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Protein

Protein HEXIM2

Gene

Hexim2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

GO - Molecular functioni

  1. cyclin-dependent protein serine/threonine kinase inhibitor activity Source: MGI
  2. snRNA binding Source: MGI

GO - Biological processi

  1. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: MGI
  2. negative regulation of transcription, DNA-templated Source: MGI
  3. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein HEXIM2
Gene namesi
Name:Hexim2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1918309. Hexim2.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleoplasm Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 313313Protein HEXIM2PRO_0000305268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei75 – 751PhosphoserineBy similarity
Modified residuei80 – 801PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ3TVI4.
PRIDEiQ3TVI4.

PTM databases

PhosphoSiteiQ3TVI4.

Expressioni

Gene expression databases

BgeeiQ3TVI4.
CleanExiMM_HEXIM2.
ExpressionAtlasiQ3TVI4. baseline and differential.
GenevestigatoriQ3TVI4.

Interactioni

Subunit structurei

Homooligomer and heterooligomer with HEXIM1; 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 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ3TVI4. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ3TVI4.
SMRiQ3TVI4. Positions 186-275.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 1424Interaction with P-TEFbBy similarity
Regioni225 – 28662Interaction with CCNT1, HEXIM1 and HEXIM2By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili207 – 27670Sequence 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.
HOVERGENiHBG107976.
InParanoidiQ3TVI4.
KOiK15189.
OMAiPCRQVEE.
PhylomeDBiQ3TVI4.
TreeFamiTF336851.

Family and domain databases

InterProiIPR024872. HEXIM.
IPR024876. HEXIM2.
[Graphical view]
PANTHERiPTHR13469. PTHR13469. 1 hit.
PTHR13469:SF3. PTHR13469:SF3. 1 hit.
PfamiPF15313. HEXIM. 1 hit.
[Graphical view]
PRINTSiPR02094. HEXIMFAMILY.

Sequencei

Sequence statusi: Complete.

Q3TVI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVNHTNCN TASPAALEEA KTSGGLRSPQ IAHEPHDFGG SQLLPSGQEI
60 70 80 90 100
QSEDEGTVPA GDGSSCNIRG SRTQSPGGCS VEAVLARKKH RRRPSKRKRH
110 120 130 140 150
WRPYLELSWA EKQQRDERQS QRASRVREEM FAKGQPLAPY NTTQFLMNDR
160 170 180 190 200
DLEEPNLDVL HGPSHSGSGG ENEAGDSDGQ GRAHGEFQQR DFSEAYERYH
210 220 230 240 250
TESLQGRSKQ ELVRDYLDLE RRLSQAEQET RRLRQLQGCS SRQPCQQVEE
260 270 280 290 300
LAAEVERLRT ENQRLRQENE MWNREGGYCD QEKPASEGTP WPKVEAPFQT
310
HTGQLGHREA GDR
Length:313
Mass (Da):35,397
Last modified:October 11, 2005 - v1
Checksum:i37DC31F063D7C60A
GO

Sequence cautioni

The sequence BAB30344.1 differs from that shown. Reason: Frameshift at positions 93 and 99. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016624 mRNA. Translation: BAB30344.1. Frameshift.
AK140145 mRNA. Translation: BAE24255.1.
AK160110 mRNA. Translation: BAE35634.1.
AL662804, AL731805 Genomic DNA. Translation: CAM21575.1.
AL731805, AL662804 Genomic DNA. Translation: CAM22096.1.
BC026458 mRNA. Translation: AAH26458.1.
BC115597 mRNA. Translation: AAI15598.1.
BC115598 mRNA. Translation: AAI15599.1.
CCDSiCCDS25514.1.
RefSeqiNP_001123987.1. NM_001130515.1.
NP_001123988.1. NM_001130516.1.
NP_081934.1. NM_027658.2.
XP_006534291.1. XM_006534228.1.
XP_006534292.1. XM_006534229.1.
XP_006534293.1. XM_006534230.1.
XP_006534294.1. XM_006534231.1.
UniGeneiMm.273871.

Genome annotation databases

EnsembliENSMUST00000062530; ENSMUSP00000053678; ENSMUSG00000043372.
ENSMUST00000107037; ENSMUSP00000102652; ENSMUSG00000043372.
GeneIDi71059.
KEGGimmu:71059.
UCSCiuc007ltp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016624 mRNA. Translation: BAB30344.1. Frameshift.
AK140145 mRNA. Translation: BAE24255.1.
AK160110 mRNA. Translation: BAE35634.1.
AL662804, AL731805 Genomic DNA. Translation: CAM21575.1.
AL731805, AL662804 Genomic DNA. Translation: CAM22096.1.
BC026458 mRNA. Translation: AAH26458.1.
BC115597 mRNA. Translation: AAI15598.1.
BC115598 mRNA. Translation: AAI15599.1.
CCDSiCCDS25514.1.
RefSeqiNP_001123987.1. NM_001130515.1.
NP_001123988.1. NM_001130516.1.
NP_081934.1. NM_027658.2.
XP_006534291.1. XM_006534228.1.
XP_006534292.1. XM_006534229.1.
XP_006534293.1. XM_006534230.1.
XP_006534294.1. XM_006534231.1.
UniGeneiMm.273871.

3D structure databases

ProteinModelPortaliQ3TVI4.
SMRiQ3TVI4. Positions 186-275.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ3TVI4. 1 interaction.

PTM databases

PhosphoSiteiQ3TVI4.

Proteomic databases

MaxQBiQ3TVI4.
PRIDEiQ3TVI4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000062530; ENSMUSP00000053678; ENSMUSG00000043372.
ENSMUST00000107037; ENSMUSP00000102652; ENSMUSG00000043372.
GeneIDi71059.
KEGGimmu:71059.
UCSCiuc007ltp.2. mouse.

Organism-specific databases

CTDi124790.
MGIiMGI:1918309. Hexim2.

Phylogenomic databases

eggNOGiNOG72325.
GeneTreeiENSGT00390000002808.
HOGENOMiHOG000060338.
HOVERGENiHBG107976.
InParanoidiQ3TVI4.
KOiK15189.
OMAiPCRQVEE.
PhylomeDBiQ3TVI4.
TreeFamiTF336851.

Miscellaneous databases

NextBioi332919.
PROiQ3TVI4.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TVI4.
CleanExiMM_HEXIM2.
ExpressionAtlasiQ3TVI4. baseline and differential.
GenevestigatoriQ3TVI4.

Family and domain databases

InterProiIPR024872. HEXIM.
IPR024876. HEXIM2.
[Graphical view]
PANTHERiPTHR13469. PTHR13469. 1 hit.
PTHR13469:SF3. PTHR13469:SF3. 1 hit.
PfamiPF15313. HEXIM. 1 hit.
[Graphical view]
PRINTSiPR02094. HEXIMFAMILY.
ProtoNetiSearch...

Publicationsi

  1. "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: Corpora quadrigemina and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Tissue: Eye.

Entry informationi

Entry nameiHEXI2_MOUSE
AccessioniPrimary (citable) accession number: Q3TVI4
Secondary accession number(s): Q9D4C7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: October 11, 2005
Last modified: March 4, 2015
This is version 79 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.