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Protein

Protein BANP

Gene

Banp

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Controls V(D)J recombination during T-cell development by repressing T-cell receptor (TCR) beta enhancer function. Binds to scaffold/matrix attachment region beta (S/MARbeta), an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Represses cyclin D1 transcription by recruiting HDAC1 to its promoter, thereby diminishing H3K9ac, H3S10ph and H4K8ac levels. Promotes TP53 'Ser-15' phosphorylation and nuclear accumulation, which causes cell cycle arrest and inhibits tumor growth.7 Publications

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • p53 binding Source: MGI

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • chromatin modification Source: UniProtKB-KW
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of protein catabolic process Source: MGI
  • positive regulation of transcription, DNA-templated Source: CACAO
  • protein localization to nucleus Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Developmental protein, Repressor

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein BANP
Alternative name(s):
Btg3-associated nuclear protein
Scaffold/matrix-associated region-1-binding protein
Gene namesi
Name:Banp
Synonyms:Smar1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1889023. Banp.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi347 – 3471S → A: Impairs TP53 activation. 1 Publication
Mutagenesisi348 – 3481S → A: No effect on TP53 activation. 1 Publication
Mutagenesisi349 – 3491S → A: No effect on TP53 activation. 1 Publication
Mutagenesisi350 – 3501S → A: No effect on TP53 activation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Protein BANPPRO_0000297911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191PhosphoserineBy similarity
Modified residuei283 – 2831N6-acetyllysineCombined sources
Modified residuei347 – 3471Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8VBU8.
MaxQBiQ8VBU8.
PaxDbiQ8VBU8.
PRIDEiQ8VBU8.

PTM databases

iPTMnetiQ8VBU8.
PhosphoSiteiQ8VBU8.

Expressioni

Tissue specificityi

Highly expressed in heart, spleen, and thymus. Isoform 1 is highly expressed in kidney, brain and testis. Isoform 3 is highly expressed in kidney and lung.3 Publications

Gene expression databases

BgeeiQ8VBU8.
CleanExiMM_BANP.
ExpressionAtlasiQ8VBU8. baseline and differential.
GenevisibleiQ8VBU8. MM.

Interactioni

Subunit structurei

Interacts with TP53, CUX1/CDP and HDAC1. Part of a corepressor complex containing BANP, HDAC1, SIN3A, SIN3B, RBL1 and RBL2.4 Publications

GO - Molecular functioni

  • p53 binding Source: MGI

Protein-protein interaction databases

BioGridi207288. 1 interaction.
IntActiQ8VBU8. 1 interaction.
MINTiMINT-1686827.
STRINGi10090.ENSMUSP00000132095.

Structurei

3D structure databases

ProteinModelPortaliQ8VBU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini234 – 33097BENPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni160 – 350191Interaction with CUX1 and HDAC1Add
BLAST
Regioni328 – 35730Necessary and sufficient for TP53 activationAdd
BLAST
Regioni350 – 40051DNA-bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili65 – 9834Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi347 – 3548Poly-Ser
Compositional biasi368 – 44174Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the BANP/SMAR1 family.Curated
Contains 1 BEN domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IGMM. Eukaryota.
ENOG410Z2PJ. LUCA.
GeneTreeiENSGT00390000011116.
HOGENOMiHOG000015355.
HOVERGENiHBG107493.
InParanoidiQ8VBU8.
OMAiIISNAVP.
OrthoDBiEOG7XDBFQ.
PhylomeDBiQ8VBU8.
TreeFamiTF331908.

Family and domain databases

InterProiIPR018379. BEN_domain.
[Graphical view]
PfamiPF10523. BEN. 1 hit.
[Graphical view]
SMARTiSM01025. BEN. 1 hit.
[Graphical view]
PROSITEiPS51457. BEN. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8VBU8-1) [UniParc]FASTAAdd to basket

Also known as: Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MMSEQDLADV VQIAVEDLSP DHPVVLENHV VTDDDEPALK RQRLEINCQD
60 70 80 90 100
PSIKSFLYSI NQTICLRLDS IEAKLQALEA TCKSLEEKLD LVTNKQHSPI
110 120 130 140 150
QVPMVAGSPL GATQTCNKVR CVVPQTTVIL NNDRQNAIVA KMEDPLSNRA
160 170 180 190 200
PDSLENIISN AVPGRRQNTI VVKVPGQDDS HNEDGESGSE ASDSVSNCGQ
210 220 230 240 250
PGSQNIGSNV TLITLNSEED YPNGTWLGDE NNPEMRVRCA IIPSDMLHIS
260 270 280 290 300
TNCRTAEKMA LTLLDYLFHR EVQAVSNLSG QGKHGKKQLD PLTIYGIRCH
310 320 330 340 350
LFYKFGITES DWYRIKQSID SKCRTAWRRK QRGQSLAVKS FSRRTPSSSS
360 370 380 390 400
YSASETMMGT PPPTSELQQS QPQALHYALA NAQQVQIHQI GEDGQVQVIP
410 420 430 440 450
QGHLHIAQVP QGEQVQITQD SEGNLQIHHV GQDGQSWGLC QNPIPVSGDS
460 470 480 490 500
VAQANPSQLW PLGGDTLDLP AGNEMIQVLQ GAQLIAVASS DPAATGVDGS
510 520 530 540
PLQGSDIQVQ YVQLAPVSDH TAAAQTAEAL QPTLQPDMQL EHGAIQIQ
Length:548
Mass (Da):59,657
Last modified:March 1, 2002 - v1
Checksum:i9C48D5E122ECB2D1
GO
Isoform 2 (identifier: Q8VBU8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     122-160: Missing.

Show »
Length:509
Mass (Da):55,384
Checksum:i5CA169C13D207173
GO
Isoform 3 (identifier: Q8VBU8-3) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     122-160: Missing.
     399-401: Missing.

Show »
Length:506
Mass (Da):55,045
Checksum:iB71B80862BB10443
GO
Isoform 4 (identifier: Q8VBU8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     435-476: Missing.

Note: No experimental confirmation available.
Show »
Length:506
Mass (Da):55,297
Checksum:i7F6F4CD08FE3F87C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti131 – 1311N → I in AAG16659 (PubMed:10950932).Curated
Sequence conflicti147 – 1471S → I in AAG16659 (PubMed:10950932).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei122 – 16039Missing in isoform 2 and isoform 3. 3 PublicationsVSP_027403Add
BLAST
Alternative sequencei399 – 4013Missing in isoform 3. 2 PublicationsVSP_027404
Alternative sequencei435 – 47642Missing in isoform 4. 1 PublicationVSP_027405Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091234 mRNA. Translation: AAC36358.1.
AF235503 mRNA. Translation: AAG16659.1.
AK154088 mRNA. Translation: BAE32366.1.
BC013339 mRNA. Translation: AAH13339.1.
BC021650 mRNA. Translation: AAH21650.1.
BC022168 mRNA. Translation: AAH22168.1.
BC062641 mRNA. Translation: AAH62641.1.
CCDSiCCDS40502.1. [Q8VBU8-1]
CCDS72176.1. [Q8VBU8-2]
CCDS72177.1. [Q8VBU8-3]
RefSeqiNP_001103570.1. NM_001110100.2.
NP_001272910.1. NM_001285981.1. [Q8VBU8-2]
NP_001272912.1. NM_001285983.1. [Q8VBU8-3]
NP_058092.2. NM_016812.4. [Q8VBU8-1]
XP_011246744.1. XM_011248442.1. [Q8VBU8-4]
UniGeneiMm.287163.

Genome annotation databases

EnsembliENSMUST00000026354; ENSMUSP00000026354; ENSMUSG00000025316. [Q8VBU8-2]
ENSMUST00000093078; ENSMUSP00000090766; ENSMUSG00000025316. [Q8VBU8-3]
ENSMUST00000170857; ENSMUSP00000132095; ENSMUSG00000025316. [Q8VBU8-1]
ENSMUST00000173254; ENSMUSP00000133783; ENSMUSG00000025316. [Q8VBU8-4]
GeneIDi53325.
KEGGimmu:53325.
UCSCiuc009nsg.3. mouse. [Q8VBU8-1]
uc009nsh.3. mouse. [Q8VBU8-3]
uc033jih.1. mouse. [Q8VBU8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF091234 mRNA. Translation: AAC36358.1.
AF235503 mRNA. Translation: AAG16659.1.
AK154088 mRNA. Translation: BAE32366.1.
BC013339 mRNA. Translation: AAH13339.1.
BC021650 mRNA. Translation: AAH21650.1.
BC022168 mRNA. Translation: AAH22168.1.
BC062641 mRNA. Translation: AAH62641.1.
CCDSiCCDS40502.1. [Q8VBU8-1]
CCDS72176.1. [Q8VBU8-2]
CCDS72177.1. [Q8VBU8-3]
RefSeqiNP_001103570.1. NM_001110100.2.
NP_001272910.1. NM_001285981.1. [Q8VBU8-2]
NP_001272912.1. NM_001285983.1. [Q8VBU8-3]
NP_058092.2. NM_016812.4. [Q8VBU8-1]
XP_011246744.1. XM_011248442.1. [Q8VBU8-4]
UniGeneiMm.287163.

3D structure databases

ProteinModelPortaliQ8VBU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207288. 1 interaction.
IntActiQ8VBU8. 1 interaction.
MINTiMINT-1686827.
STRINGi10090.ENSMUSP00000132095.

PTM databases

iPTMnetiQ8VBU8.
PhosphoSiteiQ8VBU8.

Proteomic databases

EPDiQ8VBU8.
MaxQBiQ8VBU8.
PaxDbiQ8VBU8.
PRIDEiQ8VBU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026354; ENSMUSP00000026354; ENSMUSG00000025316. [Q8VBU8-2]
ENSMUST00000093078; ENSMUSP00000090766; ENSMUSG00000025316. [Q8VBU8-3]
ENSMUST00000170857; ENSMUSP00000132095; ENSMUSG00000025316. [Q8VBU8-1]
ENSMUST00000173254; ENSMUSP00000133783; ENSMUSG00000025316. [Q8VBU8-4]
GeneIDi53325.
KEGGimmu:53325.
UCSCiuc009nsg.3. mouse. [Q8VBU8-1]
uc009nsh.3. mouse. [Q8VBU8-3]
uc033jih.1. mouse. [Q8VBU8-2]

Organism-specific databases

CTDi54971.
MGIiMGI:1889023. Banp.

Phylogenomic databases

eggNOGiENOG410IGMM. Eukaryota.
ENOG410Z2PJ. LUCA.
GeneTreeiENSGT00390000011116.
HOGENOMiHOG000015355.
HOVERGENiHBG107493.
InParanoidiQ8VBU8.
OMAiIISNAVP.
OrthoDBiEOG7XDBFQ.
PhylomeDBiQ8VBU8.
TreeFamiTF331908.

Miscellaneous databases

NextBioi310141.
PROiQ8VBU8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8VBU8.
CleanExiMM_BANP.
ExpressionAtlasiQ8VBU8. baseline and differential.
GenevisibleiQ8VBU8. MM.

Family and domain databases

InterProiIPR018379. BEN_domain.
[Graphical view]
PfamiPF10523. BEN. 1 hit.
[Graphical view]
SMARTiSM01025. BEN. 1 hit.
[Graphical view]
PROSITEiPS51457. BEN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Embryo.
  2. "SMAR1, a novel, alternatively spliced gene product, binds the Scaffold/Matrix-associated region at the T cell receptor beta locus."
    Chattopadhyay S., Kaul R., Charest A., Housman D., Chen J.
    Genomics 68:93-96(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, FUNCTION.
    Strain: C57BL/6J.
    Tissue: Thymus.
  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] (ISOFORM 3).
    Strain: NOD.
    Tissue: Dendritic cell.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-548 (ISOFORM 4).
    Strain: C57BL/6J, Czech II and FVB/N.
    Tissue: Brain, Mammary tumor and Salivary gland.
  5. "Direct interaction with and activation of p53 by SMAR1 retards cell-cycle progression at G2/M phase and delays tumor growth in mice."
    Kaul R., Mukherjee S., Ahmed F., Bhat M.K., Chhipa R., Galande S., Chattopadhyay S.
    Int. J. Cancer 103:606-615(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  6. "SMAR1 and Cux/CDP modulate chromatin and act as negative regulators of the TCRbeta enhancer (Ebeta)."
    Kaul-Ghanekar R., Jalota-Badhwar A., Pavithra L., Tucker P., Chattopadhyay S.
    Nucleic Acids Res. 32:4862-4875(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUX1, SUBCELLULAR LOCATION.
  7. "Abnormal V(D)J recombination of T cell receptor beta locus in SMAR1 transgenic mice."
    Kaul-Ghanekar R., Majumdar S., Jalota-Badhwar A., Gulati N., Dubey N., Saha B., Chattopadhyay S.
    J. Biol. Chem. 280:9450-9459(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Tumor suppressor SMAR1 activates and stabilizes p53 through its arginine-serine-rich motif."
    Jalota-Badhwar A., Singh K., Pavithra L., Kaul-Ghanekar R., Jameel S., Chattopadhyay S.
    J. Biol. Chem. 280:16019-16029(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TP53, SUBCELLULAR LOCATION.
  9. "Tumor suppressor SMAR1 mediates cyclin D1 repression by recruitment of the SIN3/histone deacetylase 1 complex."
    Rampalli S., Pavithra L., Bhatt A., Kundu T.K., Chattopadhyay S.
    Mol. Cell. Biol. 25:8415-8429(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HDAC1, IDENTIFICATION IN A COMPLEX WITH HDAC1; SIN3A; SIN3B; RBL1 AND RBL2, SUBCELLULAR LOCATION.
  10. "SMAR1-derived P44 peptide retains its tumor suppressor function through modulation of p53."
    Jalota-Badhwar A., Kaul-Ghanekar R., Mogare D., Boppana R., Paknikar K.M., Chattopadhyay S.
    J. Biol. Chem. 282:9902-9913(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-347, MUTAGENESIS OF SER-347; SER-348; SER-349 AND SER-350.
  11. "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-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiBANP_MOUSE
AccessioniPrimary (citable) accession number: Q8VBU8
Secondary accession number(s): O88973
, Q3U4R5, Q91YZ1, Q9ES51
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 21, 2007
Last sequence update: March 1, 2002
Last modified: May 11, 2016
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.