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Protein

Protein HEXIM1

Gene

Hexim1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional regulator which functions as a general RNA polymerase II transcription inhibitor. In cooperation with 7SK snRNA sequesters P-TEFb in a large inactive 7SK snRNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation. May also regulate NF-kappa-B, ESR1, NR3C1 and CIITA-dependent transcriptional activity (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein HEXIM1
Alternative name(s):
Cardiac lineage protein 1
Gene namesi
Name:Hexim1
Synonyms:Clp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2385923. Hexim1.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Binds alpha-importin and is mostly nuclear.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 356356Protein HEXIM1PRO_0000305264Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei98 – 981PhosphoserineBy similarity
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei233 – 2331PhosphothreonineBy similarity
Modified residuei234 – 2341PhosphoserineBy similarity
Modified residuei249 – 2491PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8R409.
PaxDbiQ8R409.
PRIDEiQ8R409.

PTM databases

PhosphoSiteiQ8R409.

Expressioni

Tissue specificityi

Widely expressed with higher expression in heart, skeletal muscle and brain (at protein level).1 Publication

Inductioni

Up-regulated by HMBA (hexamethylene bisacetamide).1 Publication

Gene expression databases

BgeeiQ8R409.
CleanExiMM_HEXIM1.
ExpressionAtlasiQ8R409. baseline and differential.
GenevisibleiQ8R409. MM.

Interactioni

Subunit structurei

Homooligomer and heterooligomer with HEXIM2; probably dimeric. Component of the 7SK snRNP complex at least composed of P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2, BCDIN3, SART3 proteins and 7SK and U6 snRNAs. Interacts with the N-CoR complex through NCOR1. Interacts with ESR1 and NR3C1. May interact with NF-kappa-B through RELA (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Srsf1Q6PDM24EBI-6261031,EBI-2550360
Srsf2Q620934EBI-6261031,EBI-2550402

Protein-protein interaction databases

IntActiQ8R409. 4 interactions.
MINTiMINT-4119070.
STRINGi10090.ENSMUSP00000057339.

Structurei

3D structure databases

ProteinModelPortaliQ8R409.
SMRiQ8R409. Positions 251-356.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni147 – 17428Basic region; mediates nuclear localization and interaction with 7SK snRNA and NR3C1By similarityAdd
BLAST
Regioni199 – 2024Interaction with P-TEFbBy similarity
Regioni207 – 24741Autoinhibitory acidic region; in absence of 7SK snRNA interacts with the basic region preventing interaction with P-TEFb and modulating subcellular localizationBy similarityAdd
BLAST
Regioni283 – 31129Mediates interaction with CCNT1By similarityAdd
BLAST
Regioni307 – 35246Required for inhibition of ESR1-dependent transcriptionBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili280 – 34667Sequence AnalysisAdd
BLAST

Domaini

The coiled-coil domain mediates oligomerization.By similarity

Sequence similaritiesi

Belongs to the HEXIM family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG72325.
GeneTreeiENSGT00390000002808.
HOGENOMiHOG000060338.
HOVERGENiHBG053249.
InParanoidiQ8R409.
KOiK15189.
OMAiEDSRWQS.
OrthoDBiEOG771281.
PhylomeDBiQ8R409.
TreeFamiTF336851.

Family and domain databases

InterProiIPR024872. HEXIM.
[Graphical view]
PANTHERiPTHR13469. PTHR13469. 1 hit.
PfamiPF15313. HEXIM. 1 hit.
[Graphical view]
PRINTSiPR02094. HEXIMFAMILY.

Sequencei

Sequence statusi: Complete.

Q8R409-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPLLTEHQ HQPQTSNCTG AAVVHEEHTS ERPPSAEERV PKEDSRWQSR
60 70 80 90 100
ASLQSGSRPG QEGEGGLKHQ LPPLQTNACP ELSSLEKGEK GQNGEDLSTG
110 120 130 140 150
GASPSAEGEP MSESLVQPGH DSEATKQEAP AAGGEEPWGQ QQRQLGKKKH
160 170 180 190 200
RRRPSKKKRH WKPYYKLTWE EKKKFDEKQS LRASRVRAEM FAKGQPVAPY
210 220 230 240 250
NTTQFLMDDH DQEEPDLKTG LYPKRAAAKS DDTSDEDFVE EAGEEDGGSD
260 270 280 290 300
GMGGDGSEFL QRDFSETYER YHAESLQNMS KQELIKEYLE LEKCLSRKED
310 320 330 340 350
ENNRLRLESK RLGGVDARVR ELELELDRLR AENLQLLTEN ELHRQQERAP

LSKFGD
Length:356
Mass (Da):40,243
Last modified:June 1, 2002 - v1
Checksum:i242DE7EE66BA293B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY090614 mRNA. Translation: AAM09026.1.
AK134535 mRNA. Translation: BAE22173.1.
AL731805 Genomic DNA. Translation: CAM22092.1.
CCDSiCCDS25513.1.
RefSeqiNP_620092.1. NM_138753.2.
UniGeneiMm.8763.

Genome annotation databases

EnsembliENSMUST00000053063; ENSMUSP00000057339; ENSMUSG00000048878.
GeneIDi192231.
KEGGimmu:192231.
UCSCiuc007lto.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY090614 mRNA. Translation: AAM09026.1.
AK134535 mRNA. Translation: BAE22173.1.
AL731805 Genomic DNA. Translation: CAM22092.1.
CCDSiCCDS25513.1.
RefSeqiNP_620092.1. NM_138753.2.
UniGeneiMm.8763.

3D structure databases

ProteinModelPortaliQ8R409.
SMRiQ8R409. Positions 251-356.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R409. 4 interactions.
MINTiMINT-4119070.
STRINGi10090.ENSMUSP00000057339.

PTM databases

PhosphoSiteiQ8R409.

Proteomic databases

MaxQBiQ8R409.
PaxDbiQ8R409.
PRIDEiQ8R409.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053063; ENSMUSP00000057339; ENSMUSG00000048878.
GeneIDi192231.
KEGGimmu:192231.
UCSCiuc007lto.1. mouse.

Organism-specific databases

CTDi10614.
MGIiMGI:2385923. Hexim1.

Phylogenomic databases

eggNOGiNOG72325.
GeneTreeiENSGT00390000002808.
HOGENOMiHOG000060338.
HOVERGENiHBG053249.
InParanoidiQ8R409.
KOiK15189.
OMAiEDSRWQS.
OrthoDBiEOG771281.
PhylomeDBiQ8R409.
TreeFamiTF336851.

Miscellaneous databases

ChiTaRSiHexim1. mouse.
NextBioi371270.
PROiQ8R409.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R409.
CleanExiMM_HEXIM1.
ExpressionAtlasiQ8R409. baseline and differential.
GenevisibleiQ8R409. MM.

Family and domain databases

InterProiIPR024872. HEXIM.
[Graphical view]
PANTHERiPTHR13469. PTHR13469. 1 hit.
PfamiPF15313. HEXIM. 1 hit.
[Graphical view]
PRINTSiPR02094. HEXIMFAMILY.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structure, expression, and functional characterization of the mouse CLP-1 gene."
    Huang F., Wagner M., Siddiqui M.A.Q.
    Gene 292:245-259(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: 129/SvJ.
    Tissue: Embryonic heart.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Medulla oblongata.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiHEXI1_MOUSE
AccessioniPrimary (citable) accession number: Q8R409
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: June 1, 2002
Last modified: June 24, 2015
This is version 95 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

External Data

Dasty 3

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 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.