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Q86U86

- PB1_HUMAN

UniProt

Q86U86 - PB1_HUMAN

Protein

Protein polybromo-1

Gene

PBRM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Acts as a negative regulator of cell proliferation.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi1379 – 144769HMG boxPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. DNA binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. chromatin remodeling Source: UniProtKB
    2. heart development Source: Ensembl
    3. mitotic nuclear division Source: UniProtKB
    4. negative regulation of cell proliferation Source: UniProtKB
    5. placenta development Source: Ensembl
    6. regulation of transcription, DNA-templated Source: UniProtKB-KW
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein polybromo-1
    Short name:
    hPB1
    Alternative name(s):
    BRG1-associated factor 180
    Short name:
    BAF180
    Polybromo-1D
    Gene namesi
    Name:PBRM1
    Synonyms:BAF180, PB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:30064. PBRM1.

    Subcellular locationi

    GO - Cellular componenti

    1. kinetochore Source: Ensembl
    2. nuclear chromosome Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Renal cell carcinoma (RCC) [MIM:144700]: Renal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    MIMi144700. phenotype.
    PharmGKBiPA162398846.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16891689Protein polybromo-1PRO_0000211207Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei10 – 101Phosphoserine2 Publications
    Modified residuei39 – 391Phosphoserine4 Publications
    Modified residuei131 – 1311Phosphoserine1 Publication
    Modified residuei316 – 3161Phosphoserine1 Publication
    Modified residuei319 – 3191Phosphoserine1 Publication
    Modified residuei353 – 3531Phosphoserine4 Publications
    Modified residuei355 – 3551Phosphoserine4 Publications
    Modified residuei371 – 3711Phosphoserine1 Publication
    Modified residuei375 – 3751Phosphoserine1 Publication
    Modified residuei414 – 4141N6-acetyllysineBy similarity
    Modified residuei498 – 4981Phosphoserine1 Publication
    Modified residuei636 – 6361Phosphoserine3 Publications
    Modified residuei648 – 6481Phosphoserine1 Publication
    Modified residuei1289 – 12891PhosphotyrosineBy similarity
    Modified residuei1405 – 14051Phosphoserine2 Publications
    Modified residuei1453 – 14531Phosphoserine3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ86U86.
    PaxDbiQ86U86.
    PRIDEiQ86U86.

    PTM databases

    PhosphoSiteiQ86U86.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ86U86.
    BgeeiQ86U86.
    GenevestigatoriQ86U86.

    Organism-specific databases

    HPAiHPA015629.

    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 PHF10/BAF45A By similarity. Interacts with acetylated 'Lys-14' of histone H3 (H3K14ac), and may also interact with other acetylated or methylated Lys residues on histone H3.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ARID2Q68CP95EBI-637807,EBI-637818
    SMARCA4P515324EBI-637807,EBI-302489

    Protein-protein interaction databases

    BioGridi120490. 32 interactions.
    DIPiDIP-33045N.
    IntActiQ86U86. 14 interactions.
    MINTiMINT-1195749.

    Structurei

    Secondary structure

    1
    1689
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi46 – 5914
    Helixi68 – 725
    Helixi78 – 803
    Helixi82 – 876
    Helixi94 – 1029
    Helixi109 – 12618
    Helixi132 – 15221
    Beta strandi176 – 1783
    Helixi179 – 19517
    Helixi206 – 2083
    Turni214 – 2163
    Helixi218 – 2236
    Helixi230 – 23910
    Helixi245 – 26218
    Helixi268 – 29124
    Helixi388 – 3947
    Beta strandi399 – 4013
    Helixi406 – 4083
    Turni414 – 4163
    Helixi418 – 4236
    Helixi430 – 4389
    Helixi445 – 46218
    Helixi468 – 49023
    Helixi511 – 53222
    Turni536 – 5383
    Helixi542 – 5465
    Turni552 – 5543
    Helixi556 – 5616
    Helixi568 – 5769
    Helixi583 – 60018
    Helixi606 – 62520
    Helixi657 – 67115
    Helixi680 – 6845
    Turni690 – 6923
    Helixi694 – 6996
    Beta strandi700 – 7023
    Helixi706 – 7149
    Helixi721 – 73818
    Helixi744 – 76219
    Turni763 – 7653
    Helixi777 – 79014
    Helixi800 – 8045
    Helixi822 – 8309
    Helixi837 – 85418
    Helixi860 – 88223
    Helixi889 – 8924
    Helixi895 – 90915
    Helixi910 – 9134

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2KTBNMR-B174-293[»]
    3G0JX-ray1.78A/B645-766[»]
    3HMFX-ray1.63A178-291[»]
    3IU5X-ray1.63A43-154[»]
    3IU6X-ray1.79A773-914[»]
    3K2JX-ray2.20A/B388-494[»]
    3LJWX-ray1.50A/B174-293[»]
    3MB4X-ray1.66A/B645-766[»]
    3TLPX-ray2.13A/B496-637[»]
    4Q0NX-ray1.78A/B/C/D/E/F/G/H645-766[»]
    4Q0OX-ray1.83A645-766[»]
    ProteinModelPortaliQ86U86.
    SMRiQ86U86. Positions 26-293, 383-766, 773-914, 957-1102, 1160-1272, 1370-1444.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86U86.

    Family & Domainsi

    Domains and Repeats

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

    Compositional bias

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

    Sequence similaritiesi

    Contains 2 BAH domains.PROSITE-ProRule annotation
    Contains 6 bromo domains.PROSITE-ProRule annotation
    Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Bromodomain, Repeat

    Phylogenomic databases

    eggNOGiCOG5076.
    HOVERGENiHBG079860.
    InParanoidiQ86U86.
    KOiK11757.
    OMAiILGKCVV.
    OrthoDBiEOG78H3S6.
    PhylomeDBiQ86U86.
    TreeFamiTF106120.

    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 (9)i

    Sequence statusi: Complete.

    This entry describes 9 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86U86-1) [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 DGHHSVSTPG PSRKRRRLSN LPTVDPIAVC     50
    HELYNTIRDY KDEQGRLLCE LFIRAPKRRN QPDYYEVVSQ PIDLMKIQQK 100
    LKMEEYDDVN LLTADFQLLF NNAKSYYKPD SPEYKAACKL WDLYLRTRNE 150
    FVQKGEADDE DDDEDGQDNQ GTVTEGSSPA YLKEILEQLL EAIVVATNPS 200
    GRLISELFQK LPSKVQYPDY YAIIKEPIDL KTIAQRIQNG SYKSIHAMAK 250
    DIDLLAKNAK TYNEPGSQVF KDANSIKKIF YMKKAEIEHH EMAKSSLRMR 300
    TPSNLAAARL TGPSHSKGSL GEERNPTSKY YRNKRAVQGG RLSAITMALQ 350
    YGSESEEDAA LAAARYEEGE SEAESITSFM DVSNPFYQLY DTVRSCRNNQ 400
    GQLIAEPFYH LPSKKKYPDY YQQIKMPISL QQIRTKLKNQ EYETLDHLEC 450
    DLNLMFENAK RYNVPNSAIY KRVLKLQQVM QAKKKELARR DDIEDGDSMI 500
    SSATSDTGSA KRKSKKNIRK QRMKILFNVV LEAREPGSGR RLCDLFMVKP 550
    SKKDYPDYYK IILEPMDLKI IEHNIRNDKY AGEEGMIEDM KLMFRNARHY 600
    NEEGSQVYND AHILEKLLKE KRKELGPLPD DDDMASPKLK LSRKSGISPK 650
    KSKYMTPMQQ KLNEVYEAVK NYTDKRGRRL SAIFLRLPSR SELPDYYLTI 700
    KKPMDMEKIR SHMMANKYQD IDSMVEDFVM MFNNACTYNE PESLIYKDAL 750
    VLHKVLLETR RDLEGDEDSH VPNVTLLIQE LIHNLFVSVM SHQDDEGRCY 800
    SDSLAEIPAV DPNFPNKPPL TFDIIRKNVE NNRYRRLDLF QEHMFEVLER 850
    ARRMNRTDSE IYEDAVELQQ FFIKIRDELC KNGEILLSPA LSYTTKHLHN 900
    DVEKERKEKL PKEIEEDKLK REEEKREAEK SEDSSGAAGL SGLHRTYSQD 950
    CSFKNSMYHV GDYVYVEPAE ANLQPHIVCI ERLWEDSAGE KWLYGCWFYR 1000
    PNETFHLATR KFLEKEVFKS DYYNKVPVSK ILGKCVVMFV KEYFKLCPEN 1050
    FRDEDVFVCE SRYSAKTKSF KKIKLWTMPI SSVRFVPRDV PLPVVRVASV 1100
    FANADKGDDE KNTDNSEDSR AEDNFNLEKE KEDVPVEMSN GEPGCHYFEQ 1150
    LHYNDMWLKV GDCVFIKSHG LVRPRVGRIE KVWVRDGAAY FYGPIFIHPE 1200
    ETEHEPTKMF YKKEVFLSNL EETCPMTCIL GKCAVLSFKD FLSCRPTEIP 1250
    ENDILLCESR YNESDKQMKK FKGLKRFSLS AKVVDDEIYY FRKPIVPQKE 1300
    PSPLLEKKIQ LLEAKFAELE GGDDDIEEMG EEDSEVIEPP SLPQLQTPLA 1350
    SELDLMPYTP PQSTPKSAKG SAKKEGSKRK INMSGYILFS SEMRAVIKAQ 1400
    HPDYSFGELS RLVGTEWRNL ETAKKAEYEE RAAKVAEQQE RERAAQQQQP 1450
    SASPRAGTPV GALMGVVPPP TPMGMLNQQL TPVAGMMGGY PPGLPPLQGP 1500
    VDGLVSMGSM QPLHPGGPPP HHLPPGVPGL PGIPPPGVMN QGVAPMVGTP 1550
    APGGSPYGQQ VGVLGPPGQQ APPPYPGPHP AGPPVIQQPT TPMFVAPPPK 1600
    TQRLLHSEAY LKYIEGLSAE SNSISKWDQT LAARRRDVHL SKEQESRLPS 1650
    HWLKSKGAHT TMADALWRLR DLMLRDTLNI RQAYNLENV 1689
    Length:1,689
    Mass (Da):192,948
    Last modified:June 1, 2003 - v1
    Checksum:i0A656E319C4FC748
    GO
    Isoform 2 (identifier: Q86U86-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1430-1484: Missing.

    Show »
    Length:1,634
    Mass (Da):187,188
    Checksum:iFAB1C935A9B8B4DD
    GO
    Isoform 3 (identifier: Q86U86-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         300-332: RTPSNLAAARLTGPSHSKGSLGEERNPTSKYYR → S
         1430-1484: Missing.

    Show »
    Length:1,602
    Mass (Da):183,690
    Checksum:iB8BA103E359A48DA
    GO
    Isoform 4 (identifier: Q86U86-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         989-1013: Missing.
         1336-1362: Missing.
         1430-1484: Missing.

    Show »
    Length:1,582
    Mass (Da):181,085
    Checksum:iA2B8A14FAB928A3C
    GO
    Isoform 5 (identifier: Q86U86-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1430-1484: Missing.
         1485-1536: Missing.

    Show »
    Length:1,582
    Mass (Da):182,118
    Checksum:iBCBD5D8E42BAB076
    GO
    Isoform 6 (identifier: Q86U86-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         857-1689: Missing.

    Show »
    Length:856
    Mass (Da):99,142
    Checksum:iAE378B417E0493B3
    GO
    Isoform 7 (identifier: Q86U86-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         513-513: K → KRNTHDSEMLGLRRLS
         1430-1484: Missing.
         1485-1536: Missing.

    Show »
    Length:1,597
    Mass (Da):183,885
    Checksum:i710520F65FF9E981
    GO
    Isoform 8 (identifier: Q86U86-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         513-513: K → KRNTHDSEMLGLRRLS
         1485-1536: Missing.

    Show »
    Length:1,652
    Mass (Da):189,645
    Checksum:iE5BA80E11EE7E6C0
    GO
    Isoform 9 (identifier: Q86U86-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         989-1013: Missing.
         1430-1484: Missing.

    Show »
    Length:1,609
    Mass (Da):184,043
    Checksum:i38BB16B06929BFFC
    GO

    Sequence cautioni

    The sequence AAI15010.1 differs from that shown. Reason: Contaminating sequence.
    The sequence AAI15011.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB71210.1 differs from that shown. Reason: Erroneous initiation.
    The sequence AAI15012.1 differs from that shown. Reason: Erroneous termination at position 78. Translated as Arg.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → T in AAI15011. (PubMed:15489334)Curated
    Sequence conflicti65 – 651G → S in AAI15011. (PubMed:15489334)Curated
    Sequence conflicti242 – 2421Y → C in AAI15012. (PubMed:15489334)Curated
    Sequence conflicti251 – 2511D → V in AAI15011. (PubMed:15489334)Curated
    Sequence conflicti430 – 4301L → P in AAI15012. (PubMed:15489334)Curated
    Sequence conflicti553 – 5531K → R in AAG34760. (PubMed:11078522)Curated
    Sequence conflicti567 – 5671D → Y in AAI15012. (PubMed:15489334)Curated
    Sequence conflicti750 – 7501L → P in AAI15012. (PubMed:15489334)Curated
    Sequence conflicti792 – 7921H → R in AAI15012. (PubMed:15489334)Curated
    Sequence conflicti927 – 9271Missing in AAI15010. (PubMed:15489334)Curated
    Sequence conflicti927 – 9271Missing in BAB71210. (PubMed:14702039)Curated
    Sequence conflicti963 – 9631Y → H in BAB71210. (PubMed:14702039)Curated
    Sequence conflicti1144 – 11441G → V in AAG34760. (PubMed:11078522)Curated
    Sequence conflicti1245 – 12451R → K in AAG34760. (PubMed:11078522)Curated
    Sequence conflicti1306 – 13061E → G in AAG34760. (PubMed:11078522)Curated
    Sequence conflicti1349 – 13491L → P in AAI15010. (PubMed:15489334)Curated
    Sequence conflicti1488 – 14881G → D in AAI15012. (PubMed:15489334)Curated
    Sequence conflicti1568 – 15681G → R in AAG34760. (PubMed:11078522)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491V → L Found in a lung cancer cell line. 1 Publication
    VAR_064653
    Natural varianti56 – 561T → A Found in a brain cancer cell line. 1 Publication
    VAR_064654
    Natural varianti57 – 571Missing Found in a case of clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064655
    Natural varianti66 – 661R → G Found in a colon cancer cell line. 1 Publication
    VAR_064656
    Natural varianti90 – 901Q → E Found in a bladder cancer cell line. 1 Publication
    VAR_064657
    Natural varianti144 – 1441Y → F Found in a malignant melanoma cell line. 1 Publication
    VAR_064658
    Natural varianti160 – 1601E → A Found in a malignant melanoma cell line. 1 Publication
    VAR_064659
    Natural varianti202 – 2021R → C Found in a endometrial cancer cell line. 1 Publication
    VAR_064660
    Natural varianti206 – 2061E → K Found in hematopoietic and lymphoid cancer cell lines. 1 Publication
    VAR_064661
    Natural varianti226 – 2261E → G Found in hematopoietic and lymphoid cancer cell lines. 1 Publication
    VAR_064662
    Natural varianti228 – 2281I → V Found in a breast cancer cell line. 1 Publication
    Corresponds to variant rs201022657 [ dbSNP | Ensembl ].
    VAR_064663
    Natural varianti232 – 2321T → P Found in a case of clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064664
    Natural varianti233 – 2331I → T Found in a renal carcinoma cell line. 1 Publication
    VAR_064665
    Natural varianti256 – 2561A → T Found in an ovary carcinoma cell line. 1 Publication
    VAR_064666
    Natural varianti340 – 3401G → A Found in a malignant melanoma cell line. 1 Publication
    VAR_064667
    Natural varianti523 – 5231M → I Found in a case of clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064668
    Natural varianti540 – 5401R → S Found in a case of clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064669
    Natural varianti597 – 5971A → D Found in a case of clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064670
    Natural varianti621 – 6211K → E Found in a case of clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064671
    Natural varianti661 – 6611K → N Found in a case of clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064672
    Natural varianti674 – 6741D → E Found in a case of clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064673
    Natural varianti678 – 6781R → C.1 Publication
    VAR_064674
    Natural varianti893 – 8931Y → C Found in hematopoietic, lymphoid, lung and liver cancer cell lines. 1 Publication
    VAR_064675
    Natural varianti895 – 8951T → S Found in a lung cancer cell line. 1 Publication
    VAR_064676
    Natural varianti922 – 9221E → Q Found in a breast cancer cell line. 1 Publication
    VAR_064677
    Natural varianti925 – 9251K → Q Found in a colon cancer cell line. 1 Publication
    VAR_064678
    Natural varianti1079 – 10791P → Y Requires 2 nucleotide substitutions; found in a colon cancer cell line. 1 Publication
    VAR_064679
    Natural varianti1098 – 10981A → S Found in hematopoietic and lymphoid cancer cell lines. 1 Publication
    VAR_064680
    Natural varianti1120 – 11201R → Q Found in hematopoietic and lymphoid cancer cell lines. 1 Publication
    VAR_064681
    Natural varianti1177 – 11771G → S Found in a kidney cancer cell line. 1 Publication
    VAR_064682
    Natural varianti1204 – 12041H → P Found in a case of clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064683
    Natural varianti1209 – 12146Missing Found in a case of clear cell renal carcinoma; somatic mutation.
    VAR_064684
    Natural varianti1287 – 12871E → Q Found in a breast cancer cell line. 1 Publication
    VAR_064685
    Natural varianti1414 – 14141G → E Found in a lung cancer cell line. 1 Publication
    VAR_064686
    Natural varianti1503 – 15031G → C Found in a stomach cancer cell line. 1 Publication
    VAR_064687
    Natural varianti1560 – 15601Q → H Found in an endometrial cancer cell line. 1 Publication
    VAR_064688
    Natural varianti1614 – 16141I → N Found in a case of clear cell renal carcinoma; somatic mutation. 1 Publication
    VAR_064689
    Natural varianti1647 – 16471R → C Found in a breast cancer cell line. 1 Publication
    VAR_064690

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei300 – 33233RTPSN…SKYYR → S in isoform 3. 1 PublicationVSP_015231Add
    BLAST
    Alternative sequencei513 – 5131K → KRNTHDSEMLGLRRLS in isoform 7 and isoform 8. 2 PublicationsVSP_035499
    Alternative sequencei857 – 1689833Missing in isoform 6. 1 PublicationVSP_015232Add
    BLAST
    Alternative sequencei989 – 101325Missing in isoform 4 and isoform 9. 2 PublicationsVSP_015233Add
    BLAST
    Alternative sequencei1336 – 136227Missing in isoform 4. 2 PublicationsVSP_015234Add
    BLAST
    Alternative sequencei1430 – 148455Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 7 and isoform 9. 4 PublicationsVSP_015235Add
    BLAST
    Alternative sequencei1485 – 153652Missing in isoform 5, isoform 7 and isoform 8. 3 PublicationsVSP_015236Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197569 mRNA. Translation: AAG34760.1.
    AF225870 mRNA. Translation: AAG48939.1.
    AF225871 mRNA. Translation: AAG48940.1.
    AF225872 mRNA. Translation: AAG48941.1.
    AF177387 mRNA. Translation: AAG48933.1.
    AY281068 mRNA. Translation: AAP34197.1.
    BC115009 mRNA. Translation: AAI15010.1. Different termination.
    BC115010 mRNA. Translation: AAI15011.1. Different initiation.
    BC115011 mRNA. Translation: AAI15012.1. Sequence problems.
    BC129934 mRNA. Translation: AAI29935.1.
    BC129935 mRNA. Translation: AAI29936.1.
    AK056541 mRNA. Translation: BAB71210.1. Different initiation.
    CCDSiCCDS43099.1. [Q86U86-4]
    RefSeqiNP_060783.3. NM_018313.4. [Q86U86-4]
    UniGeneiHs.189920.

    Genome annotation databases

    EnsembliENST00000296302; ENSP00000296302; ENSG00000163939. [Q86U86-1]
    ENST00000337303; ENSP00000338302; ENSG00000163939. [Q86U86-5]
    ENST00000356770; ENSP00000349213; ENSG00000163939. [Q86U86-3]
    ENST00000394830; ENSP00000378307; ENSG00000163939. [Q86U86-4]
    ENST00000409057; ENSP00000386593; ENSG00000163939. [Q86U86-2]
    ENST00000409114; ENSP00000386643; ENSG00000163939. [Q86U86-8]
    ENST00000409767; ENSP00000386601; ENSG00000163939. [Q86U86-7]
    ENST00000410007; ENSP00000386529; ENSG00000163939. [Q86U86-9]
    ENST00000412587; ENSP00000404579; ENSG00000163939. [Q86U86-6]
    GeneIDi55193.
    KEGGihsa:55193.
    UCSCiuc003deq.2. human. [Q86U86-5]
    uc003der.2. human. [Q86U86-3]
    uc003des.2. human. [Q86U86-1]
    uc003det.2. human. [Q86U86-7]
    uc003deu.2. human. [Q86U86-8]
    uc003dew.2. human. [Q86U86-2]
    uc003dey.2. human. [Q86U86-4]
    uc010hmk.1. human. [Q86U86-9]

    Polymorphism databases

    DMDMi73921624.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197569 mRNA. Translation: AAG34760.1 .
    AF225870 mRNA. Translation: AAG48939.1 .
    AF225871 mRNA. Translation: AAG48940.1 .
    AF225872 mRNA. Translation: AAG48941.1 .
    AF177387 mRNA. Translation: AAG48933.1 .
    AY281068 mRNA. Translation: AAP34197.1 .
    BC115009 mRNA. Translation: AAI15010.1 . Different termination.
    BC115010 mRNA. Translation: AAI15011.1 . Different initiation.
    BC115011 mRNA. Translation: AAI15012.1 . Sequence problems.
    BC129934 mRNA. Translation: AAI29935.1 .
    BC129935 mRNA. Translation: AAI29936.1 .
    AK056541 mRNA. Translation: BAB71210.1 . Different initiation.
    CCDSi CCDS43099.1. [Q86U86-4 ]
    RefSeqi NP_060783.3. NM_018313.4. [Q86U86-4 ]
    UniGenei Hs.189920.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KTB NMR - B 174-293 [» ]
    3G0J X-ray 1.78 A/B 645-766 [» ]
    3HMF X-ray 1.63 A 178-291 [» ]
    3IU5 X-ray 1.63 A 43-154 [» ]
    3IU6 X-ray 1.79 A 773-914 [» ]
    3K2J X-ray 2.20 A/B 388-494 [» ]
    3LJW X-ray 1.50 A/B 174-293 [» ]
    3MB4 X-ray 1.66 A/B 645-766 [» ]
    3TLP X-ray 2.13 A/B 496-637 [» ]
    4Q0N X-ray 1.78 A/B/C/D/E/F/G/H 645-766 [» ]
    4Q0O X-ray 1.83 A 645-766 [» ]
    ProteinModelPortali Q86U86.
    SMRi Q86U86. Positions 26-293, 383-766, 773-914, 957-1102, 1160-1272, 1370-1444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120490. 32 interactions.
    DIPi DIP-33045N.
    IntActi Q86U86. 14 interactions.
    MINTi MINT-1195749.

    Chemistry

    ChEMBLi CHEMBL1795184.

    PTM databases

    PhosphoSitei Q86U86.

    Polymorphism databases

    DMDMi 73921624.

    Proteomic databases

    MaxQBi Q86U86.
    PaxDbi Q86U86.
    PRIDEi Q86U86.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296302 ; ENSP00000296302 ; ENSG00000163939 . [Q86U86-1 ]
    ENST00000337303 ; ENSP00000338302 ; ENSG00000163939 . [Q86U86-5 ]
    ENST00000356770 ; ENSP00000349213 ; ENSG00000163939 . [Q86U86-3 ]
    ENST00000394830 ; ENSP00000378307 ; ENSG00000163939 . [Q86U86-4 ]
    ENST00000409057 ; ENSP00000386593 ; ENSG00000163939 . [Q86U86-2 ]
    ENST00000409114 ; ENSP00000386643 ; ENSG00000163939 . [Q86U86-8 ]
    ENST00000409767 ; ENSP00000386601 ; ENSG00000163939 . [Q86U86-7 ]
    ENST00000410007 ; ENSP00000386529 ; ENSG00000163939 . [Q86U86-9 ]
    ENST00000412587 ; ENSP00000404579 ; ENSG00000163939 . [Q86U86-6 ]
    GeneIDi 55193.
    KEGGi hsa:55193.
    UCSCi uc003deq.2. human. [Q86U86-5 ]
    uc003der.2. human. [Q86U86-3 ]
    uc003des.2. human. [Q86U86-1 ]
    uc003det.2. human. [Q86U86-7 ]
    uc003deu.2. human. [Q86U86-8 ]
    uc003dew.2. human. [Q86U86-2 ]
    uc003dey.2. human. [Q86U86-4 ]
    uc010hmk.1. human. [Q86U86-9 ]

    Organism-specific databases

    CTDi 55193.
    GeneCardsi GC03M052579.
    H-InvDB HIX0003364.
    HGNCi HGNC:30064. PBRM1.
    HPAi HPA015629.
    MIMi 144700. phenotype.
    606083. gene.
    neXtProti NX_Q86U86.
    PharmGKBi PA162398846.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5076.
    HOVERGENi HBG079860.
    InParanoidi Q86U86.
    KOi K11757.
    OMAi ILGKCVV.
    OrthoDBi EOG78H3S6.
    PhylomeDBi Q86U86.
    TreeFami TF106120.

    Miscellaneous databases

    ChiTaRSi PBRM1. human.
    EvolutionaryTracei Q86U86.
    GeneWikii PBRM1.
    GenomeRNAii 55193.
    NextBioi 59051.
    PROi Q86U86.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86U86.
    Bgeei Q86U86.
    Genevestigatori Q86U86.

    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

    1. "The human SWI/SNF-B chromatin-remodeling complex is related to yeast rsc and localizes at kinetochores of mitotic chromosomes."
      Xue Y., Canman J.C., Lee C.S., Nie Z., Yang D., Moreno G.T., Young M.K., Salmon E.D., Wang W.
      Proc. Natl. Acad. Sci. U.S.A. 97:13015-13020(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PBAF COMPLEX.
    2. "cDNA cloning of the human polybromo-1 gene on chromosome 3p21."
      Horikawa I., Barrett J.C.
      DNA Seq. 13:211-215(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 5 AND 6), TISSUE SPECIFICITY.
    3. "The 3p21 candidate tumor suppressor gene BAF180 is normally expressed in human lung cancer."
      Sekine I., Sato M., Sunaga N., Toyooka S., Peyton M., Parsons R., Wang W., Gazdar A.F., Minna J.D.
      Oncogene 24:2735-2738(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORMS 2; 4; 7; 8 AND 9).
    5. "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] OF 57-1127 (ISOFORM 7).
      Tissue: Teratocarcinoma.
    6. "Selectivity of chromatin-remodelling cofactors for ligand-activated transcription."
      Lemon B., Inouye C., King D.S., Tjian R.
      Nature 414:924-928(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PBAF COMPLEX, IDENTIFICATION IN A SWI/SNF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-39; SER-131; SER-316; SER-319; SER-353; SER-355 AND SER-1405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-39; SER-353; SER-355; SER-371; SER-375; SER-498 AND SER-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-353; SER-355; SER-636; SER-1405 AND SER-1453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: FUNCTION AS NEGATIVE REGULATOR OF CELL PROLIFERATION, INVOLVEMENT IN RCC, VARIANTS LEU-49; ALA-56; ILE-57 DEL; GLY-66; GLU-90; PHE-144; ALA-160; CYS-202; LYS-206; GLY-226; VAL-228; PRO-232; THR-233; THR-256; ALA-340; ILE-523; SER-540; ASP-597; GLU-621; ASN-661; GLU-674; CYS-678; CYS-893; SER-895; GLN-922; GLN-925; TYR-1079; SER-1098; GLN-1120; SER-1177; PRO-1204; 1209-MET--GLU-1214 DEL; GLN-1287; GLU-1414; CYS-1503; HIS-1560; ASN-1614 AND CYS-1647.
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-353; SER-355; SER-636; SER-648 AND SER-1453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Recent advances in understanding chromatin remodeling by SWI/SNF complexes."
      Martens J.A., Winston F.
      Curr. Opin. Genet. Dev. 13:136-142(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON SWI/SNF CHROMATIN-REMODELING COMPLEXES.
    17. "PBAF chromatin-remodeling complex requires a novel specificity subunit, BAF200, to regulate expression of selective interferon-responsive genes."
      Yan Z., Cui K., Murray D.M., Ling C., Xue Y., Gerstein A., Parsons R., Zhao K., Wang W.
      Genes Dev. 19:1662-1667(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PBAF COMPLEX.
    18. "Structural insights into selective histone H3 recognition by the human polybromo bromodomain 2."
      Charlop-Powers Z., Zeng L., Zhang Q., Zhou M.M.
      Cell Res. 20:529-538(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 174-293, INTERACTION WITH ACETYLATED HISTONE H3.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 43-917, INTERACTION WITH HISTONE H3.

    Entry informationi

    Entry nameiPB1_HUMAN
    AccessioniPrimary (citable) accession number: Q86U86
    Secondary accession number(s): A1L381
    , A1L382, A4FUJ7, Q1RMD1, Q1RMD2, Q96MS2, Q9H2T3, Q9H2T4, Q9H2T5, Q9H301, Q9H314
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 113 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, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3