HOVERGENiHBG050729.
InParanoidiQ99MP8.
KOiK10632.
OMAiCLQRWED.
OrthoDBiEOG7XM2X9.
PhylomeDBiQ99MP8.
TreeFamiTF313622.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-5673000. RAF activation.
R-MMU-5675221. Negative regulation of MAPK pathway.

Miscellaneous databases

NextBioi336190.
PROiQ99MP8.
SOURCEiSearch...

Gene expression databases

BgeeiQ99MP8.
CleanExiMM_BRAP.
ExpressionAtlasiQ99MP8. baseline and differential.
GenevisibleiQ99MP8. MM.

Family and domain databases

Gene3Di3.30.40.10. 2 hits.
3.30.70.330. 1 hit.
InterProiIPR011422. BRAP2.
IPR012677. Nucleotide-bd_a/b_plait.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR001607. Znf_UBP.
[Graphical view]
PfamiPF07576. BRAP2. 1 hit.
PF13639. zf-RING_2. 1 hit.
PF02148. zf-UBP. 1 hit.
[Graphical view]
ProDomiPD017029. BRAP2. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00184. RING. 1 hit.
SM00290. ZnF_UBP. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50089. ZF_RING_2. 1 hit.
PS50271. ZF_UBP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential."
    Nakajima A., Kataoka K., Hong M., Sakaguchi M., Huh N.-H.
    Cancer Lett. 201:195-201(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Strain: ICRImported.
    Tissue: TestisImported.
  2. "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] (ISOFORM 3).
    Strain: FVB/NImported.
    Tissue: Mammary tumor.
  3. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 102-591 (ISOFORMS 1/2).
    Strain: C57BL/6J.
    Tissue: Diencephalon and Embryo.

Entry informationi

Entry nameiBRAP_MOUSE
AccessioniPrimary (citable) accession number: Q99MP8
Secondary accession number(s): Q8CC00
, Q8CHX1, Q99MP7, Q9CXX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 120 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.