Q8R409 (HEXI1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein HEXIM1

Alternative name(s):
Cardiac lineage protein 1

Gene names

Name:	Hexim1
Synonyms:	Clp1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	356 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subunit structure	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.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Note: Binds alpha-importin and is mostly nuclear By similarity.
Tissue specificity	Widely expressed with higher expression in heart, skeletal muscle and brain (at protein level). Ref.1
Induction	Up-regulated by HMBA (hexamethylene bisacetamide). Ref.1
Domain	The coiled-coil domain mediates oligomerization By similarity.
Sequence similarities	Belongs to the HEXIM family.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Coiled coil
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	heart development Inferred from mutant phenotype PubMed 15172687. Source: MGI negative regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	cyclin-dependent protein serine/threonine kinase inhibitor activity Inferred from sequence or structural similarity. Source: UniProtKB snRNA binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 356	356	Protein HEXIM1		PRO_0000305264
Regions
	Region	147 – 174	28	Basic region; mediates nuclear localization and interaction with 7SK snRNA and NR3C1 By similarity
	Region	199 – 202	4	Interaction with P-TEFb By similarity
	Region	207 – 247	41	Autoinhibitory acidic region; in absence of 7SK snRNA interacts with the basic region preventing interaction with P-TEFb and modulating subcellular localization By similarity
	Region	283 – 311	29	Mediates interaction with CCNT1 By similarity
	Region	307 – 352	46	Required for inhibition of ESR1-dependent transcription By similarity
	Coiled coil	280 – 346	67	Potential
Amino acid modifications
	Modified residue	98	1	Phosphoserine By similarity
	Modified residue	230	1	Phosphoserine By similarity
	Modified residue	233	1	Phosphothreonine By similarity
	Modified residue	234	1	Phosphoserine By similarity
	Modified residue	249	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8R409 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 242DE7EE66BA293B	FASTA	356	40,243
	10 20 30 40 50 60 MAEPLLTEHQ HQPQTSNCTG AAVVHEEHTS ERPPSAEERV PKEDSRWQSR ASLQSGSRPG 70 80 90 100 110 120 QEGEGGLKHQ LPPLQTNACP ELSSLEKGEK GQNGEDLSTG GASPSAEGEP MSESLVQPGH 130 140 150 160 170 180 DSEATKQEAP AAGGEEPWGQ QQRQLGKKKH RRRPSKKKRH WKPYYKLTWE EKKKFDEKQS 190 200 210 220 230 240 LRASRVRAEM FAKGQPVAPY NTTQFLMDDH DQEEPDLKTG LYPKRAAAKS DDTSDEDFVE 250 260 270 280 290 300 EAGEEDGGSD GMGGDGSEFL QRDFSETYER YHAESLQNMS KQELIKEYLE LEKCLSRKED 310 320 330 340 350 ENNRLRLESK RLGGVDARVR ELELELDRLR AENLQLLTEN ELHRQQERAP LSKFGD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY090614 mRNA. Translation: AAM09026.1. AK134535 mRNA. Translation: BAE22173.1. AL731805 Genomic DNA. Translation: CAM22092.1.
IPI	IPI00153798.
RefSeq	NP_620092.1. NM_138753.2.
UniGene	Mm.489620.
3D structure databases
ProteinModelPortal	Q8R409.
SMR	Q8R409. Positions 251-356.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8R409. 1 interaction.
STRING	10090.ENSMUSP00000057339.
PTM databases
PhosphoSite	Q8R409.
Proteomic databases
PaxDb	Q8R409.
PRIDE	Q8R409.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000053063; ENSMUSP00000057339; ENSMUSG00000048878.
GeneID	192231.
KEGG	mmu:192231.
UCSC	uc007lto.1. mouse.
Organism-specific databases
CTD	10614.
MGI	MGI:2385923. Hexim1.
Phylogenomic databases
eggNOG	NOG72325.
GeneTree	ENSGT00390000002808.
HOGENOM	HOG000060338.
HOVERGEN	HBG053249.
InParanoid	Q8R409.
KO	K15189.
OMA	EDSRWQS.
OrthoDB	EOG40GCRK.
Gene expression databases
ArrayExpress	Q8R409.
Bgee	Q8R409.
CleanEx	MM_HEXIM1.
Genevestigator	Q8R409.
Family and domain databases
InterPro	IPR024872. HEXIM. [Graphical view]
PANTHER	PTHR13469. PTHR13469. 1 hit.
PRINTS	PR02094. HEXIMFAMILY.
ProtoNet	Search...
Other
ChiTaRS	HEXIM1. mouse.
NextBio	371270.
SOURCE	Search...

Entry information

Entry name

HEXI1_MOUSE

Accession

Primary (citable) accession number: Q8R409

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 2, 2007
Last sequence update:	June 1, 2002
Last modified:	May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program