Q86U86 · PB1_HUMAN

  • Protein
    Protein polybromo-1
  • Gene
    PBRM1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for the stability of the SWI/SNF chromatin remodeling complex SWI/SNF-B (PBAF). Acts as a negative regulator of cell proliferation.

Features

Showing features for dna binding.

116892004006008001,0001,2001,4001,600
TypeIDPosition(s)Description
DNA binding1379-1447HMG box

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromatin
Cellular Componentkinetochore
Cellular Componentnuclear chromosome
Cellular Componentnuclear matrix
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentRSC-type complex
Cellular ComponentSWI/SNF complex
Molecular Functionchromatin binding
Molecular FunctionDNA binding
Biological Processchromatin remodeling
Biological Processmitotic cell cycle
Biological Processnegative regulation of cell population proliferation
Biological Processpositive regulation of cell differentiation
Biological Processpositive regulation of double-strand break repair
Biological Processpositive regulation of myoblast differentiation
Biological Processpositive regulation of T cell differentiation
Biological Processregulation of G0 to G1 transition
Biological Processregulation of G1/S transition of mitotic cell cycle
Biological Processregulation of mitotic metaphase/anaphase transition
Biological Processregulation of nucleotide-excision repair
Biological Processregulation of transcription by RNA polymerase II
Biological Processtranscription elongation by RNA polymerase II

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein polybromo-1
  • Short names
    hPB1
  • Alternative names
    • BRG1-associated factor 180 (BAF180)
    • Polybromo-1D

Gene names

    • Name
      PBRM1
    • Synonyms
      BAF180, PB1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q86U86
  • Secondary accessions
    • A1L381
    • A1L382
    • A4FUJ7
    • Q1RMD1
    • Q1RMD2

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Involvement in disease

Renal cell carcinoma (RCC)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    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.
  • See also
    MIM:144700

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_06465349found in a lung cancer cell line; dbSNP:rs542945393
Natural variantVAR_06465456found in a brain cancer cell line; dbSNP:rs923060956
Natural variantVAR_06465557found in a case of clear cell renal carcinoma; somatic mutation
Natural variantVAR_06465666found in a colon cancer cell line; dbSNP:rs368888772
Natural variantVAR_06465790found in a bladder cancer cell line
Natural variantVAR_064658144found in a malignant melanoma cell line; dbSNP:rs2153927262
Natural variantVAR_064659160found in a malignant melanoma cell line
Natural variantVAR_064660202found in a endometrial cancer cell line; dbSNP:rs765525545
Natural variantVAR_064661206found in hematopoietic and lymphoid cancer cell lines; dbSNP:rs1359676390
Natural variantVAR_064662226found in hematopoietic and lymphoid cancer cell lines
Natural variantVAR_064663228found in a breast cancer cell line; dbSNP:rs201022657
Natural variantVAR_064664232found in a case of clear cell renal carcinoma; somatic mutation
Natural variantVAR_064665233found in a renal carcinoma cell line
Natural variantVAR_064666256found in an ovary carcinoma cell line; dbSNP:rs776146971
Natural variantVAR_064667340found in a malignant melanoma cell line; dbSNP:rs200106731
Natural variantVAR_064668523found in a case of clear cell renal carcinoma; somatic mutation; dbSNP:rs2153490743
Natural variantVAR_064669540found in a case of clear cell renal carcinoma; somatic mutation
Natural variantVAR_064670597found in a case of clear cell renal carcinoma; somatic mutation
Natural variantVAR_064671621found in a case of clear cell renal carcinoma; somatic mutation
Natural variantVAR_064672661found in a case of clear cell renal carcinoma; somatic mutation
Natural variantVAR_064673674found in a case of clear cell renal carcinoma; somatic mutation
Natural variantVAR_064674678in dbSNP:rs1422119249
Natural variantVAR_064675893found in hematopoietic, lymphoid, lung and liver cancer cell lines; dbSNP:rs753344888
Natural variantVAR_064676895found in a lung cancer cell line
Natural variantVAR_064677922found in a breast cancer cell line
Natural variantVAR_064678925found in a colon cancer cell line
Natural variantVAR_0646791079found in a colon cancer cell line; requires 2 nucleotide substitutions
Natural variantVAR_0646801098found in hematopoietic and lymphoid cancer cell lines; dbSNP:rs201156614
Natural variantVAR_0646811120found in hematopoietic and lymphoid cancer cell lines; dbSNP:rs35102895
Natural variantVAR_0646821177found in a kidney cancer cell line
Natural variantVAR_0646831204found in a case of clear cell renal carcinoma; somatic mutation
Natural variantVAR_0646841209-1214found in a case of clear cell renal carcinoma; somatic mutation
Natural variantVAR_0646851287found in a breast cancer cell line; dbSNP:rs2084387436
Natural variantVAR_0646861414found in a lung cancer cell line; dbSNP:rs2153489547
Natural variantVAR_0646871503found in a stomach cancer cell line
Natural variantVAR_0646881560found in an endometrial cancer cell line
Natural variantVAR_0646891614found in a case of clear cell renal carcinoma; somatic mutation; dbSNP:rs2080680257
Natural variantVAR_0646901647found in a breast cancer cell line; dbSNP:rs200020801

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 4,661 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue, cross-link.

TypeIDPosition(s)SourceDescription
ChainPRO_00002112071-1689UniProtProtein polybromo-1
Modified residue (large scale data)9PRIDEPhosphothreonine
Modified residue10UniProtPhosphoserine
Modified residue (large scale data)10PRIDEPhosphoserine
Modified residue (large scale data)12PRIDEPhosphoserine
Modified residue (large scale data)13PRIDEPhosphoserine
Modified residue (large scale data)14PRIDEPhosphoserine
Modified residue (large scale data)16PRIDEPhosphoserine
Modified residue (large scale data)25PRIDEPhosphoserine
Modified residue (large scale data)28PRIDEPhosphothreonine
Modified residue39UniProtPhosphoserine
Modified residue (large scale data)39PRIDEPhosphoserine
Modified residue (large scale data)43PRIDEPhosphothreonine
Cross-link96UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue131UniProtPhosphoserine
Modified residue (large scale data)131PRIDEPhosphoserine
Modified residue134UniProtPhosphotyrosine
Cross-link154UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue178UniProtPhosphoserine
Modified residue (large scale data)178PRIDEPhosphoserine
Cross-link210UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)301PRIDEPhosphothreonine
Modified residue (large scale data)303PRIDEPhosphoserine
Modified residue (large scale data)314PRIDEPhosphoserine
Modified residue316UniProtPhosphoserine
Modified residue (large scale data)316PRIDEPhosphoserine
Modified residue319UniProtPhosphoserine
Modified residue (large scale data)319PRIDEPhosphoserine
Modified residue (large scale data)351PRIDEPhosphotyrosine
Modified residue353UniProtPhosphoserine
Modified residue (large scale data)353PRIDEPhosphoserine
Modified residue355UniProtPhosphoserine
Modified residue (large scale data)355PRIDEPhosphoserine
Modified residue (large scale data)366PRIDEPhosphotyrosine
Modified residue371UniProtPhosphoserine
Modified residue (large scale data)371PRIDEPhosphoserine
Modified residue375UniProtPhosphoserine
Modified residue (large scale data)375PRIDEPhosphoserine
Modified residue414UniProtN6-acetyllysine
Cross-link425UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link471UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue498UniProtPhosphoserine
Modified residue (large scale data)498PRIDEPhosphoserine
Modified residue (large scale data)501PRIDEPhosphoserine
Modified residue (large scale data)502PRIDEPhosphoserine
Modified residue (large scale data)505PRIDEPhosphoserine
Modified residue (large scale data)507PRIDEPhosphothreonine
Modified residue509UniProtPhosphoserine
Modified residue (large scale data)509PRIDEPhosphoserine
Cross-link511UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link591UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)605PRIDEPhosphoserine
Modified residue636UniProtPhosphoserine
Modified residue (large scale data)636PRIDEPhosphoserine
Cross-link638UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue648UniProtPhosphoserine
Modified residue (large scale data)648PRIDEPhosphoserine
Cross-link653UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)681PRIDEPhosphoserine
Modified residue689UniProtPhosphoserine
Modified residue (large scale data)931PRIDEPhosphoserine
Modified residue (large scale data)934PRIDEPhosphoserine
Modified residue (large scale data)935PRIDEPhosphoserine
Modified residue (large scale data)946PRIDEPhosphothreonine
Modified residue948UniProtPhosphoserine
Modified residue (large scale data)948PRIDEPhosphoserine
Modified residue (large scale data)952PRIDEPhosphoserine
Modified residue987UniProtPhosphoserine
Modified residue (large scale data)987PRIDEPhosphoserine
Modified residue (large scale data)1099PRIDEPhosphoserine
Cross-link1106UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1111UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)1116PRIDEPhosphoserine
Modified residue1119UniProtPhosphoserine
Modified residue (large scale data)1119PRIDEPhosphoserine
Cross-link1167UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1289UniProtPhosphotyrosine
Cross-link1293UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate
Cross-link1293UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate
Cross-link1308UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1398UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue1405UniProtPhosphoserine
Modified residue (large scale data)1405PRIDEPhosphoserine
Modified residue (large scale data)1410PRIDEPhosphoserine
Modified residue (large scale data)1451PRIDEPhosphoserine
Modified residue1453UniProtPhosphoserine
Modified residue (large scale data)1453PRIDEPhosphoserine
Cross-link1642UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1654UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link1656UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Widely expressed.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 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

Binary interactions

View interactors in UniProtKB
View CPX-1196 in Complex Portal

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-21Polar residues
Region1-39Disordered
Domain64-134Bromo 1
Region155-177Disordered
Domain200-270Bromo 2
Domain400-470Bromo 3
Region487-517Disordered
Domain538-608Bromo 4
Compositional bias625-639Basic and acidic residues
Region625-646Disordered
Domain676-746Bromo 5
Domain792-862Bromo 6
Compositional bias902-933Basic and acidic residues
Region902-941Disordered
Domain956-1074BAH 1
Region1106-1133Disordered
Domain1156-1272BAH 2
Region1354-1378Disordered
Region1431-1460Disordered

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (9)
  • Sequence status
    Complete

This entry describes 9 isoforms produced by Alternative splicing.

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.

  • Length
    1,689
  • Mass (Da)
    192,948
  • Last updated
    2003-06-01 v1
  • Checksum
    0A656E319C4FC748
MGSKRRRATSPSSSVSGDFDDGHHSVSTPGPSRKRRRLSNLPTVDPIAVCHELYNTIRDYKDEQGRLLCELFIRAPKRRNQPDYYEVVSQPIDLMKIQQKLKMEEYDDVNLLTADFQLLFNNAKSYYKPDSPEYKAACKLWDLYLRTRNEFVQKGEADDEDDDEDGQDNQGTVTEGSSPAYLKEILEQLLEAIVVATNPSGRLISELFQKLPSKVQYPDYYAIIKEPIDLKTIAQRIQNGSYKSIHAMAKDIDLLAKNAKTYNEPGSQVFKDANSIKKIFYMKKAEIEHHEMAKSSLRMRTPSNLAAARLTGPSHSKGSLGEERNPTSKYYRNKRAVQGGRLSAITMALQYGSESEEDAALAAARYEEGESEAESITSFMDVSNPFYQLYDTVRSCRNNQGQLIAEPFYHLPSKKKYPDYYQQIKMPISLQQIRTKLKNQEYETLDHLECDLNLMFENAKRYNVPNSAIYKRVLKLQQVMQAKKKELARRDDIEDGDSMISSATSDTGSAKRKSKKNIRKQRMKILFNVVLEAREPGSGRRLCDLFMVKPSKKDYPDYYKIILEPMDLKIIEHNIRNDKYAGEEGMIEDMKLMFRNARHYNEEGSQVYNDAHILEKLLKEKRKELGPLPDDDDMASPKLKLSRKSGISPKKSKYMTPMQQKLNEVYEAVKNYTDKRGRRLSAIFLRLPSRSELPDYYLTIKKPMDMEKIRSHMMANKYQDIDSMVEDFVMMFNNACTYNEPESLIYKDALVLHKVLLETRRDLEGDEDSHVPNVTLLIQELIHNLFVSVMSHQDDEGRCYSDSLAEIPAVDPNFPNKPPLTFDIIRKNVENNRYRRLDLFQEHMFEVLERARRMNRTDSEIYEDAVELQQFFIKIRDELCKNGEILLSPALSYTTKHLHNDVEKERKEKLPKEIEEDKLKREEEKREAEKSEDSSGAAGLSGLHRTYSQDCSFKNSMYHVGDYVYVEPAEANLQPHIVCIERLWEDSAGEKWLYGCWFYRPNETFHLATRKFLEKEVFKSDYYNKVPVSKILGKCVVMFVKEYFKLCPENFRDEDVFVCESRYSAKTKSFKKIKLWTMPISSVRFVPRDVPLPVVRVASVFANADKGDDEKNTDNSEDSRAEDNFNLEKEKEDVPVEMSNGEPGCHYFEQLHYNDMWLKVGDCVFIKSHGLVRPRVGRIEKVWVRDGAAYFYGPIFIHPEETEHEPTKMFYKKEVFLSNLEETCPMTCILGKCAVLSFKDFLSCRPTEIPENDILLCESRYNESDKQMKKFKGLKRFSLSAKVVDDEIYYFRKPIVPQKEPSPLLEKKIQLLEAKFAELEGGDDDIEEMGEEDSEVIEPPSLPQLQTPLASELDLMPYTPPQSTPKSAKGSAKKEGSKRKINMSGYILFSSEMRAVIKAQHPDYSFGELSRLVGTEWRNLETAKKAEYEERAAKVAEQQERERAAQQQQPSASPRAGTPVGALMGVVPPPTPMGMLNQQLTPVAGMMGGYPPGLPPLQGPVDGLVSMGSMQPLHPGGPPPHHLPPGVPGLPGIPPPGVMNQGVAPMVGTPAPGGSPYGQQVGVLGPPGQQAPPPYPGPHPAGPPVIQQPTTPMFVAPPPKTQRLLHSEAYLKYIEGLSAESNSISKWDQTLAARRRDVHLSKEQESRLPSHWLKSKGAHTTMADALWRLRDLMLRDTLNIRQAYNLENV

Q86U86-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86U86-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86U86-4

Q86U86-5

Q86U86-6

  • Name
    6
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86U86-7

Q86U86-8

  • Name
    8
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q86U86-9

Computationally mapped potential isoform sequences

There are 9 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9J9L6C9J9L6_HUMANPBRM126
C9J409C9J409_HUMANPBRM143
C9J053C9J053_HUMANPBRM1118
E7EVG2E7EVG2_HUMANPBRM11460
C9JPI5C9JPI5_HUMANPBRM1230
C9JQF1C9JQF1_HUMANPBRM1152
C9JCJ2C9JCJ2_HUMANPBRM187
H0Y5B5H0Y5B5_HUMANPBRM11085
A0A9L9PXL4A0A9L9PXL4_HUMANPBRM11704

Sequence caution

The sequence AAI15010.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence.
The sequence AAI15011.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.
The sequence AAI15012.1 differs from that shown. Reason: Erroneous termination Truncated C-terminus.
The sequence BAB71210.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict, compositional bias, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict1in Ref. 4; AAI15011
Compositional bias1-21Polar residues
Sequence conflict65in Ref. 4; AAI15011
Sequence conflict242in Ref. 4; AAI15012
Sequence conflict251in Ref. 4; AAI15011
Alternative sequenceVSP_015231300-332in isoform 3
Sequence conflict430in Ref. 4; AAI15012
Alternative sequenceVSP_035499513in isoform 7 and isoform 8
Sequence conflict553in Ref. 1; AAG34760
Sequence conflict567in Ref. 4; AAI15012
Compositional bias625-639Basic and acidic residues
Sequence conflict750in Ref. 4; AAI15012
Sequence conflict792in Ref. 4; AAI15012
Alternative sequenceVSP_015232857-1689in isoform 6
Compositional bias902-933Basic and acidic residues
Sequence conflict927in Ref. 4; AAI15010 and 5; BAB71210
Sequence conflict963in Ref. 5; BAB71210
Alternative sequenceVSP_015233989-1013in isoform 4 and isoform 9
Sequence conflict1144in Ref. 1; AAG34760
Sequence conflict1245in Ref. 1; AAG34760
Sequence conflict1306in Ref. 1; AAG34760
Alternative sequenceVSP_0152341336-1362in isoform 4
Sequence conflict1349in Ref. 4; AAI15010
Alternative sequenceVSP_0152351430-1484in isoform 2, isoform 3, isoform 4, isoform 5, isoform 7 and isoform 9
Alternative sequenceVSP_0152361485-1536in isoform 5, isoform 7 and isoform 8
Sequence conflict1488in Ref. 4; AAI15012
Sequence conflict1568in Ref. 1; AAG34760

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF197569
EMBL· GenBank· DDBJ
AAG34760.1
EMBL· GenBank· DDBJ
mRNA
AF225870
EMBL· GenBank· DDBJ
AAG48939.1
EMBL· GenBank· DDBJ
mRNA
AF225871
EMBL· GenBank· DDBJ
AAG48940.1
EMBL· GenBank· DDBJ
mRNA
AF225872
EMBL· GenBank· DDBJ
AAG48941.1
EMBL· GenBank· DDBJ
mRNA
AF177387
EMBL· GenBank· DDBJ
AAG48933.1
EMBL· GenBank· DDBJ
mRNA
AY281068
EMBL· GenBank· DDBJ
AAP34197.1
EMBL· GenBank· DDBJ
mRNA
BC115009
EMBL· GenBank· DDBJ
AAI15010.1
EMBL· GenBank· DDBJ
mRNA Different termination.
BC115010
EMBL· GenBank· DDBJ
AAI15011.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC115011
EMBL· GenBank· DDBJ
AAI15012.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC129934
EMBL· GenBank· DDBJ
AAI29935.1
EMBL· GenBank· DDBJ
mRNA
BC129935
EMBL· GenBank· DDBJ
AAI29936.1
EMBL· GenBank· DDBJ
mRNA
AK056541
EMBL· GenBank· DDBJ
BAB71210.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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