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Q86U86 (PB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein polybromo-1

Short name=hPB1
Alternative name(s):
BRG1-associated factor 180
Short name=BAF180
Polybromo-1D
Gene names
Name:PBRM1
Synonyms:BAF180, PB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1689 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.14

Subunit structure

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. Ref.1 Ref.6 Ref.17 Ref.18 Ref.19

Subcellular location

Nucleus.

Tissue specificity

Widely expressed. Ref.2

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Sequence similarities

Contains 2 BAH domains.

Contains 6 bromo domains.

Contains 1 HMG box DNA-binding domain.

Sequence caution

The sequence AAI15010.1 differs from that shown. Reason: Contaminating sequence.

The sequence AAI15011.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAI15012.1 differs from that shown. Reason: Erroneous termination at position 78. Translated as Arg.

The sequence BAB71210.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARID2Q68CP95EBI-637807,EBI-637818
SMARCA4P515324EBI-637807,EBI-302489

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86U86-1)

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.
Isoform 2 (identifier: Q86U86-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1430-1484: Missing.
Isoform 3 (identifier: Q86U86-3)

The sequence of this isoform differs from the canonical sequence as follows:
     300-332: RTPSNLAAARLTGPSHSKGSLGEERNPTSKYYR → S
     1430-1484: Missing.
Isoform 4 (identifier: Q86U86-4)

The sequence of this isoform differs from the canonical sequence as follows:
     989-1013: Missing.
     1336-1362: Missing.
     1430-1484: Missing.
Isoform 5 (identifier: Q86U86-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1430-1484: Missing.
     1485-1536: Missing.
Isoform 6 (identifier: Q86U86-6)

The sequence of this isoform differs from the canonical sequence as follows:
     857-1689: Missing.
Isoform 7 (identifier: Q86U86-7)

The sequence of this isoform differs from the canonical sequence as follows:
     513-513: K → KRNTHDSEMLGLRRLS
     1430-1484: Missing.
     1485-1536: Missing.
Isoform 8 (identifier: Q86U86-8)

The sequence of this isoform differs from the canonical sequence as follows:
     513-513: K → KRNTHDSEMLGLRRLS
     1485-1536: Missing.
Isoform 9 (identifier: Q86U86-9)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16891689Protein polybromo-1
PRO_0000211207

Regions

Domain64 – 13471Bromo 1
Domain200 – 27071Bromo 2
Domain400 – 47071Bromo 3
Domain538 – 60871Bromo 4
Domain676 – 74671Bromo 5
Domain792 – 86271Bromo 6
Domain956 – 1074119BAH 1
Domain1156 – 1272117BAH 2
DNA binding1379 – 144769HMG box
Compositional bias630 – 6334Poly-Asp
Compositional bias1468 – 1599132Pro-rich

Amino acid modifications

Modified residue101Phosphoserine Ref.9 Ref.11
Modified residue391Phosphoserine Ref.7 Ref.9 Ref.11 Ref.12
Modified residue1311Phosphoserine Ref.9
Modified residue3161Phosphoserine Ref.9
Modified residue3191Phosphoserine Ref.9
Modified residue3531Phosphoserine Ref.9 Ref.11 Ref.12 Ref.15
Modified residue3551Phosphoserine Ref.9 Ref.11 Ref.12 Ref.15
Modified residue3711Phosphoserine Ref.11
Modified residue3751Phosphoserine Ref.11
Modified residue4141N6-acetyllysine By similarity
Modified residue4981Phosphoserine Ref.11
Modified residue6361Phosphoserine Ref.11 Ref.12 Ref.15
Modified residue6481Phosphoserine Ref.15
Modified residue12891Phosphotyrosine By similarity
Modified residue14051Phosphoserine Ref.9 Ref.12
Modified residue14531Phosphoserine Ref.8 Ref.12 Ref.15

Natural variations

Alternative sequence300 – 33233RTPSN…SKYYR → S in isoform 3.
VSP_015231
Alternative sequence5131K → KRNTHDSEMLGLRRLS in isoform 7 and isoform 8.
VSP_035499
Alternative sequence857 – 1689833Missing in isoform 6.
VSP_015232
Alternative sequence989 – 101325Missing in isoform 4 and isoform 9.
VSP_015233
Alternative sequence1336 – 136227Missing in isoform 4.
VSP_015234
Alternative sequence1430 – 148455Missing in isoform 2, isoform 3, isoform 4, isoform 5, isoform 7 and isoform 9.
VSP_015235
Alternative sequence1485 – 153652Missing in isoform 5, isoform 7 and isoform 8.
VSP_015236
Natural variant491V → L Found in a lung cancer cell line. Ref.14
VAR_064653
Natural variant561T → A Found in a brain cancer cell line. Ref.14
VAR_064654
Natural variant571Missing Found in a case of clear cell renal carcinoma; somatic mutation. Ref.14
VAR_064655
Natural variant661R → G Found in a colon cancer cell line. Ref.14
VAR_064656
Natural variant901Q → E Found in a bladder cancer cell line. Ref.14
VAR_064657
Natural variant1441Y → F Found in a malignant melanoma cell line. Ref.14
VAR_064658
Natural variant1601E → A Found in a malignant melanoma cell line. Ref.14
VAR_064659
Natural variant2021R → C Found in a endometrial cancer cell line. Ref.14
VAR_064660
Natural variant2061E → K Found in hematopoietic and lymphoid cancer cell lines. Ref.14
VAR_064661
Natural variant2261E → G Found in hematopoietic and lymphoid cancer cell lines. Ref.14
VAR_064662
Natural variant2281I → V Found in a breast cancer cell line. Ref.14
Corresponds to variant rs201022657 [ dbSNP | Ensembl ].
VAR_064663
Natural variant2321T → P Found in a case of clear cell renal carcinoma; somatic mutation. Ref.14
VAR_064664
Natural variant2331I → T Found in a renal carcinoma cell line. Ref.14
VAR_064665
Natural variant2561A → T Found in an ovary carcinoma cell line. Ref.14
VAR_064666
Natural variant3401G → A Found in a malignant melanoma cell line. Ref.14
VAR_064667
Natural variant5231M → I Found in a case of clear cell renal carcinoma; somatic mutation. Ref.14
VAR_064668
Natural variant5401R → S Found in a case of clear cell renal carcinoma; somatic mutation. Ref.14
VAR_064669
Natural variant5971A → D Found in a case of clear cell renal carcinoma; somatic mutation. Ref.14
VAR_064670
Natural variant6211K → E Found in a case of clear cell renal carcinoma; somatic mutation. Ref.14
VAR_064671
Natural variant6611K → N Found in a case of clear cell renal carcinoma; somatic mutation. Ref.14
VAR_064672
Natural variant6741D → E Found in a case of clear cell renal carcinoma; somatic mutation. Ref.14
VAR_064673
Natural variant6781R → C. Ref.14
VAR_064674
Natural variant8931Y → C Found in hematopoietic, lymphoid, lung and liver cancer cell lines. Ref.14
VAR_064675
Natural variant8951T → S Found in a lung cancer cell line. Ref.14
VAR_064676
Natural variant9221E → Q Found in a breast cancer cell line. Ref.14
VAR_064677
Natural variant9251K → Q Found in a colon cancer cell line. Ref.14
VAR_064678
Natural variant10791P → Y Requires 2 nucleotide substitutions; found in a colon cancer cell line. Ref.14
VAR_064679
Natural variant10981A → S Found in hematopoietic and lymphoid cancer cell lines. Ref.14
VAR_064680
Natural variant11201R → Q Found in hematopoietic and lymphoid cancer cell lines. Ref.14
VAR_064681
Natural variant11771G → S Found in a kidney cancer cell line. Ref.14
VAR_064682
Natural variant12041H → P Found in a case of clear cell renal carcinoma; somatic mutation. Ref.14
VAR_064683
Natural variant1209 – 12146Missing Found in a case of clear cell renal carcinoma; somatic mutation.
VAR_064684
Natural variant12871E → Q Found in a breast cancer cell line. Ref.14
VAR_064685
Natural variant14141G → E Found in a lung cancer cell line. Ref.14
VAR_064686
Natural variant15031G → C Found in a stomach cancer cell line. Ref.14
VAR_064687
Natural variant15601Q → H Found in an endometrial cancer cell line. Ref.14
VAR_064688
Natural variant16141I → N Found in a case of clear cell renal carcinoma; somatic mutation. Ref.14
VAR_064689
Natural variant16471R → C Found in a breast cancer cell line. Ref.14
VAR_064690

Experimental info

Sequence conflict11M → T in AAI15011. Ref.4
Sequence conflict651G → S in AAI15011. Ref.4
Sequence conflict2421Y → C in AAI15012. Ref.4
Sequence conflict2511D → V in AAI15011. Ref.4
Sequence conflict4301L → P in AAI15012. Ref.4
Sequence conflict5531K → R in AAG34760. Ref.1
Sequence conflict5671D → Y in AAI15012. Ref.4
Sequence conflict7501L → P in AAI15012. Ref.4
Sequence conflict7921H → R in AAI15012. Ref.4
Sequence conflict9271Missing in AAI15010. Ref.4
Sequence conflict9271Missing in BAB71210. Ref.5
Sequence conflict9631Y → H in BAB71210. Ref.5
Sequence conflict11441G → V in AAG34760. Ref.1
Sequence conflict12451R → K in AAG34760. Ref.1
Sequence conflict13061E → G in AAG34760. Ref.1
Sequence conflict13491L → P in AAI15010. Ref.4
Sequence conflict14881G → D in AAI15012. Ref.4
Sequence conflict15681G → R in AAG34760. Ref.1

Secondary structure

............................................................................................. 1689
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 0A656E319C4FC748

FASTA1,689192,948
        10         20         30         40         50         60 
MGSKRRRATS PSSSVSGDFD DGHHSVSTPG PSRKRRRLSN LPTVDPIAVC HELYNTIRDY 

        70         80         90        100        110        120 
KDEQGRLLCE LFIRAPKRRN QPDYYEVVSQ PIDLMKIQQK LKMEEYDDVN LLTADFQLLF 

       130        140        150        160        170        180 
NNAKSYYKPD SPEYKAACKL WDLYLRTRNE FVQKGEADDE DDDEDGQDNQ GTVTEGSSPA 

       190        200        210        220        230        240 
YLKEILEQLL EAIVVATNPS GRLISELFQK LPSKVQYPDY YAIIKEPIDL KTIAQRIQNG 

       250        260        270        280        290        300 
SYKSIHAMAK DIDLLAKNAK TYNEPGSQVF KDANSIKKIF YMKKAEIEHH EMAKSSLRMR 

       310        320        330        340        350        360 
TPSNLAAARL TGPSHSKGSL GEERNPTSKY YRNKRAVQGG RLSAITMALQ YGSESEEDAA 

       370        380        390        400        410        420 
LAAARYEEGE SEAESITSFM DVSNPFYQLY DTVRSCRNNQ GQLIAEPFYH LPSKKKYPDY 

       430        440        450        460        470        480 
YQQIKMPISL QQIRTKLKNQ EYETLDHLEC DLNLMFENAK RYNVPNSAIY KRVLKLQQVM 

       490        500        510        520        530        540 
QAKKKELARR DDIEDGDSMI SSATSDTGSA KRKSKKNIRK QRMKILFNVV LEAREPGSGR 

       550        560        570        580        590        600 
RLCDLFMVKP SKKDYPDYYK IILEPMDLKI IEHNIRNDKY AGEEGMIEDM KLMFRNARHY 

       610        620        630        640        650        660 
NEEGSQVYND AHILEKLLKE KRKELGPLPD DDDMASPKLK LSRKSGISPK KSKYMTPMQQ 

       670        680        690        700        710        720 
KLNEVYEAVK NYTDKRGRRL SAIFLRLPSR SELPDYYLTI KKPMDMEKIR SHMMANKYQD 

       730        740        750        760        770        780 
IDSMVEDFVM MFNNACTYNE PESLIYKDAL VLHKVLLETR RDLEGDEDSH VPNVTLLIQE 

       790        800        810        820        830        840 
LIHNLFVSVM SHQDDEGRCY SDSLAEIPAV DPNFPNKPPL TFDIIRKNVE NNRYRRLDLF 

       850        860        870        880        890        900 
QEHMFEVLER ARRMNRTDSE IYEDAVELQQ FFIKIRDELC KNGEILLSPA LSYTTKHLHN 

       910        920        930        940        950        960 
DVEKERKEKL PKEIEEDKLK REEEKREAEK SEDSSGAAGL SGLHRTYSQD CSFKNSMYHV 

       970        980        990       1000       1010       1020 
GDYVYVEPAE ANLQPHIVCI ERLWEDSAGE KWLYGCWFYR PNETFHLATR KFLEKEVFKS 

      1030       1040       1050       1060       1070       1080 
DYYNKVPVSK ILGKCVVMFV KEYFKLCPEN FRDEDVFVCE SRYSAKTKSF KKIKLWTMPI 

      1090       1100       1110       1120       1130       1140 
SSVRFVPRDV PLPVVRVASV FANADKGDDE KNTDNSEDSR AEDNFNLEKE KEDVPVEMSN 

      1150       1160       1170       1180       1190       1200 
GEPGCHYFEQ LHYNDMWLKV GDCVFIKSHG LVRPRVGRIE KVWVRDGAAY FYGPIFIHPE 

      1210       1220       1230       1240       1250       1260 
ETEHEPTKMF YKKEVFLSNL EETCPMTCIL GKCAVLSFKD FLSCRPTEIP ENDILLCESR 

      1270       1280       1290       1300       1310       1320 
YNESDKQMKK FKGLKRFSLS AKVVDDEIYY FRKPIVPQKE PSPLLEKKIQ LLEAKFAELE 

      1330       1340       1350       1360       1370       1380 
GGDDDIEEMG EEDSEVIEPP SLPQLQTPLA SELDLMPYTP PQSTPKSAKG SAKKEGSKRK 

      1390       1400       1410       1420       1430       1440 
INMSGYILFS SEMRAVIKAQ HPDYSFGELS RLVGTEWRNL ETAKKAEYEE RAAKVAEQQE 

      1450       1460       1470       1480       1490       1500 
RERAAQQQQP SASPRAGTPV GALMGVVPPP TPMGMLNQQL TPVAGMMGGY PPGLPPLQGP 

      1510       1520       1530       1540       1550       1560 
VDGLVSMGSM QPLHPGGPPP HHLPPGVPGL PGIPPPGVMN QGVAPMVGTP APGGSPYGQQ 

      1570       1580       1590       1600       1610       1620 
VGVLGPPGQQ APPPYPGPHP AGPPVIQQPT TPMFVAPPPK TQRLLHSEAY LKYIEGLSAE 

      1630       1640       1650       1660       1670       1680 
SNSISKWDQT LAARRRDVHL SKEQESRLPS HWLKSKGAHT TMADALWRLR DLMLRDTLNI 


RQAYNLENV 

« Hide

Isoform 2 [UniParc].

Checksum: FAB1C935A9B8B4DD
Show »

FASTA1,634187,188
Isoform 3 [UniParc].

Checksum: B8BA103E359A48DA
Show »

FASTA1,602183,690
Isoform 4 [UniParc].

Checksum: A2B8A14FAB928A3C
Show »

FASTA1,582181,085
Isoform 5 [UniParc].

Checksum: BCBD5D8E42BAB076
Show »

FASTA1,582182,118
Isoform 6 [UniParc].

Checksum: AE378B417E0493B3
Show »

FASTA85699,142
Isoform 7 [UniParc].

Checksum: 710520F65FF9E981
Show »

FASTA1,597183,885
Isoform 8 [UniParc].

Checksum: E5BA80E11EE7E6C0
Show »

FASTA1,652189,645
Isoform 9 [UniParc].

Checksum: 38BB16B06929BFFC
Show »

FASTA1,609184,043

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma."
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. expand/collapse author list , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.
Nature 469:539-542(2011) [PubMed] [Europe PMC] [Abstract]
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]"Histone recognition and large-scale structural analysis of the human bromodomain family."
Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., Gingras A.C., Arrowsmith C.H., Knapp S.
Cell 149:214-231(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS) OF 43-917, INTERACTION WITH HISTONE H3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS43099.1. [Q86U86-4]
RefSeqNP_060783.3. NM_018313.4. [Q86U86-4]
UniGeneHs.189920.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ86U86.
SMRQ86U86. Positions 26-293, 383-766, 773-914, 957-1102, 1160-1272, 1370-1444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120490. 33 interactions.
DIPDIP-33045N.
IntActQ86U86. 14 interactions.
MINTMINT-1195749.

Chemistry

ChEMBLCHEMBL1795184.

PTM databases

PhosphoSiteQ86U86.

Polymorphism databases

DMDM73921624.

Proteomic databases

MaxQBQ86U86.
PaxDbQ86U86.
PRIDEQ86U86.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296302; 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]
GeneID55193.
KEGGhsa:55193.
UCSCuc003deq.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

CTD55193.
GeneCardsGC03M052579.
H-InvDBHIX0003364.
HGNCHGNC:30064. PBRM1.
HPAHPA015629.
MIM144700. phenotype.
606083. gene.
neXtProtNX_Q86U86.
PharmGKBPA162398846.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOVERGENHBG079860.
InParanoidQ86U86.
KOK11757.
OMAILGKCVV.
OrthoDBEOG78H3S6.
PhylomeDBQ86U86.
TreeFamTF106120.

Gene expression databases

ArrayExpressQ86U86.
BgeeQ86U86.
GenevestigatorQ86U86.

Family and domain databases

Gene3D1.10.30.10. 1 hit.
1.20.920.10. 6 hits.
InterProIPR001025. BAH_dom.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR009071. HMG_box_dom.
[Graphical view]
PfamPF01426. BAH. 2 hits.
PF00439. Bromodomain. 6 hits.
PF00505. HMG_box. 1 hit.
[Graphical view]
PRINTSPR00503. BROMODOMAIN.
SMARTSM00439. BAH. 2 hits.
SM00297. BROMO. 6 hits.
SM00398. HMG. 1 hit.
[Graphical view]
SUPFAMSSF47095. SSF47095. 1 hit.
SSF47370. SSF47370. 6 hits.
PROSITEPS51038. BAH. 2 hits.
PS00633. BROMODOMAIN_1. 5 hits.
PS50014. BROMODOMAIN_2. 6 hits.
PS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPBRM1. human.
EvolutionaryTraceQ86U86.
GeneWikiPBRM1.
GenomeRNAi55193.
NextBio59051.
PROQ86U86.
SOURCESearch...

Entry information

Entry namePB1_HUMAN
AccessionPrimary (citable) accession number: Q86U86
Secondary accession number(s): A1L381 expand/collapse secondary AC list , A1L382, A4FUJ7, Q1RMD1, Q1RMD2, Q96MS2, Q9H2T3, Q9H2T4, Q9H2T5, Q9H301, Q9H314
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM