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Protein

Breast cancer metastasis-suppressor 1-like protein

Gene

BRMS1L

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

Functioni

Involved in the histone deacetylase (HDAC1)-dependent transcriptional repression activity. When overexpressed in lung cancer cell line that lacks p53/TP53 expression, inhibits cell growth.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Growth regulation, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Breast cancer metastasis-suppressor 1-like protein
Alternative name(s):
BRMS1-homolog protein p40
BRMS1-like protein p40
Gene namesi
Name:BRMS1L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20512. BRMS1L.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134968356.

Polymorphism and mutation databases

BioMutaiBRMS1L.
DMDMi158706476.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Breast cancer metastasis-suppressor 1-like proteinPRO_0000305309Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei197 – 1971PhosphoserineCombined sources
Cross-linki240 – 240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki246 – 246Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ5PSV4.
MaxQBiQ5PSV4.
PaxDbiQ5PSV4.
PeptideAtlasiQ5PSV4.
PRIDEiQ5PSV4.

PTM databases

iPTMnetiQ5PSV4.
PhosphoSiteiQ5PSV4.

Expressioni

Gene expression databases

BgeeiQ5PSV4.
CleanExiHS_BRMS1L.
ExpressionAtlasiQ5PSV4. baseline and differential.
GenevisibleiQ5PSV4. HS.

Organism-specific databases

HPAiHPA046623.

Interactioni

Subunit structurei

Component of the Sin3/HDAC1 corepressor complex at least composed of BRMS1, BRMS1L and ING2/ING1L. Interacts with HDAC and SIN3A.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTN2P356093EBI-5666615,EBI-77797
AMOTL2Q9Y2J4-43EBI-5666615,EBI-10187270
CCDC67E9PJR53EBI-5666615,EBI-10177066
EXOC5Q8IW243EBI-5666615,EBI-10171392
MID2Q9UJV3-23EBI-5666615,EBI-10172526

GO - Molecular functioni

Protein-protein interaction databases

BioGridi124038. 25 interactions.
IntActiQ5PSV4. 11 interactions.
STRINGi9606.ENSP00000216807.

Structurei

3D structure databases

ProteinModelPortaliQ5PSV4.
SMRiQ5PSV4. Positions 52-91.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili52 – 8433Sequence analysisAdd
BLAST
Coiled coili149 – 18032Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the BRMS1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4466. Eukaryota.
ENOG410Y9N9. LUCA.
GeneTreeiENSGT00530000063177.
HOGENOMiHOG000007483.
HOVERGENiHBG050734.
InParanoidiQ5PSV4.
KOiK19196.
OMAiEWYGRGQ.
OrthoDBiEOG783MZ0.
PhylomeDBiQ5PSV4.
TreeFamiTF323740.

Family and domain databases

InterProiIPR013907. Sds3.
[Graphical view]
PfamiPF08598. Sds3. 1 hit.
[Graphical view]
SMARTiSM01401. Sds3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5PSV4-1) [UniParc]FASTAAdd to basket

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
MPVHSRGDKK ETNHHDEMEV DYAENEGSSS EDEDTESSSV SEDGDSSEMD
60 70 80 90 100
DEDCERRRME CLDEMSNLEK QFTDLKDQLY KERLSQVDAK LQEVIAGKAP
110 120 130 140 150
EYLEPLATLQ ENMQIRTKVA GIYRELCLES VKNKYECEIQ ASRQHCESEK
160 170 180 190 200
LLLYDTVQSE LEEKIRRLEE DRHSIDITSE LWNDELQSRK KRKDPFSPDK
210 220 230 240 250
KKPVVVSGPY IVYMLQDLDI LEDWTTIRKA MATLGPHRVK TEPPVKLEKH
260 270 280 290 300
LHSARSEEGR LYYDGEWYIR GQTICIDKKD ECPTSAVITT INHDEVWFKR
310 320
PDGSKSKLYI SQLQKGKYSI KHS
Length:323
Mass (Da):37,629
Last modified:October 2, 2007 - v2
Checksum:i35908ACFD439A117
GO
Isoform 2 (identifier: Q5PSV4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.

Note: No experimental confirmation available.
Show »
Length:275
Mass (Da):32,345
Checksum:i8EB074B3F841B4E3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061V → G in AAV83797 (PubMed:15451426).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4848Missing in isoform 2. 1 PublicationVSP_055547Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY827074 mRNA. Translation: AAV83797.1.
AK315424 mRNA. Translation: BAG37812.1.
AL162311 Genomic DNA. No translation available.
BC006250 mRNA. Translation: AAH06250.2.
CCDSiCCDS32066.1. [Q5PSV4-1]
RefSeqiNP_115728.2. NM_032352.3. [Q5PSV4-1]
XP_006720338.1. XM_006720275.2. [Q5PSV4-2]
UniGeneiHs.525299.

Genome annotation databases

EnsembliENST00000216807; ENSP00000216807; ENSG00000100916. [Q5PSV4-1]
GeneIDi84312.
KEGGihsa:84312.
UCSCiuc001wtl.4. human. [Q5PSV4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY827074 mRNA. Translation: AAV83797.1.
AK315424 mRNA. Translation: BAG37812.1.
AL162311 Genomic DNA. No translation available.
BC006250 mRNA. Translation: AAH06250.2.
CCDSiCCDS32066.1. [Q5PSV4-1]
RefSeqiNP_115728.2. NM_032352.3. [Q5PSV4-1]
XP_006720338.1. XM_006720275.2. [Q5PSV4-2]
UniGeneiHs.525299.

3D structure databases

ProteinModelPortaliQ5PSV4.
SMRiQ5PSV4. Positions 52-91.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124038. 25 interactions.
IntActiQ5PSV4. 11 interactions.
STRINGi9606.ENSP00000216807.

PTM databases

iPTMnetiQ5PSV4.
PhosphoSiteiQ5PSV4.

Polymorphism and mutation databases

BioMutaiBRMS1L.
DMDMi158706476.

Proteomic databases

EPDiQ5PSV4.
MaxQBiQ5PSV4.
PaxDbiQ5PSV4.
PeptideAtlasiQ5PSV4.
PRIDEiQ5PSV4.

Protocols and materials databases

DNASUi84312.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216807; ENSP00000216807; ENSG00000100916. [Q5PSV4-1]
GeneIDi84312.
KEGGihsa:84312.
UCSCiuc001wtl.4. human. [Q5PSV4-1]

Organism-specific databases

CTDi84312.
GeneCardsiBRMS1L.
HGNCiHGNC:20512. BRMS1L.
HPAiHPA046623.
neXtProtiNX_Q5PSV4.
PharmGKBiPA134968356.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4466. Eukaryota.
ENOG410Y9N9. LUCA.
GeneTreeiENSGT00530000063177.
HOGENOMiHOG000007483.
HOVERGENiHBG050734.
InParanoidiQ5PSV4.
KOiK19196.
OMAiEWYGRGQ.
OrthoDBiEOG783MZ0.
PhylomeDBiQ5PSV4.
TreeFamiTF323740.

Miscellaneous databases

GenomeRNAii84312.
PROiQ5PSV4.

Gene expression databases

BgeeiQ5PSV4.
CleanExiHS_BRMS1L.
ExpressionAtlasiQ5PSV4. baseline and differential.
GenevisibleiQ5PSV4. HS.

Family and domain databases

InterProiIPR013907. Sds3.
[Graphical view]
PfamiPF08598. Sds3. 1 hit.
[Graphical view]
SMARTiSM01401. Sds3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel BRMS1-homologue protein p40 as a component of the mSin3A/p33(ING1b)/HDAC1 deacetylase complex."
    Nikolaev A.Y., Papanikolaou N.A., Li M., Qin J., Gu W.
    Biochem. Biophys. Res. Commun. 323:1216-1222(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN THE SIN3/HDAC1 COMPLEX, INTERACTION WITH HDAC AND SIN3A.
  2. "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] (ISOFORM 2).
  3. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 1).
    Tissue: Ovary.
  5. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli."
    Impens F., Radoshevich L., Cossart P., Ribet D.
    Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability."
    Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C.
    Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-240, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBRM1L_HUMAN
AccessioniPrimary (citable) accession number: Q5PSV4
Secondary accession number(s): A6NFW5
, A6NH45, B2RD65, Q9BRI4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 2, 2007
Last modified: July 6, 2016
This is version 93 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. 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.