wanglab/gogpt-training-data huggingface dataset:
Protein: Schlafen family member 13 (EC 3.1.-.-) (Schlafen-13) (hSLFN13) (Q68D06)
Organism: Homo sapiens (Human)
Function: Endoribonuclease that cleaves tRNAs and rRNAs. Cleaves tRNAs 11 nucleotides from the 3'-terminus at the acceptor stem. Does not act on tRNA(Sec). Able to restrict HIV-1 virus replication; ability to inhibit HIV-1 replication is dependent on endoribonuclease activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29563550}.
Interaction partners:
- Protein eva-1 homolog B
Sequence:
MEANHCSLGVYPSYPDLVIDVGEVTLGEENRKKLQKTQRDQERARVIRAACALLNSGGGVIQMEMANRDERPTEMGLDLEESLRKLIQYPYLQAFFETKQHGRCFYIFVKSWSGDPFLKDGSFNSRICSLSSSLYCRSGTSVLHMNSRQAFDFLKTKERQSKYNLINEGSPPSKIMKAVYQNISESNPAYEVFQTDTIEYGEILSFPESPSIEFKQFSTKHIQQYVENIIPEYISAFANTEGGYLFIGVDDKSRKVLGCAKEQVDPDSLKNVIARAISKLPIVHFCSSKPRVEYSTKIVEVFCGKELYGYLCVIKVKAFCCVVFSEAPKSWMVREKYIRPLTTEEWVEKMMDADPEFPPDFAEAFESQLSLSDSPSLCRPVYSKKGLEHKADLQQHLFPVPPGHLECTPESLWKELSLQHEGLKELIHKQMRPFSQGIVILSRSWAVDLNLQEKPGVICDALLIAQNSTPILYTILREQDAEGQDYCTRTAFTLKQKLVNMGGYTGKVCVRAKVLCLSPESSAEALEAAVSPMDYPASYSLAGTQHMEALLQSLVIVLLGFRSLLSDQLGCEVLNLLTAQQYEIFSRSLRKNRELFVHGLPGSGKTIMAMKIMEKIRNVFHCEAHRILYVCENQPLRNFISDRNICRAETRETFLREKFEHIQHIVIDEAQNFRTEDGDWYRKAKTITQREKDCPGVLWIFLDYFQTSHLGHSGLPPLSAQYPREELTRVVRNADEIAEYIQQEMQLIIENPPINIPHGYLAILSEAKWVPGVPGNTKIIKNFTLEQIVTYVADTCRCFFERGYSPKDVAVLVSTVTEVEQYQSKLLKAMRKKMVVQLSDACDMLGVHIVLDSVRRFSGLERSIVFGIHPRTADPAILPNILICLASRAKQHLYIFL
Protein: Cytochrome P450 72A397 (EC 1.14.14.-) (A0A0S2IHL2)
Organism: Kalopanax septemlobus (Castor aralia) (Acanthopanax septemlobus)
Function: Catalyzes the oxidation of oleanolate at the C-23 position to form hederagenin.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDGVVVTYTKIAAAVAVAVVVVGWAWKVLNWVWVSPRKLEESLRKQGFRGNSYRLFYGDLKESSEMTRKAKLKPINLSDDPVLRVRPFIHQTVKKYGKSSFIWIGPTPRVQIMDPEIIKEIMVKSYKFNKPKRNPLVKLFADGLANHEGELWAKHRKLLNPAFHLERLKCMLPAMYFSCIEMVSKWDKMISKDGSRELDVWPFLQRLTSDVISHTAFGSSYEEGNIVFELQTEQAELVMKTLQSVYIPGWSYLPTKRNRKMKEIDRKTQSCLMNIINKKTKAMQAGEGSTDDILGILLESNLKEQLGQGKKNVGMSIQEVMGECKQFYFAGQETTSGLLVWTMVLLSIHPNWQARAREEVLQQFGNAKPDFDNLNHLKIVTMILYEVLRLYPPVDTLFRRVDQETTLGDITLPAGVQISLPIMILHHDQNIWGDDAKEFNPERFSEGVSKATKNQVVFFPFGWGPRICIGQNFALLEAKLALAIILQRFSFELSPSYTHAPTTVLTVQPQHGANLILHKL
Protein: Uncharacterized protein (Q38EF3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQVLLKLRQPLAGCRPCVHRCVGLIFDSPMVEARLASSSFSGRNSESAILFSKGPRASVASSVKHMVPPPQRQPQTTKPVTSSPPNVLSGPLPAVGTPLLDAGEITTEVAAVLVMYRRHLNEQREMANGKGVDLGEAIATTTADTWGGVTISAPFYPPVPLEYMEEHFQPLLSRLVPGAGSPVRLVGAGVGVEHNKQLLTSRIQSTCVFTLSPSSSRTSLDGKISPESRGADEKLVIRVRPGVRELATEIAALVRTLEASNGCGERRPVPLKVIHRASLSHAATSFTRRELSNDIKRLLLVYECELFAFSSNGSVVRVRDGCGMGSARGAESTTVRSEAASPTQSHHVPVNSAPSPPVGEAHTVMHMGERIIAPSSMERYRLSQSLLPLLQFIQTIPVSSTGMSVDSDGHGFVDFAAVRNRVLAAHPSLTSLFVLNREDVRRRREVAFLSALSTLGVEWCWGRPLAECQQRKTQHQGRQSPHLESSNEALSDIGVLFLRRRLCAVPEAQVTAKGDMPPTGRLPHSVVLRELSDEGEVADAPVSRLVVDERPWWSFVSYWQGTAPDPEENVDMLDRLFCGLQAAVYEKLEQLPSARLFVQPLGEDIVAAPSCAMYPMGACANIAFVRHLMRYFTTRQHEALHPMLIGEVQGRVSPLVKNEIKENIACLFFPYEECSAQRTGSHIGAKVDSGCGACGDNATKYKLIVFNRFVDGCYKTEGGRQVLYIRARATPGEPPLASRKKLPAKLVLEVMCCLHRELLRRAEEIGMDFEDDVDESDESNRGDGSGDGSCLSFAVLRTLLPIDIRVFIRDHIGDPALIPLLVVCHPRYFFTTSDGVSNCWGAVGLTCAGRRLARHLEETSDRELGISYCGNQPSPYRNPLTGSLFMNNTRQQLESFLICH
Protein: Rab GDP dissociation inhibitor beta (Rab GDI beta) (GDI-3) (Guanosine diphosphate dissociation inhibitor 2) (GDI-2) (P50399)
Organism: Rattus norvegicus (Rat)
Function: GDP-dissociation inhibitor preventing the GDP to GTP exchange of most Rab proteins. By keeping these small GTPases in their inactive GDP-bound form regulates intracellular membrane trafficking. Negatively regulates protein transport to the cilium and ciliogenesis through the inhibition of RAB8A.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P50395}.
Interaction partners:
- small monomeric GTPase
- Ras-related protein Rab-6A
- Ras-related protein Rab-10
- Ras-related protein Rab-1B
- Ras-related protein Rab-6B
- Cell division control protein 42 homolog
- Ras-related protein Rab-8A
- Ras-related protein Rab-7a
- Ras-related protein Rab-11B
- Ras-related protein Rab-11A
Sequence:
MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDQNPYYGGESASITPLEDLYKRFKLPGQPPASMGRGRDWNVDLIPKFLMANGQLVKMLLFTEVTRYMDFKVIEGSFVYKGGKIYKVPSTEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGVDPKKTSMRDVYKKFDLGQDVIDFTGHSLALYRTDDYLDQPCCETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFARLSAIYGGTYMLNKPIEEIIVQNGKVVGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRVICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETKEPEKEIRPALELLEPIEQKFVSISDLFVPKDLGTDSQIFISRAYDATTHFETTCDDIKDIYKRMTGSEFDFEEMKRKKNDIYGED
Protein: Krueppel-like factor 15 (Cardiovascular Krueppel-like factor) (Q9EPW2)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator that binds to the GA element of the CLCNKA promoter (By similarity). Binds to the KCNIP2 promoter and regulates KCNIP2 circadian expression in the heart. Is a repressor of CCN2 expression, involved in the control of cardiac fibrosis. Is also involved in the control of cardiac hypertrophy acting through the inhibition of MEF2A, GATA4 and MYOCD activity. Is a negative regulator of TP53 acetylation. Inhibits NF-kappa-B activation through repression of EP300-dependent RELA acetylation (By similarity). Involved in podocyte differentiation.
Subcellular location: Nucleus.
Interaction partners:
- Peroxisome proliferator-activated receptor alpha
Sequence:
MVDHLLPVDETFSSPKCSVGYLGDRLASRQPYHMLPSPISEDDSDVSSPCSCASPDSQAFCSCYSAGPGPEAQGSILDFLLSRATLGSGGGSGGIGDSSGPVTWGSWRRASVPVKEEHFCFPEFLSGDTDDVSRPFQPTLEEIEEFLEENMEAEVKEAPENGSRDLETCSQLSAGSHRSHLHPESAGRERCTPPPGGTSGGGAQSAGEGPAHDGPVPVLLQIQPVAVKQEAGTGPASPGQAPESVKVAQLLVNIQGQTFALLPQVVPSSNLNLPSKFVRIAPVPIAAKPIGSGSLGPGPAGLLVGQKFPKNPAAELLKMHKCTFPGCSKMYTKSSHLKAHLRRHTGEKPFACTWPGCGWRFSRSDELSRHRRSHSGVKPYQCPVCEKKFARSDHLSKHIKVHRFPRSSRAVRAIN
Protein: Farnesyl diphosphate synthase (FPP synthase) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Geranyltranstransferase) (P22939)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm.
Interaction partners:
- 1-deoxy-D-xylulose-5-phosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- Isopentenyl-diphosphate Delta-isomerase
- Ditrans,polycis-undecaprenyl-diphosphate synthase
- Exodeoxyribonuclease 7 small subunit
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Octaprenyl diphosphate synthase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
Sequence:
MDFPQQLEACVKQANQALSRFIAPLPFQNTPVVETMQYGALLGGKRLRPFLVYATGHMFGVSTNTLDAPAAAVECIHAYSLIHDDLPAMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAFSILSDADMPEVSDRDRISMISELASASGIAGMCGGQALDLDAEGKHVPLDALERIHRHKTGALIRAAVRLGALSAGDKGRRALPVLDKYAESIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALLGLEQARKKARDLIDDARQSLKQLAEQSLDTSALEALADYIIQRNK
Protein: Activated Cdc42 kinase-like (EC 2.7.10.2) (Tyrosine-protein kinase PR2) (Q9I7F7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Likely to act as a downstream effector of Cdc42 during dorsal closure, acting in a kinase independent manner with the other ACK family member Ack to positively regulate expression of the myosin zip by promoting the endocytosis of Egfr in the amnioserosa (AS).
Interaction partners:
Sequence:
MEYPQIDLYEFLTESELQQYYNAVKNELKITNAAQFKYAADEDLRFIGLSRPEIRRLRKFYEKHFPHSYLSKIKRLLQAPGTMVKREEAPGGGSQVALDGSSASACSSLAAKNGASSPSKVPNNKHIIPADSISVNKQLGTGEFGIVQQGVWSNGNERIQVAIKCLCRERMQSNPMEFLKEAAIMHSIEHENIVRLYGVVLATDSLMLVTELAHLRSLLECLKDSGLRVSFLTIPTLCEFALQICNGMRYLEQKRLIHRDLAARNILVFSKDKVKISDFGLSRALGVGKDYYKTNFNVNLKLPIAWCAPECINYLRFTNASDVWAFGVCLWEMFSYGFQPWAALTGLQILEAIDAPNYQRLEQPDCCPSEYYTLMMKCWQDDAAKRPRFGEIYDQLPDMKPEQLKAVVNCTEPKKDHLLYRQGDIISVLDRNTGTPFWKGVLSTGKTGYFNPSNTVAFLEGLPSSTRDSFSRVSDHRISKRKLRTEMISKPQNDFKHTGHVGIDGATFGDIAFLGSSQNYNHVPKQIVTPYKPSEDIEQTPLLLPPTPTSPDSLQTASGYFPEGANSGGAMGTSMNPTFIPSAEHTPKLIATNGQSSFDFASGSTNPFFPNRGDDELEFGLHNYGADGKSVHSETGWRPTSRSIVDDPHEYHEISDDEIAADKLDFGPSLLDEINSMFGSISAATGSHPKSPGFDHVNNKNEITEMSAKLGQKSGDTNGNKHGHGLLPTLSKKKSSGTVKPISVKDEKILNHAIEIANEISARSMIDLVSDQTPVIHSPKRKFSFRFPHLSNNGSGDKSGGLGTSGSAHTPTHGNASPFPKKKNFTEELQSIPDIQSLIGKEGLEAYNSLIERKALLDIGPSPAATLLRHLDTDEFDLQSLHQSQRPMTLPTRGATQRVRKAELAAGLSRHNDENSNSLEACESPSYMTHGSYKFPEAQPTEQLPEPESPNPIPLPPREGKKQVKTSTKRHVRKYPLIIPANGLQRTLSKLADFGDEAAKSPEISTSSQPQPGRAIEVVAAVRPSGMRRPSRPSEREYENMPTVGKESAHTYQNLDKLTPADAAGLTDTASLQFESIMEADTSKEGILQSPDVTDGFYNFSIQKEHYNKGKDAEFEATQISGLYVNDDELRNLDIESSRRTATPCSSCSALESEHSQPDALPSTESVSEVSRFSSVDNELAGNALFKKVRASVNMAMNRKSVAETSLTSNQPGGASAKPQTEAEYFAATAARLADSNSVSCEDLLEFSDKKPKGCERGVDSDEVRIMVKVLGKDSTPNRCLGALEFINWDVHKSIKLIKLQNLVSEANLSLEASFEALQQHEWDLHTTAHKLNGLKL
Protein: Small nuclear ribonucleoprotein Sm D2 (Sm-D2) (snRNP core protein D2) (B5DES0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU365051}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365051}. Note=SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes. {ECO:0000256|RuleBase:RU365051}.
Interaction partners:
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein F
- Small nuclear ribonucleoprotein Sm D3
- U1 small nuclear ribonucleoprotein 70 kDa
- Small nuclear ribonucleoprotein G
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein-associated protein B
- U1 small nuclear ribonucleoprotein C
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein-associated protein N
Sequence:
MSLLNKPKSEMTPEELQKREEEEFNTGPLSVLTQSVKNNTQVLINCRNNKKLLGRVKAFDRHCNMVLENVKEMWTEVPKSGKGKKKSKPVNKDRYISKMFLRGDSVIVVLRNPLIAGK
Protein: Small ribosomal subunit protein eS10A (40S ribosomal protein S10-A) (O14112)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS19A
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS14
- Elongation factor 3
- Small ribosomal subunit protein eS8A
Sequence:
MLIPKENRKAIHQALFSQGVLVAKKDFNLPKHPEVGVPNLQVIKACQSLDSRGYLKTRYNWGWFYYTLTNEGVEYLREYLHLPAEVVPATHKRQVRPTAPRAGRPEPRERASADAGYRRAEKKDEGAAPSGFAPSFRGGFGRPQ
Protein: Meiotic 217 (Q86B50)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI21203p1
- Kinesin-like protein unc-104
Sequence:
MFTVDASEGSSVVNETPLKSQFHDQKLVEHFCRQTQLLKLVQVSSGRFVANYMSSRRPEDLLAPIQLRLDFEYRQLLDISPQLLQLIVEEPLQFQEAVRYSVYGLIRSHLKDAGLKPIDINQLHAHWRLVGLPFTPGLQFEPRDQLTRLGLSQIRGILAAFTPQETLVLQSIWYCGSGCMRNAIQTSSTDAPFCSSCSRPMSEYQKLRVTETYRILAVLPISAVQTPRVTNCLHRPKLVRLRAHAHDCELKLGASYLITGYFASSASTYQLEACHLRIN
Protein: La-related protein 7 homolog (Telomerase-associated protein of 65 kDa) (p65) (W7X6T2)
Organism: Tetrahymena thermophila (strain SB210)
Function: RNA-binding protein required for assembly of the holoenzyme telomerase ribonucleoprotein (RNP) complex. Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER. TAP65/p65 specifically binds telomerase RNA template TER and is required for biogenesis and placement of the TER stem-terminus element: TAP65/p65 first protects the 3'-end of TER from degradation and acts as a chaperone to correctly fold TER for protein binding; it then bends TER stem-loop IV to position it for interaction of stem-loop IV with catalytic TERT RNA-binding domain.
Subcellular location: Chromosome, telomere {ECO:0000305}.
Interaction partners:
- Telomerase reverse transcriptase
- Telomerase-associated protein p75.
- Telomerase associated protein p45.
- Uncharacterized protein.
- Telomerase-associated protein.
- Telomerase-associated protein.
- Uncharacterized protein.
- Cyclic nucleotide-binding domain protein.
- Mov34/MPN/PAD-1 family protein
- RNA recognition motif protein
Sequence:
MDEYLENTNLEELEQECFMEDYQHEDVVEQENHQVDANDIYENQQMNDESQLNQDVKISQQKEQAVEMIEEQQQNNQDKFKQFQDCMAHITELNFKRNYQNLTEQSSSNNVVAEELDIKESLKLQMEYYFCDTNLTHDSYLRGIISKSPKNCVDIKVFLKFNKIQQILKQIQDKQIVSTYGIENQSQKKNHKNYKNQNATFSKKDLIHLIRDSLKESKILKVKMDSLKVKRRFPFNLEQALKNSKQRTLYIDFLPPKCSKQTLVSIFGNFRIININLPLQKNSQLCQGFAFIEFFSEEEANQALITKNSSIPKELILLTEKKIGQGSIRIITYKKWQEEKQSFKELSKNQNEQKNKNMNQSRKASDEFVSIDVEIKQNCLIKIINIPQGTLKAEVVLAVRHLGYEFYCDYIDENSNQINSNKISLSTQQQNTAQCSNIQIENNLIQQDQHPQLNDLLKEGQAMIRFQNSDEQRLAIQKLLNHNNNKLQIEIRGQICDVISTIPEDEEKNYWNYIKFKKNEFRKFFFMKKQQKKQNITQNYNK
Protein: Protein GAMETE EXPRESSED 3 (Q9LFS2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for micropylar pollen tube guidance. Plays a role during early embryo patterning.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19825564}; Single-pass membrane protein {ECO:0000269|PubMed:19825564}.
Interaction partners:
- Protein GAMETE EXPRESSED 2
- Embryo defective 1381
- Protein PIR
- protein-synthesizing GTPase
- Nuclear pore complex protein GP210
- Sialyltransferase-like protein 1
- Probable helicase MAGATAMA 3
- Protein BRICK 1
- Protein GAMETE EXPRESSED 1
- Marker for oxidative stress response protein
Sequence:
MVAFRFVYIPLPFFFFFFFFFVFFSGVSQLQDQTATKKSVRILSKILIGDDGRVYACSDNDFFSFESNGSIAWSVHMNFKCNTDFAPVYSGFNQMLLLAENRILRVIFPRNGTKSEPELFFDPGETILGFAVSVSSSSVYITVKNHGLYAYNMFRQQLWIAEPKIERFGYRLGCRKDFDNCTFNSRPVIDSCEGSIYISNNEGELYSLSLRGTYYQWIQDFSLVDRFFTVTPGNNGLVYVVFPIKSLVFALDSFSGDILWQKTIGPLAETSASDPVIDSNSWASIGSLDGTLYSFSRTGDLYKIPKNAETDSVIQIEPLLDCSGYAVYVSQTKFEGMIDRVIEDYTYVSAKKPETAVFSLVVPETRSIYWSQSYSDQIPGLLLDEDLQHFVLDERIALAFVAASSSGNPFRCRSKHEKLSSSCSFAEPEHLDIYIGNERAIIWFLLFEFVIMVLFAALVRFCFIFWKKKKLQDRPFSTFLDKRRLLHRKSREIDKTITRLQNESTANESAVDKIGDLIQKRENVKRKLSSTYSLGRDIDESKSKLKDYVLPLYGGSSRSFSYRNRENESITIFQTPSDESSSEESYRDEHYDDVADDEHDEDDLDRKQKGKLLAHSEGSSNDGDGIASSRRSIYLKHIFDD
Protein: Latent membrane protein 2 (Terminal protein) (P13285)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell antigen receptor (BCR) into lipid rafts, preventing the subsequent signaling and accelerated internalization of the BCR upon BCR cross-linking. Serves as a molecular scaffold to recruit SYK, LYN and E3 protein-ubiquitin ligases, such as ITCH and NEDD4L, leading to ubiquitination and potential degradation of both tyrosines kinases. Possesses a constitutive signaling activity in non-transformed cells, inducing bypass of normal B lymphocyte developmental checkpoints allowing immunoglobulin-negative cells to colonize peripheral lymphoid organs (By similarity).
Subcellular location: [Isoform LMP2A]: Host cell membrane {ECO:0000269|PubMed:11163230, ECO:0000269|PubMed:11961256}; Multi-pass membrane protein {ECO:0000269|PubMed:11163230, ECO:0000269|PubMed:11961256}. Note=Isoform LMP2A is localized in plasma membrane lipid rafts. {ECO:0000269|PubMed:11163230}.; SUBCELLULAR LOCATION: [Isoform LMP2B]: Host endomembrane system {ECO:0000269|PubMed:11961256}; Multi-pass membrane protein {ECO:0000269|PubMed:11961256}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:11961256}. Note=Isoform LMP2B localizes to perinuclear regions. {ECO:0000269|PubMed:11961256}.
Interaction partners:
Sequence:
MGSLEMVPMGAGPPSPGGDPDGYDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQDQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALSLLLLAAVASSYAAAQRKLLTPVTVLTAVVTFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWRRLTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAALLTLAAALALLASLILGTLNLTTMFLLMLLWTLVVLLICSSCSSCPLSKILLARLFLYALALLLLASALIAGGSILQTNFKSLSSTEFIPNLFCMLLLIVAGILFILAILTEWGSGNRTYGPVFMCLGGLLTMVAGAVWLTVMSNTLLSAWILTAGFLIFLIGFALFGVIRCCRYCCYYCLTLESEERPPTPYRNTV
Protein: Suppressor of mec-8 and unc-52 protein homolog 2 (AtSMU-2) (Protein RED-like) (RNA splicing protein SMU2) (O48713)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxiliary spliceosomal protein involved in splicing of specific pre-mRNAs that affect multiple aspects of development.
Subcellular location: Nucleus {ECO:0000269|PubMed:19734266}.
Interaction partners:
- Suppressor of mec-8 and unc-52 protein homolog 1
- Protein STABILIZED1
- Pre-mRNA-splicing factor 38
- Microfibril-associated protein-like
- Microfibrillar-associated protein-like protein
- Zinc finger protein ZOP1
- Nuclear protein-like
- Small nuclear ribonucleoprotein SmD3b
- 110 kDa U5 small nuclear ribonucleoprotein component CLO
- 109 kDa U5 small nuclear ribonucleoprotein component GFL
Sequence:
MKPSKSHHKEKTARRREEKLEESDNPKYRDRAKERRENQNPDYDPSELSSFHAVAPPGAVDIRAADALKISIENSKYLGGDVEHTHLVKGLDYALLNKVRSEIVKKPDGEDGDGGKTSAPKEDQRVTFRTIAAKSVYQWIVKPQTIIKSNEMFLPGRMTFVYDMEGGYTHDIPTTLYRSKADCPVPEEFVTVNVDGSVLDRIAKIMSYLRLGSSGKVLKKKKKEKDGKGKMSTIANDYDEDDNKSKIENGSSVNISDREVLPPPPPLPPGINHLDLSTKQEEPPVARTDDDDIFVGEGVDYTVPGKDVTQSPISEDMEESPRDKEKVSYFDEPAYGPVQEKVPYFAEPAYGPVQPSAGQEWQDMSAYGAMQTQGLAPGYPGEWQEYQYAEQTGYQEQYLQPGMEGYEVQPETDVLLDPQLMSQEEKDRGLGSVFKRDDQRLQQLRESDAREKDPTFVSESYSECYPGYQEYNHEIVGSDEEPDLSKMDMGGKAKGGLHRWDFETEEEWEKYNEQKEAMPKAAFQFGVKMQDGRKTRKQNRDRDQKLNNELHQINKILTRKKMEKEGGDVASLDAAEAQTPKRSKH
Protein: Heparan-sulfate 6-O-sulfotransferase 2 (HS6ST-2) (mHS6ST-2) (EC 2.8.2.-) (Q80UW0)
Organism: Mus musculus (Mouse)
Function: 6-O-sulfation enzyme which catalyzes the transfer of sulfate from 3'-phosphoadenosine 5'-phosphosulfate (PAPS) to position 6 of the N-sulfoglucosamine residue (GlcNS) of heparan sulfate.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
- D-glucuronyl C5-epimerase
- Heparan sulfate glucosamine 3-O-sulfotransferase 1
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 2
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
Sequence:
MALPAFAARALGPPLQPEQGAPARTTCPRRHSRVEAELAASRPGSVAASVRAGPPRGVSLGFNSPPLQDKPPKAFSSLAGALRAPLFALLPRGRRRRMHDLRRRWDLGSLCRALLTRGLAAVGHSLKHVLSAIFSKIFGPLASVGNMDEKSNKLLLALVMLFLFAVIVLQYVCPGTECQLLRLQAFSSPVPDPYRSEDESSARFVPRYNFSRGDLLRKVDFDIKGDDLIVFLHIQKTGGTTFGRHLVRNIQLEQPCECRVGQKKCTCHRPGKRETWLFSRFSTGWSCGLHADWTELTSCVPAVVDGKRDARLRPSRNFHYITILRDPVSRYLSEWRHVQRGATWKASLHVCDGRPPTSEELPSCYTGDDWSGCPLKEFMDCPYNLANNRQVRMLSDLTLVGCYNLSVMPEKQRNKVLLESAKSNLKHMAFFGLTEFQRKTQYLFEKTFNMNFISPFTQYNTTRASSVEINEEIQKRIEGLNFLDMELYSYAKDLFLQRYQFMRQKEHQDARRKRQEQRKFLKGRFLQTHFQSQSQGQSQSQSPGQNLSQNPNPNPNQNLTQNLSHNLTPSSNPNSTQRENRGSQKQGSGQGQGDSGTSNGTNDYIGSVETWR
Protein: Large ribosomal subunit protein eL22B (60S ribosomal protein L22-B) (L1c) (RP4) (YL31) (P56628)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein eL31A
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL22A
- Large ribosomal subunit protein eL38
- Ribosome biogenesis protein NOP53
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL14A
Sequence:
MAPNTSRKQKVIKTLTVDVSSPTENGVFDPASYSKYLIDHIKVDGAVGNLGNAIEVTEDGSIVTVVSSAKFSGKYLKYLTKKYLKKNQLRDWIRFVSIRQNQYKLVFYQVTPEDADEEEDDE
Protein: SET domain-containing protein 4 (Ar-SETD4) (EC 2.1.1.-) (EC 2.1.1.360) (A0A140C435)
Organism: Artemia parthenogenetica (Brine shrimp)
Function: Protein-lysine N-methyltransferase involved in the regulation of cell quiescence by catalyzing the trimethylation of 'Lys-20' of histone H4 and 'Lys-79' of histone H3 (H4K20me3 and H3K79me3, respectively) during diapause formation, a state of obligate dormancy.
Subcellular location: Nucleus {ECO:0000305|PubMed:28031330}.
Interaction partners:
Sequence:
MVDRIDPLDITNIKDLSTWMKTKNWRNIAKLEPCRFKESGRGMRTRKGLKAGQLLVQIPRLLLMTAGDFRTSKEWSWIVDKNLSCHDALVLYLLVEKNKRDSSFFHAYIKTLPEVFSMPTDLRSEMTHMLPNFIAMKLQDKIKSLQDSFKNVARGYKSICIKELGFSDFKWAYYVVNTRAVHITGSSGKFNADSSDCMALAPFLDLLNHTHDTSSISGFNPYTNCYEIETLSKTPKCSEVFINYGPHDNLSLFVEYGFMIPRNPNNFVPFEMTDFISACNEYNVKLSNLCLQTINLHNLMKNLGCFADGPSWSVKVLLKVLSCDWSSLMRIEDIIYRDFENHGLTEKTLLNCILEKKKEELQNSLSTIAKDKNCQIANCIVSFLEECLSIIEFSYAN
Protein: Loner ISO3 (Schizo, isoform C) (Q6U9V3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MIICISGFIIGESFPQKSLERSGSTQYELAGAQQPGSANASTCTDSGSVGGYVYLQNHYAPGAHSSSAAINYPAQQHPQMVYQIQQYPTCHQQQQQQHLQQQQHLHQTGAGHYMQVTATGGGQYHHHHMLHGHGHHAHHHGGAVVIAGSGVGTGLGSGATSVIMQHQQQQQQQQNMHKKNSIRNGGDVLKRTRAQSAYELSQDLLEKQIELLERKYGGVRARNAAVTIQRAFRHYMMVKKFASITAMAKAEKRLSRRMVVTASSLGLAEEGASSSSAYGSATESQLTEQQQQQQAQQQQQPRVTIMAGPAGAASPGLSRTPPTRSLSMRERRQLDCSPIPRSQSGASPASISSSTVSTSALASHPHVNLLHAAEPHYYNAQALPQGAAYYTSYHGSPHDLSYASSADTSLNASWVNTSGHSPHTPYYSAAQIYMRPKGGSTTPTPSCSGSTGSGSGGSGSGSSKKVPPEVPKRTSSITAQQQTQLLLLQRQTPPPPSLLRTNGLCKTAENGSLTSVQSSGSDSSVTSAERNLNSDLGSDRSNSPHTWKRGTALNSSQQFSTHSADSAGAVSGGGVGVAGGAGVYAAQMQAAVAAATAAGGMPPADDHAISSHTSAAQYEQHEQQQHEQQQLQAAAAAAGVAQNYKMSETIRKRQYRVGLNLFNKKPEKGITYLIRRGFLENTPQGVARFLITRKGLSRQMIGEYLGNLQNQFNMAVLSCFAMELDLSGRQVDVALRKFQAYFRMPGEAQKIERLMEIFSQRYCECNADIVGRLRSSDTIFVLAFAIIMLNTDLHTPNLKPERRMRVEDFIKNLRGIDDCHDIDKDMLMGIYDRVKSDEFKPGSDHVTQVMKVQATIVGKKPNLALPHRRLVCYCRLYEIPDVNKKERPGVHQREVFLFNDLLVITKIFSKKKTSVTYTFRNSFPLCGTVVTLLDMPNYPFCIQLSQKVDGKILITFNARNEHDRCKFAEDLKESISEMDEMESLRIEAELERQKSARNRAPGNAENRDSGVADVEVCPCPYQQGSQASGEQAPNSADNSQQLKRSALSNSLLDMHEQFGNEKPQRRGSVGSLDSGMSISFQSTTTSSASRENAAAIAAAANAAAAAKMRFNMPPTAAIATPSNVYAAPGMQAYTHANFVQQSQAAYMLQQQQMLQQQAQMQAQAQAQAQAQAQAQAQAQAQAQAQPLTGRIPGRERKASRTDENGRSTEV
Protein: Beta-hexosaminidase (EC 3.2.1.52) (G5EB27)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Beta-N-acetylglucosaminidase, putative
- Beta-N-acetylglucosaminidase, putative
- Probable alpha-galactosidase B
- Alpha-galactosidase D
- Alpha-galactosidase C
- alpha-galactosidase
- Probable alpha-galactosidase G
- beta-N-acetylhexosaminidase
- Endochitinase B
- chitinase
Sequence:
MAYFRLYAVLLAVASSVAAVKVNPLPAPRHISWGHSGPKPLSDVSLRTERDTDDSILTNAWNRAWETIVSLEWVPAGIEAPIPEFDEFPTSTPSASAAATRSKRANVPIQFVDVDVEDWDADLQHGVDESYTLDAKAGSDAIDITAKTVWGALHAFTTLQQLVISDGNGGLILEQPVHIKDAPLYPYRGLMVDTGRNFISVRKLHEQLDGMALSKLNVLHWHLDDTQSWPVHIDAYPEMTKDAYSARETYSHDDLRNVVAYARARGIRVIPEIDMPAHSASGWQQVDPDIVACANSWWSNDNWPLHTAVQPNPGQLDIINPKTYEVVQDVYEELSSIFTDDWFHVGGDEIQPNCYNFSTYVTEWFQEDPSRTYNDLMQHWVDKAVPIFRSVSDSRRLVMWEDVVLNTEHADDVPTDIVMQSWNNGLENINKLTERGYDVIVSSADFMYLDCGRGGYVTNDDRYNEQTNPDPDTPSFNYGGIGGSWCGPYKTWQRIYNYDFTLNLTNAQAKHVIGATAPLWSEQVDDVNISNLFWPRAAALAELVWSGNRDAKGNKRTTLFTQRILNFREYLLANGVMAATVVPKYCLQHPHACDLNYDQTVLH