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Protein

Proteasome activator complex subunit 4

Gene

PSME4

Organism
Homo sapiens (Human)
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.4 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, DNA damage, DNA repair, Spermatogenesis

Enzyme and pathway databases

ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome activator complex subunit 4
Alternative name(s):
Proteasome activator PA200
Gene namesi
Name:PSME4
Synonyms:KIAA0077
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:20635. PSME4.

Subcellular locationi

  • Cytoplasmcytosol By similarity
  • Nucleus 1 Publication
  • Nucleus speckle By similarity

  • Note: Found in nuclear foci following treatment with ionizing radiation, but not with ultraviolet irradiation or H2O2.

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1716 – 17172NF → TS: Abolihes binding to acetylated histones. 1 Publication

Organism-specific databases

PharmGKBiPA134872587.

Polymorphism and mutation databases

BioMutaiPSME4.
DMDMi134034993.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18431843Proteasome activator complex subunit 4PRO_0000280718Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1121 – 11211PhosphoserineCombined sources
Modified residuei1614 – 16141PhosphoserineCombined sources
Modified residuei1746 – 17461PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ14997.
MaxQBiQ14997.
PaxDbiQ14997.
PeptideAtlasiQ14997.
PRIDEiQ14997.

PTM databases

iPTMnetiQ14997.
PhosphoSiteiQ14997.

Expressioni

Gene expression databases

BgeeiENSG00000068878.
CleanExiHS_PSME4.
ExpressionAtlasiQ14997. baseline and differential.
GenevisibleiQ14997. HS.

Organism-specific databases

HPAiHPA060922.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CALCOCO2Q131373EBI-1236916,EBI-739580
NUTM1Q86Y263EBI-1236916,EBI-10178410

GO - Molecular functioni

Protein-protein interaction databases

BioGridi116807. 40 interactions.
DIPiDIP-38203N.
IntActiQ14997. 16 interactions.
MINTiMINT-4050711.
STRINGi9606.ENSP00000384211.

Structurei

3D structure databases

ProteinModelPortaliQ14997.
SMRiQ14997. Positions 1677-1843.
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)Add
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.
InParanoidiQ14997.
KOiK06699.
OMAiFEHISIG.
OrthoDBiEOG091G0DWV.
PhylomeDBiQ14997.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14997-1) [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
MEPAERAGVG EPPEPGGRPE PGPRGFVPQK EIVYNKLLPY AERLDAESDL
60 70 80 90 100
QLAQIKCNLG RAVQLQELWP GGLFWTRKLS TYIRLYGRKF SKEDHVLFIK
110 120 130 140 150
LLYELVSIPK LEISMMQGFA RLLINLLKKK ELLSRADLEL PWRPLYDMVE
160 170 180 190 200
RILYSKTEHL GLNWFPNSVE NILKTLVKSC RPYFPADATA EMLEEWRPLM
210 220 230 240 250
CPFDVTMQKA ITYFEIFLPT 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 ERYKKPSWLT PVPDSHKLTD QDVTDFVQCI
410 420 430 440 450
IQPVLLAMFS KTGSLEAAQA LQNLALMRPE LVIPPVLERT YPALETLTEP
460 470 480 490 500
HQLTATLSCV IGVARSLVSG GRWFPEGPTH MLPLLMRALP GVDPNDFSKC
510 520 530 540 550
MITFQFIATF STLVPLVDCS SVLQERNDLT EVERELCSAT AEFEDFVLQF
560 570 580 590 600
MDRCFGLIES STLEQTREET ETEKMTHLES LVELGLSSTF STILTQCSKE
610 620 630 640 650
IFMVALQKVF NFSTSHIFET RVAGRMVADM CRAAVKCCPE ESLKLFVPHC
660 670 680 690 700
CSVITQLTMN DDVLNDEELD KELLWNLQLL SEITRVDGRK LLLYREQLVK
710 720 730 740 750
ILQRTLHLTC KQGYTLSCNL LHHLLRSTTL IYPTEYCSVP GGFDKPPSEY
760 770 780 790 800
FPIKDWGKPG DLWNLGIQWH VPSSEEVSFA FYLLDSFLQP ELVKLQHCGD
810 820 830 840 850
GKLEMSRDDI LQSLTIVHNC LIGSGNLLPP LKGEPVTNLV PSMVSLEETK
860 870 880 890 900
LYTGLEYDLS RENHREVIAT VIRKLLNHIL DNSEDDTKSL FLIIKIIGDL
910 920 930 940 950
LQFQGSHKHE FDSRWKSFNL VKKSMENRLH GKKQHIRALL IDRVMLQHEL
960 970 980 990 1000
RTLTVEGCEY KKIHQDMIRD LLRLSTSSYS QVRNKAQQTF FAALGAYNFC
1010 1020 1030 1040 1050
CRDIIPLVLE FLRPDRQGVT QQQFKGALYC LLGNHSGVCL ANLHDWDCIV
1060 1070 1080 1090 1100
QTWPAIVSSG LSQAMSLEKP SIVRLFDDLA EKIHRQYETI GLDFTIPKSC
1110 1120 1130 1140 1150
VEIAELLQQS KNPSINQILL SPEKIKEGIK RQQEKNADAL RNYENLVDTL
1160 1170 1180 1190 1200
LDGVEQRNLP WKFEHIGIGL LSLLLRDDRV LPLRAIRFFV ENLNHDAIVV
1210 1220 1230 1240 1250
RKMAISAVAG ILKQLKRTHK KLTINPCEIS GCPKPTQIIA GDRPDNHWLH
1260 1270 1280 1290 1300
YDSKTIPRTK KEWESSCFVE KTHWGYYTWP KNMVVYAGVE EQPKLGRSRE
1310 1320 1330 1340 1350
DMTEAEQIIF DHFSDPKFVE QLITFLSLED RKGKDKFNPR RFCLFKGIFR
1360 1370 1380 1390 1400
NFDDAFLPVL KPHLEHLVAD SHESTQRCVA EIIAGLIRGS KHWTFEKVEK
1410 1420 1430 1440 1450
LWELLCPLLR TALSNITVET YNDWGACIAT SCESRDPRKL HWLFELLLES
1460 1470 1480 1490 1500
PLSGEGGSFV DACRLYVLQG GLAQQEWRVP ELLHRLLKYL EPKLTQVYKN
1510 1520 1530 1540 1550
VRERIGSVLT YIFMIDVSLP NTTPTISPHV PEFTARILEK LKPLMDVDEE
1560 1570 1580 1590 1600
IQNHVMEENG IGEEDERTQG IKLLKTILKW LMASAGRSFS TAVTEQLQLL
1610 1620 1630 1640 1650
PLFFKIAPVE NDNSYDELKR DAKLCLSLMS QGLLYPHQVP LVLQVLKQTA
1660 1670 1680 1690 1700
RSSSWHARYT VLTYLQTMVF YNLFIFLNNE DAVKDIRWLV ISLLEDEQLE
1710 1720 1730 1740 1750
VREMAATTLS GLLQCNFLTM DSPMQIHFEQ 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):211,334
Last modified:March 20, 2007 - v2
Checksum:i2D2C3A594E4FA4E7
GO
Isoform 2 (identifier: Q14997-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-625: Missing.

Show »
Length:1,218
Mass (Da):139,963
Checksum:i1ABE87B5DCED3915
GO
Isoform 3 (identifier: Q14997-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-856: Missing.
     857-871: YDLSRENHREVIATV → MGENLAKKIMFFLLI

Show »
Length:987
Mass (Da):113,757
Checksum:i38486C4A85C31995
GO
Isoform 4 (identifier: Q14997-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1628: Missing.

Note: No experimental confirmation available.
Show »
Length:215
Mass (Da):24,699
Checksum:i035FA5A26BF4457F
GO

Sequence cautioni

The sequence AAI12170 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI13669 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 2171F → V in AAX83871 (Ref. 1) Curated
Sequence conflicti710 – 7101C → R in AAX83871 (Ref. 1) Curated
Sequence conflicti984 – 9841N → S in AAX83871 (Ref. 1) Curated
Sequence conflicti1401 – 14011L → F in AAH43602 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti872 – 8721I → V.
Corresponds to variant rs2302878 [ dbSNP | Ensembl ].
VAR_031189
Natural varianti1371 – 13711S → T.
Corresponds to variant rs805408 [ dbSNP | Ensembl ].
VAR_031190
Natural varianti1825 – 18251T → A.
Corresponds to variant rs35903236 [ dbSNP | Ensembl ].
VAR_059755

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 16281628Missing in isoform 4. 1 PublicationVSP_023876Add
BLAST
Alternative sequencei1 – 856856Missing in isoform 3. 1 PublicationVSP_023877Add
BLAST
Alternative sequencei1 – 625625Missing in isoform 2. 1 PublicationVSP_023878Add
BLAST
Alternative sequencei857 – 87115YDLSR…VIATV → MGENLAKKIMFFLLI in isoform 3. 1 PublicationVSP_023879Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY894754 mRNA. Translation: AAX83869.1.
AY894755 mRNA. Translation: AAX83870.1.
AY894756 mRNA. Translation: AAX83871.1.
BC043602 mRNA. Translation: AAH43602.1.
BC071768 mRNA. Translation: AAH71768.1.
BC112169 mRNA. Translation: AAI12170.1. Different initiation.
BC113668 mRNA. Translation: AAI13669.1. Different initiation.
D38521 mRNA. Translation: BAA07526.1.
CCDSiCCDS33197.2. [Q14997-1]
RefSeqiNP_055429.2. NM_014614.2. [Q14997-1]
UniGeneiHs.413801.

Genome annotation databases

EnsembliENST00000404125; ENSP00000384211; ENSG00000068878. [Q14997-1]
GeneIDi23198.
KEGGihsa:23198.
UCSCiuc002rxp.2. human. [Q14997-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY894754 mRNA. Translation: AAX83869.1.
AY894755 mRNA. Translation: AAX83870.1.
AY894756 mRNA. Translation: AAX83871.1.
BC043602 mRNA. Translation: AAH43602.1.
BC071768 mRNA. Translation: AAH71768.1.
BC112169 mRNA. Translation: AAI12170.1. Different initiation.
BC113668 mRNA. Translation: AAI13669.1. Different initiation.
D38521 mRNA. Translation: BAA07526.1.
CCDSiCCDS33197.2. [Q14997-1]
RefSeqiNP_055429.2. NM_014614.2. [Q14997-1]
UniGeneiHs.413801.

3D structure databases

ProteinModelPortaliQ14997.
SMRiQ14997. Positions 1677-1843.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116807. 40 interactions.
DIPiDIP-38203N.
IntActiQ14997. 16 interactions.
MINTiMINT-4050711.
STRINGi9606.ENSP00000384211.

PTM databases

iPTMnetiQ14997.
PhosphoSiteiQ14997.

Polymorphism and mutation databases

BioMutaiPSME4.
DMDMi134034993.

Proteomic databases

EPDiQ14997.
MaxQBiQ14997.
PaxDbiQ14997.
PeptideAtlasiQ14997.
PRIDEiQ14997.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000404125; ENSP00000384211; ENSG00000068878. [Q14997-1]
GeneIDi23198.
KEGGihsa:23198.
UCSCiuc002rxp.2. human. [Q14997-1]

Organism-specific databases

CTDi23198.
GeneCardsiPSME4.
H-InvDBHIX0200268.
HGNCiHGNC:20635. PSME4.
HPAiHPA060922.
MIMi607705. gene.
neXtProtiNX_Q14997.
PharmGKBiPA134872587.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1851. Eukaryota.
ENOG410XP7J. LUCA.
GeneTreeiENSGT00390000011433.
HOVERGENiHBG082223.
InParanoidiQ14997.
KOiK06699.
OMAiFEHISIG.
OrthoDBiEOG091G0DWV.
PhylomeDBiQ14997.
TreeFamiTF106237.

Enzyme and pathway databases

ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPSME4. human.
GeneWikiiPSME4.
GenomeRNAii23198.
PROiQ14997.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000068878.
CleanExiHS_PSME4.
ExpressionAtlasiQ14997. baseline and differential.
GenevisibleiQ14997. HS.

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...

Entry informationi

Entry nameiPSME4_HUMAN
AccessioniPrimary (citable) accession number: Q14997
Secondary accession number(s): Q1XBG4
, Q1XBG5, Q1XBG6, Q2M1Z0, Q6IPR2, Q86XF8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: March 20, 2007
Last modified: September 7, 2016
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.