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Q8BSQ9

- PB1_MOUSE

UniProt

Q8BSQ9 - PB1_MOUSE

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Protein
Protein polybromo-1
Gene
Pbrm1, Baf180, Pb1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology) By similarity. Acts as a negative regulator of cell proliferation By similarity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi1379 – 144769HMG box
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. chromatin binding Source: MGI
  3. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. blood vessel remodeling Source: DFLAT
  2. cardiac vascular smooth muscle cell development Source: DFLAT
  3. chromatin modification Source: UniProtKB-KW
  4. epicardium-derived cardiac endothelial cell differentiation Source: DFLAT
  5. heart development Source: MGI
  6. heart morphogenesis Source: DFLAT
  7. negative regulation of cell proliferation Source: UniProtKB
  8. placenta development Source: MGI
  9. positive regulation of transcription, DNA-templated Source: DFLAT
  10. transcription, DNA-templated Source: UniProtKB-KW
  11. vasculogenesis involved in coronary vascular morphogenesis Source: DFLAT
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein polybromo-1
Alternative name(s):
BRG1-associated factor 180
Short name:
BAF180
Gene namesi
Name:Pbrm1
Synonyms:Baf180, Pb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1923998. Pbrm1.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. kinetochore Source: MGI
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16341634Protein polybromo-1
PRO_0000351134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine By similarity
Modified residuei39 – 391Phosphoserine By similarity
Modified residuei131 – 1311Phosphoserine By similarity
Modified residuei319 – 3191Phosphoserine By similarity
Modified residuei353 – 3531Phosphoserine1 Publication
Modified residuei355 – 3551Phosphoserine1 Publication
Modified residuei371 – 3711Phosphoserine By similarity
Modified residuei375 – 3751Phosphoserine By similarity
Modified residuei414 – 4141N6-acetyllysine1 Publication
Modified residuei498 – 4981Phosphoserine By similarity
Modified residuei636 – 6361Phosphoserine By similarity
Modified residuei648 – 6481Phosphoserine By similarity
Modified residuei1289 – 12891Phosphotyrosine1 Publication
Modified residuei1405 – 14051Phosphoserine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8BSQ9.
PaxDbiQ8BSQ9.
PRIDEiQ8BSQ9.

PTM databases

PhosphoSiteiQ8BSQ9.

Expressioni

Developmental stagei

Expressed ubiquitously throughout the developing spinal cord, brain and other embryonic tissues at E10.5-E16.5.1 Publication

Gene expression databases

ArrayExpressiQ8BSQ9.
BgeeiQ8BSQ9.
GenevestigatoriQ8BSQ9.

Interactioni

Subunit structurei

Component of the SWI/SNF-B (PBAF) chromatin-remodeling complex, which contains at least SMARCA4/BRG1, SMARCB1/SNF5/INI1/BAF47, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PB1/BAF180, ARID2/BAF200, ARID1A/BAF250A or ARID1B/BAF250B and actin. Interacts with acetylated 'Lys-14' of histone H3 (H3K14ac), and may also interact with other acetylated or methylated Lys residues on histone H3 By similarity. Interacts with PHF10/BAF45A.1 Publication

Protein-protein interaction databases

DIPiDIP-48885N.
IntActiQ8BSQ9. 2 interactions.
MINTiMINT-4112204.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi659 – 67113
Beta strandi675 – 6773
Beta strandi679 – 6813
Helixi682 – 6843
Turni690 – 6923
Helixi694 – 6996
Helixi706 – 7149
Helixi721 – 73818
Helixi744 – 75916

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YQDNMR-A650-762[»]
ProteinModelPortaliQ8BSQ9.
SMRiQ8BSQ9. Positions 43-154, 176-292, 388-494, 510-628, 651-766, 773-914, 957-1102.

Miscellaneous databases

EvolutionaryTraceiQ8BSQ9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini64 – 13471Bromo 1
Add
BLAST
Domaini200 – 27071Bromo 2
Add
BLAST
Domaini400 – 47071Bromo 3
Add
BLAST
Domaini538 – 60871Bromo 4
Add
BLAST
Domaini676 – 74671Bromo 5
Add
BLAST
Domaini792 – 86271Bromo 6
Add
BLAST
Domaini956 – 1074119BAH 1
Add
BLAST
Domaini1156 – 1272117BAH 2
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi630 – 6334Poly-Asp
Compositional biasi1468 – 1599132Pro-rich
Add
BLAST

Sequence similaritiesi

Contains 2 BAH domains.
Contains 6 bromo domains.

Keywords - Domaini

Bromodomain, Repeat

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00390000003017.
HOVERGENiHBG079860.
OrthoDBiEOG78H3S6.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
1.20.920.10. 6 hits.
InterProiIPR001025. BAH_dom.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR009071. HMG_box_dom.
[Graphical view]
PfamiPF01426. BAH. 2 hits.
PF00439. Bromodomain. 6 hits.
PF00505. HMG_box. 1 hit.
[Graphical view]
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00439. BAH. 2 hits.
SM00297. BROMO. 6 hits.
SM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
SSF47370. SSF47370. 6 hits.
PROSITEiPS51038. BAH. 2 hits.
PS00633. BROMODOMAIN_1. 5 hits.
PS50014. BROMODOMAIN_2. 6 hits.
PS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8BSQ9-1) [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

MGSKRRRATS PSSSVSGDFD DGHHSVPTPG PSRKRRRLSN LPTVDPIAVC     50
HELYNTIRDY KDEQGRLLCE LFIRAPKRRN QPDYYEVVSQ PIDLMKIQQK 100
LKMEEYDDVN LLTADFQLLF NNAKAYYKPD SPEYKAACKL WDLYLRTRNE 150
FVQKGEADDE DDDEDGQDNQ GTLADGSSPG YLKEILEQLL EAIVVATNPS 200
GRLISELFQK LPSKVQYPDY YAIIKEPIDL KTIAQRIQNG SYKSIHAMAK 250
DIDLLAKNAK TYNEPGSQVF KDANSIKKIF YMKKAEIEHH EMTKSSLRIR 300
TASNLAAARL TGPSHNKSSL GEERNPTSKY YRNKRAVQGG RLSAITMALQ 350
YGSESEEDAA LAAARYEEGE SEAESITSFM DVSNPFHQLY DTVRSCRNHQ 400
GQLIAEPFFH LPSKKKYPDY YQQIKMPISL QQIRTKLKNQ EYETLDHLEC 450
DLNLMFENAK RYNVPNSAIY KRVLKLQQVM QAKKKELARR DDIEDGDSMI 500
SSATSDTGSA KRKSKKNIRK QRMKILFNVV LEAREPGSGR RLCDLFMVKP 550
SKKDYPDYYK IILEPMDLKI IEHNIRNDKY AGEEGMMEDM KLMFRNARHY 600
NEEGSQVYND AHILEKLLKD KRKELGPLPD DDDMASPKLK LSRKSGVSPK 650
KSKYMTPMQQ KLNEVYEAVK NYTDKRGRRL SAIFLRLPSR SELPDYYLTI 700
KKPMDMEKIR SHMMANKYQD IDSMVEDFVM MFNNACTYNE PESLIYKDAL 750
VLHKVLLETR RDLEGDEDSH VPNVTLLIQE LIHNLFVSVM SHQDDEGRCY 800
SDSLAEIPAV DPNSPNKPPL TFDIIRKNVE SNRYRRLDLF QEHMFEVLER 850
ARRMNRTDSE IYEDAVELQQ FFIRIRDELC KNGEILLSPA LSYTTKHLHN 900
DVEKEKKEKL PKEIEEDKLK REEEKREAEK SEDSSGTTGL SGLHRTYSQD 950
CSFKNSMYHV GDYVYVEPAE ANLQPHIVCI ERLWEDSAGE KWLYGCWFYR 1000
PNETFHLATR KFLEKEVFKS DYYNKVPVSK ILGKCVVMFV KEYFKLCPEN 1050
FRDEDVFVCE SRYSAKTKSF KKIKLWTMPI SSVRFVPRDV PLPVVRVASV 1100
FANADKGDDE KNTDNSDDNR AEDNFNLEKE KEDVPVEMSN GEPGCHYFEQ 1150
LRYNDMWLKV GDCVFIKSHG LVRPRVGRIE KVWVRDGAAY FYGPIFIHPE 1200
ETEHEPTKMF YKKEVFLSNL EETCPMSCIL GKCAVLSFKD FLSCRPTEIP 1250
ENDILLCESR YNESDKQMKK FKGLKRFSLS AKVVDDEIYY FRKPIIPQKE 1300
PSPLLEKKIQ LLEAKFAELE GGDDDIEEMG EEDSEVIEAP SLPQLQTPLA 1350
NELDLMPYTP PQSTPKSAKG SAKKESSKRK INMSGYILFS SEMRAVIKAQ 1400
HPDYSFGELS RLVGTEWRNL ETAKKAEYEG MMGGYPPGLP PLQGPVDGLV 1450
SMGSMQPLHP GGPPPHHLPP GVPGLPGIPP PGVMNQGVAP MVGTPAPGGS 1500
PYGQQVGVLG PPGQQAPPPY PGPHPAGPPV IQQPTTPMFV APPPKTQRLL 1550
HSEAYLKYIE GLSAESNSIS KWDQTLAARR RDVHLSKEQE SRLPSHWLKS 1600
KGAHTTMADA LWRLRDLMLR DTLNIRQAYN LENV 1634
Length:1,634
Mass (Da):187,188
Last modified:July 27, 2011 - v4
Checksum:iA905963F22ECD75E
GO
Isoform 2 (identifier: Q8BSQ9-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     300-332: RTASNLAAARLTGPSHNKSSLGEERNPTSKYYR → S

Show »
Length:1,602
Mass (Da):183,659
Checksum:i29EEFCA9EF8A94C9
GO

Sequence cautioni

The sequence AAH29037.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAH55456.1 differs from that shown. Reason: Contaminating sequence.
The sequence AAH55708.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei300 – 33233RTASN…SKYYR → S in isoform 2.
VSP_035471Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti417 – 4171Y → K in AAH23452. 1 Publication
Sequence conflicti695 – 6951D → E in BAC27136. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC154446 Genomic DNA. No translation available.
AC154727 Genomic DNA. No translation available.
BC023452 mRNA. Translation: AAH23452.1.
BC029037 mRNA. Translation: AAH29037.1. Different termination.
BC055456 mRNA. Translation: AAH55456.1. Different termination.
BC055708 mRNA. Translation: AAH55708.1. Different initiation.
BF451491 mRNA. No translation available.
CN530699 mRNA. No translation available.
AK009582 mRNA. Translation: BAB26374.2.
AK030781 mRNA. Translation: BAC27136.2.
AK030252 mRNA. No translation available.
AK166588 mRNA. No translation available.
UniGeneiMm.27913.

Genome annotation databases

EnsembliENSMUST00000112094; ENSMUSP00000107723; ENSMUSG00000042323. [Q8BSQ9-2]
ENSMUST00000112095; ENSMUSP00000107724; ENSMUSG00000042323. [Q8BSQ9-1]
UCSCiuc007swl.1. mouse. [Q8BSQ9-1]
uc007swm.1. mouse. [Q8BSQ9-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC154446 Genomic DNA. No translation available.
AC154727 Genomic DNA. No translation available.
BC023452 mRNA. Translation: AAH23452.1 .
BC029037 mRNA. Translation: AAH29037.1 . Different termination.
BC055456 mRNA. Translation: AAH55456.1 . Different termination.
BC055708 mRNA. Translation: AAH55708.1 . Different initiation.
BF451491 mRNA. No translation available.
CN530699 mRNA. No translation available.
AK009582 mRNA. Translation: BAB26374.2 .
AK030781 mRNA. Translation: BAC27136.2 .
AK030252 mRNA. No translation available.
AK166588 mRNA. No translation available.
UniGenei Mm.27913.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YQD NMR - A 650-762 [» ]
ProteinModelPortali Q8BSQ9.
SMRi Q8BSQ9. Positions 43-154, 176-292, 388-494, 510-628, 651-766, 773-914, 957-1102.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-48885N.
IntActi Q8BSQ9. 2 interactions.
MINTi MINT-4112204.

PTM databases

PhosphoSitei Q8BSQ9.

Proteomic databases

MaxQBi Q8BSQ9.
PaxDbi Q8BSQ9.
PRIDEi Q8BSQ9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000112094 ; ENSMUSP00000107723 ; ENSMUSG00000042323 . [Q8BSQ9-2 ]
ENSMUST00000112095 ; ENSMUSP00000107724 ; ENSMUSG00000042323 . [Q8BSQ9-1 ]
UCSCi uc007swl.1. mouse. [Q8BSQ9-1 ]
uc007swm.1. mouse. [Q8BSQ9-2 ]

Organism-specific databases

MGIi MGI:1923998. Pbrm1.

Phylogenomic databases

eggNOGi COG5076.
GeneTreei ENSGT00390000003017.
HOVERGENi HBG079860.
OrthoDBi EOG78H3S6.

Miscellaneous databases

ChiTaRSi PBRM1. mouse.
EvolutionaryTracei Q8BSQ9.
PROi Q8BSQ9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BSQ9.
Bgeei Q8BSQ9.
Genevestigatori Q8BSQ9.

Family and domain databases

Gene3Di 1.10.30.10. 1 hit.
1.20.920.10. 6 hits.
InterProi IPR001025. BAH_dom.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR009071. HMG_box_dom.
[Graphical view ]
Pfami PF01426. BAH. 2 hits.
PF00439. Bromodomain. 6 hits.
PF00505. HMG_box. 1 hit.
[Graphical view ]
PRINTSi PR00503. BROMODOMAIN.
SMARTi SM00439. BAH. 2 hits.
SM00297. BROMO. 6 hits.
SM00398. HMG. 1 hit.
[Graphical view ]
SUPFAMi SSF47095. SSF47095. 1 hit.
SSF47370. SSF47370. 6 hits.
PROSITEi PS51038. BAH. 2 hits.
PS00633. BROMODOMAIN_1. 5 hits.
PS50014. BROMODOMAIN_2. 6 hits.
PS50118. HMG_BOX_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6, Czech II and FVB/N.
    Tissue: Brain and 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 1-919 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-512 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Embryo and Tongue.
  4. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  5. "An essential switch in subunit composition of a chromatin remodeling complex during neural development."
    Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H., Aebersold R., Graef I.A., Crabtree G.R.
    Neuron 55:201-215(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PHF10, DEVELOPMENTAL STAGE.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353 AND SER-355, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-414, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. "Solution structure of the fifth bromodomain from mouse polybromo-1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 646-762.

Entry informationi

Entry nameiPB1_MOUSE
AccessioniPrimary (citable) accession number: Q8BSQ9
Secondary accession number(s): E9QPW1
, Q05C64, Q05CL6, Q7TMP1, Q7TNU2, Q9CV51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 23, 2008
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 95 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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