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Q96MH2 (HEXI2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein HEXIM2
Alternative name(s):
Hexamethylene bis-acetamide-inducible protein 2
Gene names
Name:HEXIM2
ORF Names:L3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence 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. Ref.5 Ref.6

Subunit structure

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. Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus Ref.7.

Tissue specificity

Ubiquitously expressed with higher expression in testis. HEXIM1 and HEXIM2 are differentially expressed. Ref.6

Induction

Up-regulated by HMBA (hexamethylene bisacetamide) (at protein level). Ref.6

Domain

The coiled-coil domain mediates oligomerization.

Sequence similarities

Belongs to the HEXIM family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Protein HEXIM2
PRO_0000305267

Regions

Region140 – 1434Interaction with P-TEFb
Region226 – 28661Interaction with CCNT1, HEXIM1 and HEXIM2
Coiled coil207 – 27771 Potential

Amino acid modifications

Modified residue291Phosphoserine Ref.9
Modified residue321Phosphothreonine Ref.9
Modified residue461Phosphothreonine Ref.8 Ref.9
Modified residue511Phosphoserine Ref.9 Ref.12 Ref.13
Modified residue531Phosphoserine Ref.9 Ref.12 Ref.13
Modified residue711Phosphoserine Ref.9
Modified residue761Phosphoserine Ref.9
Modified residue811Phosphoserine Ref.9

Experimental info

Mutagenesis1431T → A: Loss of interaction with P-TEFb. Ref.5
Mutagenesis1431T → D: Loss of interaction with P-TEFb. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q96MH2 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 58576D72096A8A6F

FASTA28632,419
        10         20         30         40         50         60 
MMATPNQTAC NAESPVALEE AKTSGAPGSP QTPPERHDSG GSLPLTPRME SHSEDEDLAG 

        70         80         90        100        110        120 
AVGGLGWNSR SPRTQSPGGC SAEAVLARKK HRRRPSKRKR HWRPYLELSW AEKQQRDERQ 

       130        140        150        160        170        180 
SQRASRVREE MFAKGQPVAP YNTTQFLMND RDPEEPNLDV PHGISHPGSS GESEAGDSDG 

       190        200        210        220        230        240 
RGRAHGEFQR KDFSETYERF HTESLQGRSK QELVRDYLEL EKRLSQAEEE TRRLQQLQAC 

       250        260        270        280 
TGQQSCRQVE ELAAEVQRLR TENQRLRQEN QMWNREGCRC DEEPGT 

« Hide

References

« Hide 'large scale' references
[1]"Suppression subtractive hybridization and expression profiling identifies a unique set of genes overexpressed in non-small-cell lung cancer."
Petroziello J., Yamane A., Westendorf L., Thompson M., McDonagh C., Cerveny C., Law C.-L., Wahl A., Carter P.
Oncogene 23:7734-7745(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Eye, Prostate and Uterus.
[5]"HEXIM2, a HEXIM1-related protein, regulates positive transcription elongation factor b through association with 7SK."
Byers S.A., Price J.P., Cooper J.J., Li Q., Price D.H.
J. Biol. Chem. 280:16360-16367(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, MUTAGENESIS OF THR-143.
[6]"Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the balance of active and inactive positive transcription elongation factor b complexes for control of transcription."
Yik J.H.N., Chen R., Pezda A.C., Zhou Q.
J. Biol. Chem. 280:16368-16376(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE 7SK SNRNP COMPLEX, INTERACTION WITH HEXIM1, OLIGOMERIZATION, TISSUE SPECIFICITY, INDUCTION.
[7]"Transcription-dependent association of multiple positive transcription elongation factor units to a HEXIM multimer."
Dulac C., Michels A.A., Fraldi A., Bonnet F., Nguyen V.T., Napolitano G., Lania L., Bensaude O.
J. Biol. Chem. 280:30619-30629(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: OLIGOMERIZATION, INTERACTION WITH CCNT1, SUBCELLULAR LOCATION.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; THR-32; THR-46; SER-51; SER-53; SER-71; SER-76 AND SER-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY598322 mRNA. Translation: AAT06733.1.
AK056946 mRNA. Translation: BAB71319.1.
CH471178 Genomic DNA. Translation: EAW51541.1.
CH471178 Genomic DNA. Translation: EAW51542.1.
BC003531 mRNA. Translation: AAH03531.1.
BC012474 mRNA. Translation: AAH12474.1.
BC025970 mRNA. Translation: AAH25970.1.
CCDSCCDS11496.1.
RefSeqNP_653209.1. NM_144608.1.
XP_005257095.1. XM_005257038.2.
XP_005257096.1. XM_005257039.2.
XP_005257097.1. XM_005257040.2.
XP_005257098.1. XM_005257041.2.
XP_006721751.1. XM_006721688.1.
XP_006721752.1. XM_006721689.1.
UniGeneHs.56382.

3D structure databases

ProteinModelPortalQ96MH2.
SMRQ96MH2. Positions 187-276.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125888. 7 interactions.
IntActQ96MH2. 3 interactions.
STRING9606.ENSP00000302276.

PTM databases

PhosphoSiteQ96MH2.

Polymorphism databases

DMDM74732374.

Proteomic databases

MaxQBQ96MH2.
PaxDbQ96MH2.
PRIDEQ96MH2.

Protocols and materials databases

DNASU124790.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307275; ENSP00000302276; ENSG00000168517.
ENST00000591576; ENSP00000465727; ENSG00000168517.
ENST00000592695; ENSP00000467517; ENSG00000168517.
GeneID124790.
KEGGhsa:124790.
UCSCuc002iih.1. human.

Organism-specific databases

CTD124790.
GeneCardsGC17P043238.
HGNCHGNC:28591. HEXIM2.
HPAHPA023323.
HPA028455.
neXtProtNX_Q96MH2.
PharmGKBPA142671695.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG72325.
HOGENOMHOG000060338.
HOVERGENHBG107976.
InParanoidQ96MH2.
KOK15189.
OMAPCRQVEE.
OrthoDBEOG771281.
PhylomeDBQ96MH2.
TreeFamTF336851.

Gene expression databases

ArrayExpressQ96MH2.
BgeeQ96MH2.
CleanExHS_HEXIM2.
GenevestigatorQ96MH2.

Family and domain databases

InterProIPR024872. HEXIM.
IPR024876. HEXIM2.
[Graphical view]
PANTHERPTHR13469. PTHR13469. 1 hit.
PTHR13469:SF3. PTHR13469:SF3. 1 hit.
PfamPF15313. HEXIM. 1 hit.
[Graphical view]
PRINTSPR02094. HEXIMFAMILY.
ProtoNetSearch...

Other

GeneWikiHEXIM2.
GenomeRNAi124790.
NextBio81380.
PROQ96MH2.

Entry information

Entry nameHEXI2_HUMAN
AccessionPrimary (citable) accession number: Q96MH2
Secondary accession number(s): D3DX66
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM