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Protein

Proteasome activator complex subunit 4

Gene

Psme4

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

Functioni

Associated component of the proteasome that specifically recognizes acetylated histones and promotes ATP- and ubiquitin-independent degradation of core histones during spermatogenesis and DNA damage response. Recognizes and binds acetylated histones via its bromodomain-like (BRDL) region and activates the proteasome by opening the gated channel for substrate entry. Binds to the core proteasome via its C-terminus, which occupies the same binding sites as the proteasomal ATPases, opening the closed structure of the proteasome via an active gating mechanism. Component of the spermatoproteasome, a form of the proteasome specifically found in testis: binds to acetylated histones and promotes degradation of histones, thereby participating actively to the exchange of histones during spermatogenesis. Also involved in DNA damage response in somatic cells, by promoting degradation of histones following DNA double-strand breaks.2 Publications

GO - Molecular functioni

  • lysine-acetylated histone binding Source: UniProtKB
  • peptidase activator activity Source: UniProtKB

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA repair Source: UniProtKB
  • multicellular organism development Source: UniProtKB-KW
  • positive regulation of peptidase activity Source: GOC
  • proteasomal ubiquitin-independent protein catabolic process Source: UniProtKB
  • spermatogenesis, exchange of chromosomal proteins Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, DNA damage, DNA repair, Spermatogenesis

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome activator complex subunit 4
Alternative name(s):
Proteasome activator PA200
Protein TEMO
Gene namesi
Name:Psme4
Synonyms:Kiaa0077
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2143994. Psme4.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • spermatoproteasome complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Disruption phenotypei

Mice are viable and show no obvious developmental abnormalities. They have reduced male fertility due to defects in spermatogenesis in meiotic spermatocytes and during the maturation of postmeiotic haploid spermatids. Testes are defective in core histone replacement.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18431843Proteasome activator complex subunit 4PRO_0000280719Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1121 – 11211PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5SSW2.
MaxQBiQ5SSW2.
PaxDbiQ5SSW2.
PRIDEiQ5SSW2.

PTM databases

iPTMnetiQ5SSW2.
PhosphoSiteiQ5SSW2.
SwissPalmiQ5SSW2.

Expressioni

Tissue specificityi

Broadly expressed. Present in heart (at protein level).2 Publications

Gene expression databases

BgeeiQ5SSW2.
ExpressionAtlasiQ5SSW2. baseline and differential.
GenevisibleiQ5SSW2. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with the 20S and 26S proteasomes. Component of the spermatoproteasome, a form of the proteasome specifically found in testis.1 Publication

GO - Molecular functioni

  • lysine-acetylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi222113. 1 interaction.
IntActiQ5SSW2. 5 interactions.
MINTiMINT-4606985.
STRINGi10090.ENSMUSP00000045460.

Structurei

3D structure databases

ProteinModelPortaliQ5SSW2.
SMRiQ5SSW2. Positions 1381-1843.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati475 – 51945HEAT 1Add
BLAST
Repeati998 – 103740HEAT 2Add
BLAST
Repeati1179 – 121739HEAT 3Add
BLAST
Repeati1354 – 139239HEAT 4Add
BLAST
Repeati1636 – 167439HEAT 5Add
BLAST
Repeati1680 – 171839HEAT 6Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1650 – 173889Bromodomain-like (BRDL)By similarityAdd
BLAST

Domaini

The bromodomain-like (BRDL) region specifically recognizes and binds acetylated histones.1 Publication

Sequence similaritiesi

Belongs to the BLM10 family.Curated
Contains 6 HEAT repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1851. Eukaryota.
ENOG410XP7J. LUCA.
GeneTreeiENSGT00390000011433.
HOVERGENiHBG082223.
InParanoidiQ5SSW2.
KOiK06699.
OMAiQHCGDGK.
OrthoDBiEOG7R830P.
PhylomeDBiQ5SSW2.
TreeFamiTF106237.

Family and domain databases

Gene3Di1.25.10.10. 7 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR032430. Blm10_mid.
IPR021843. DUF3437.
[Graphical view]
PfamiPF16507. BLM10_mid. 1 hit.
PF11919. DUF3437. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 8 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5SSW2-1) [UniParc]FASTAAdd to basket

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
MEAPERAGGG EPPEPGGRPV LGPRAFVPQK EIVYNKLLPY AERLDAESDL
60 70 80 90 100
QLAQIKSNLG RAVQLQELWP GGLFWTRKLS TYIRLYGRKF SKEDHVLFIK
110 120 130 140 150
LLYELVSIPK LEISMMQGFA RLLINLLKKK ELLSRDDLEL PWRPLYDLVE
160 170 180 190 200
RILYSKTEHL RLNSFPNSIE NVLKTLVKSC RPYFPADSTA EMLEEWRPLM
210 220 230 240 250
CPFDVTMQKA ISYFEIFLPT SLPPELHHKG FKLWFDELIG LWVSVQNLPQ
260 270 280 290 300
WEGQLVNLFA RLATDNIGYI DWDPYVPKIF TRILRSLNLP VGSSQVLVPR
310 320 330 340 350
FLTNAYDIGH AVIWITAMMG GPSKLVQKHL AGLFNSITSF YHPSNNGRWL
360 370 380 390 400
NKLMKLLQRL PNSVVRRLHR ERFKKPSWLT PVPESHKLTD EDVTDFVQCI
410 420 430 440 450
IQPVLLAMFS KTGSLEAAQA LQNLALMRPE LVIPPVLERT YPALETLTEP
460 470 480 490 500
HQLTATLNCV IGVARSLVSG SKWFPEGPTH MLPLLMRALP GVDPNDFSKC
510 520 530 540 550
MITFQFIGTF STLVPLVDCS SVLQERNDLT EIEKELCSAT AEFEDFVLQF
560 570 580 590 600
MDRCFGLIES STLEQTREET ETEKMTHLES LVELGLSSTF STILTQCSKD
610 620 630 640 650
IFMVALQKVF NFSVSHIFET RVAGRMVADM CRAAVKCCPE ESLKLFVPHC
660 670 680 690 700
YGVITQLTMN DDVLNEEELD KELLWNLQLL SEITRVDGKK LLLYREQLVK
710 720 730 740 750
ILQRTLHLTC KQGYTLSCNL LHHLLRSTTL IYPTEYCSVP GGFNKPPSEY
760 770 780 790 800
FPVKDWGKPG DLWNLGIQWH VPSSEEVSFA FYLLDSFLQP ELIKLQCCGD
810 820 830 840 850
GELEMSRDDI LQSLTIVHSC LIGSGNLLPP LKGEAVTNLV PSMVSLEETK
860 870 880 890 900
LYTGLEHDLS RENYREVIAS VIRKLLSHIL DNSEDDTKSL FLIIKIIGDL
910 920 930 940 950
LHFQGSHKHE FDSRWKSFNL VKKSMENRLH GKKQHIRALL IDRVMLQHEL
960 970 980 990 1000
RTLTVEGCEY KKIHQDMIRD LLRLSTSSYS QVRNKAQQTF FAALGAYNFC
1010 1020 1030 1040 1050
CRDIIPLVLE FLRPDRKDVT QQQFKGALYC LLGNHSGVCL ANLHDWDCIV
1060 1070 1080 1090 1100
QTWPALVSSG LSQAMSLEKP SIVRLFDDLA EKIHRQYETI GLDFTIPKSC
1110 1120 1130 1140 1150
AAIAELLQQS KNPSISQTLL SPEKIKEGQK RQQDKNADAL RNYECLVNTL
1160 1170 1180 1190 1200
LDGVEQRNLP WKFEHIGIGL LSLLLRDDRV LPLRAIRFFV ENLNHDAIVV
1210 1220 1230 1240 1250
RKMAISAVAG ILKQLKRTHK KLTINPYEIS GCPKPTKILA GDRPDNHWLH
1260 1270 1280 1290 1300
YDSKNIPRTK KEWESSCFVE KTHWGYYNWP KNMVVYAGVE EQPKLGRSRE
1310 1320 1330 1340 1350
DMIEAEQIIY DRFSDPKFVE QLITFLSLED RKGRDKFSPR RFCLFKGIFR
1360 1370 1380 1390 1400
NFDDAFLPVL KPHLERLVAD SHESTQRCVA EIIAGLIRGS KHWTFEKVEK
1410 1420 1430 1440 1450
LWELLCPLLR TALSNMTVET YNDWGTCIAT SCESRDPRKL HWLFELLLES
1460 1470 1480 1490 1500
PLSGEGGSFV DACRLYVLQG GLAQQEWRVP ELLHRLLKYL EPKLTQVYKN
1510 1520 1530 1540 1550
VRERIGSVLT YIFMIDVSLP NTAPTTSPCI PEFTARVLEK LKPLTDVDEE
1560 1570 1580 1590 1600
IQNHVMEENG IGEEDERTQG IKLLKTILKW LMASAGRSFS TAVKEQLQLL
1610 1620 1630 1640 1650
PLFFKIAPVE NDNSYDELKR DAKLCLSLMS QGLLYPQQVP LILQVLSQTA
1660 1670 1680 1690 1700
RSSSWHARYT VLTYLQTMVF YNLFIFLNNE DAVKDIRWLI ICLLEDEQLE
1710 1720 1730 1740 1750
VREMAATTLS GLLQCNFLTM DSAMQIHFEQ LCKTKLPKKR KRDPGSVGDT
1760 1770 1780 1790 1800
IPSAELVKRH AGVLGLGACV LSSPYDVPTW MPQLLMNLSA HLNDPQPIEM
1810 1820 1830 1840
TVKKTLSNFR RTHHDNWQEH KQQFTDDQLL VLTDLLVSPC YYA
Length:1,843
Mass (Da):211,197
Last modified:December 21, 2004 - v1
Checksum:i326FD7B3A070C502
GO
Isoform 2 (identifier: Q5SSW2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1703: Missing.

Note: No experimental confirmation available.
Show »
Length:140
Mass (Da):15,778
Checksum:i51711972B0FBF2CF
GO

Sequence cautioni

The sequence AAG09060.1 differs from that shown. Reason: Frameshift at position 43. Curated
The sequence BAC97859.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521L → Q in AAG09060 (Ref. 3) Curated
Sequence conflicti316 – 3161T → A in AAG09060 (Ref. 3) Curated
Sequence conflicti392 – 3921D → V in AAG09060 (Ref. 3) Curated
Sequence conflicti433 – 4331I → V in AAG09060 (Ref. 3) Curated
Sequence conflicti470 – 4701G → R in AAG09060 (Ref. 3) Curated
Sequence conflicti478 – 4781P → L in AAG09060 (Ref. 3) Curated
Sequence conflicti482 – 4821L → P in AAG09060 (Ref. 3) Curated
Sequence conflicti542 – 5421E → G in AAG09060 (Ref. 3) Curated
Sequence conflicti622 – 6221V → A in AAG09060 (Ref. 3) Curated
Sequence conflicti651 – 6511Y → C in AAG09060 (Ref. 3) Curated
Sequence conflicti651 – 6511Y → C in AAI41382 (PubMed:15489334).Curated
Sequence conflicti1163 – 11631F → S in AAG09060 (Ref. 3) Curated
Sequence conflicti1181 – 11811L → S in AAG09060 (Ref. 3) Curated
Sequence conflicti1234 – 12341K → R in AAG09060 (Ref. 3) Curated
Sequence conflicti1234 – 12341K → R in AAH31174 (PubMed:15489334).Curated
Sequence conflicti1234 – 12341K → R in AAI41382 (PubMed:15489334).Curated
Sequence conflicti1238 – 12381I → V in AAG09060 (Ref. 3) Curated
Sequence conflicti1238 – 12381I → V in AAH31174 (PubMed:15489334).Curated
Sequence conflicti1238 – 12381I → V in AAI41382 (PubMed:15489334).Curated
Sequence conflicti1342 – 13421F → S in AAG09060 (Ref. 3) Curated
Sequence conflicti1404 – 14041L → V in AAG09060 (Ref. 3) Curated
Sequence conflicti1404 – 14041L → V in AAH31174 (PubMed:15489334).Curated
Sequence conflicti1404 – 14041L → V in AAI41382 (PubMed:15489334).Curated
Sequence conflicti1545 – 15451T → P in AAG09060 (Ref. 3) Curated
Sequence conflicti1782 – 17821P → S in AAG09060 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 17031703Missing in isoform 2. 1 PublicationVSP_023880Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129049 mRNA. Translation: BAC97859.1. Different initiation.
AL662891 Genomic DNA. Translation: CAI24530.1.
AF296169 mRNA. Translation: AAG09060.1. Frameshift.
BC004575 mRNA. Translation: AAH04575.1.
BC031174 mRNA. Translation: AAH31174.1.
BC054364 mRNA. Translation: AAH54364.1.
BC141381 mRNA. Translation: AAI41382.1.
AK131932 mRNA. Translation: BAE20881.1.
AK169447 mRNA. Translation: BAE41181.1.
CCDSiCCDS36124.1. [Q5SSW2-1]
RefSeqiNP_598774.2. NM_134013.3. [Q5SSW2-1]
UniGeneiMm.240066.

Genome annotation databases

EnsembliENSMUST00000041231; ENSMUSP00000045460; ENSMUSG00000040850. [Q5SSW2-1]
GeneIDi103554.
KEGGimmu:103554.
UCSCiuc007ihx.1. mouse. [Q5SSW2-1]
uc007iia.1. mouse. [Q5SSW2-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK129049 mRNA. Translation: BAC97859.1. Different initiation.
AL662891 Genomic DNA. Translation: CAI24530.1.
AF296169 mRNA. Translation: AAG09060.1. Frameshift.
BC004575 mRNA. Translation: AAH04575.1.
BC031174 mRNA. Translation: AAH31174.1.
BC054364 mRNA. Translation: AAH54364.1.
BC141381 mRNA. Translation: AAI41382.1.
AK131932 mRNA. Translation: BAE20881.1.
AK169447 mRNA. Translation: BAE41181.1.
CCDSiCCDS36124.1. [Q5SSW2-1]
RefSeqiNP_598774.2. NM_134013.3. [Q5SSW2-1]
UniGeneiMm.240066.

3D structure databases

ProteinModelPortaliQ5SSW2.
SMRiQ5SSW2. Positions 1381-1843.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222113. 1 interaction.
IntActiQ5SSW2. 5 interactions.
MINTiMINT-4606985.
STRINGi10090.ENSMUSP00000045460.

PTM databases

iPTMnetiQ5SSW2.
PhosphoSiteiQ5SSW2.
SwissPalmiQ5SSW2.

Proteomic databases

EPDiQ5SSW2.
MaxQBiQ5SSW2.
PaxDbiQ5SSW2.
PRIDEiQ5SSW2.

Protocols and materials databases

DNASUi103554.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041231; ENSMUSP00000045460; ENSMUSG00000040850. [Q5SSW2-1]
GeneIDi103554.
KEGGimmu:103554.
UCSCiuc007ihx.1. mouse. [Q5SSW2-1]
uc007iia.1. mouse. [Q5SSW2-2]

Organism-specific databases

CTDi23198.
MGIiMGI:2143994. Psme4.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1851. Eukaryota.
ENOG410XP7J. LUCA.
GeneTreeiENSGT00390000011433.
HOVERGENiHBG082223.
InParanoidiQ5SSW2.
KOiK06699.
OMAiQHCGDGK.
OrthoDBiEOG7R830P.
PhylomeDBiQ5SSW2.
TreeFamiTF106237.

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPsme4. mouse.
NextBioi35548198.
PROiQ5SSW2.
SOURCEiSearch...

Gene expression databases

BgeeiQ5SSW2.
ExpressionAtlasiQ5SSW2. baseline and differential.
GenevisibleiQ5SSW2. MM.

Family and domain databases

Gene3Di1.25.10.10. 7 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR032430. Blm10_mid.
IPR021843. DUF3437.
[Graphical view]
PfamiPF16507. BLM10_mid. 1 hit.
PF11919. DUF3437. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 8 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "TEMO is a marker to study sertoli-germ cell interactions: cloning and regulation of a novel testicular molecule."
    Mruk D., Mo M.-Y., Cheng C.Y.
    Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 28-1843 (ISOFORM 1).
  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] OF 28-1843 (ISOFORM 1).
    Strain: Czech II and FVB/N.
    Tissue: Brain, Colon and Mammary tumor.
  5. "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] OF 1399-1843 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Thymus.
  6. "PA200, a nuclear proteasome activator involved in DNA repair."
    Ustrell V., Hoffman L., Pratt G., Rechsteiner M.
    EMBO J. 21:3516-3525(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  7. Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  8. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. Cited for: FUNCTION, IDENTIFICATION IN THE SPERMATOPROTEASOME, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiPSME4_MOUSE
AccessioniPrimary (citable) accession number: Q5SSW2
Secondary accession number(s): C4IXU5
, Q3TER7, Q3V2B7, Q6ZQJ7, Q7TMY9, Q8K0K0, Q99KM2, Q9ESY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: December 21, 2004
Last modified: May 11, 2016
This is version 101 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.