wanglab/gogpt-training-data huggingface dataset:
Protein: Prolactin-8A5 (Growth hormone-related placental protein 2) (Placental prolactin-like protein C) (PLP-C) (PRL-like protein C) (P33579)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted.
Interaction partners:
Sequence:
MELALSQPSFFGTLLMLVVSNLLLWEKAASIPACMVEDGGCWDPLREAFNSATQRAETLRNLSDQLYVEFFQNQFSSRQFADLSSQLIRKDETVLKAGTYCHSNRAKPKSRGVNIDIEEYLKMSINFCGFMDQPLFHLVIELSAMEGVPETILSKAKDLEENNRQLLDDLRWILTKVFPTAEIKEEFPSWDYLSFLKSSNKNHKFLAIFNLSSCLDYDTQVHYTLSQILNCLITGKDC
Protein: Fos-related antigen 1 (FRA-1) (P10158)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P51145}.
Interaction partners:
- Transcription factor Jun
- Transcription factor JunD
- Protein FosB
- Protein c-Fos
- Transcription factor JunB
- Fos-related antigen 2.
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase 13
Sequence:
MYRDFGEPGPSSGAGSAYGRPAQPQQAQTQTVQQQKFHLVPSINAVSGSQELQWMVQPHFLGPSGYPRPLTYPQYSPPQPRPGVIRALGPPPGVRRRPCEQISPEEEERRRVRRERNKLAAAKCRNRRKELTDFLQAETDKLEDEKSGLQREIEELQKQKERLELVLEAHRPICKIPEEDKKDTGGTSSTSGAGSPPGPCRPVPCISLSPGPVLEPEALHTPTLMTTPSLTPFTPSLVFTYPSTPEPCSSAHRKSSSSSGDPSSDPLGSPTLLAL
Protein: Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] (EC 3.6.1.17) (Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase) (Ap4A hydrolase) (Ap4Aase) (Diadenosine tetraphosphatase) (Nucleoside diphosphate-linked moiety X motif 2) (Nudix motif 2) (P56380)
Organism: Mus musculus (Mouse)
Function: Catalyzes the asymmetric hydrolysis of diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) to yield AMP and ATP (By similarity). Exhibits decapping activity towards FAD-capped RNAs and dpCoA-capped RNAs in vitro.
Interaction partners:
- Inosine triphosphate pyrophosphatase
- Nucleoside diphosphate kinase 6
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Nucleoside diphosphate kinase 3
- CTP synthase 2
- CTP synthase 1
- Adenylate cyclase type 9
- Adenylate cyclase type 1
- Nucleoside diphosphate kinase B
Sequence:
MALRACGLIIFRRHLIPKMDNSTIEFLLLQASDGIHHWTPPKGHVDPGENDLETALRETREETGIEASQLTIIEGFRRELNYVARQKPKTVIYWLAEVKDYNVEIRLSQEHQAYRWLGLEEACQLAQFKEMKATLQEGHQFLCSTPA
Protein: Flagellar hook-associated protein 1 (HAP1) (P70859)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Subcellular location: Secreted {ECO:0000250}. Bacterial flagellum {ECO:0000250}.
Interaction partners:
Sequence:
MDSTFSGIEIGKRSLFAHKDAMNTVGHNLSNATKPGYSRQRVTMKTEIPLYAPQLNRAKKQGQLGQGIVVQSIDRVKDELLNTRIIEESHRLGYWTSQDKFISILEDVYNEPEDQSIRKRLNDFWESWHDLANQPQGLAERKIILERGKSFCEGIRNRFHSLERIYIMANDEIKITTDEANNYIRNIANLNKQISKSQAMKDNPNDLMDARDLMVEKLGNIISVSIENKQDPNEFLIHAEGRHLVQGSIANEFKLEATNGPTRTRWNILWANNDKAYLKTGKLGSLLNIRDEEIKNEINELNNIAANIIEIVNEIHEAGRGMDKKNGRSFFSQELKLTDDRGRYDTNGNGQFDSVHIFKINSTNEIFPEEKLGFYGTLKFEATNSNEIVEIPYNAPDTVQDVINRINNSNAQVTARINSEGKLEIKAVKEQEDENITFKIKHIEDSGSFLTKYTGILNASGPEGAYDYKNIDTTDKLAPKSTYSISPLKNPAAWIKVADIIDSDPSKIASGIKNPTNEISIGDNQAALRISSFGNSQIMIGKNLTLNDYFANTASNIAIKGQISEITKESQSQILKDLTDLRMSISGVNKDEELANMIEFQQAFIAASKFITVSVELIDTVINKMGV
Protein: Splicing factor U2af large subunit B (U2 auxiliary factor 65 kDa subunit B) (U2 small nuclear ribonucleoprotein auxiliary factor large subunit B) (U2 snRNP auxiliary factor large subunit B) (Q8L716)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Necessary for the splicing of pre-mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:24580679}. Nucleus speckle {ECO:0000269|PubMed:28760995, ECO:0000269|PubMed:36282917}. Note=Colocalizes in nuclear speckles with DRT111/RSN2/SFPS. {ECO:0000269|PubMed:28760995, ECO:0000269|PubMed:36282917}.
Interaction partners:
- Splicing factor U2af small subunit A
- Nuclear protein-like
- Zinc finger C-x8-C-x5-C-x3-H type family protein
- Splicing factor U2af small subunit B
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing factor 17
- U11/U12 small nuclear ribonucleoprotein 35 kDa protein
- Splicing factor U2af large subunit A
- RNA-binding
- Zinc finger CCCH domain-containing protein 5
Sequence:
MMSYEGNGDGVAISTENHNENYISLESSPFHEDSKSRESHDLKKDSSKISEKDNENGRDKDGNKDRDREKDRDREKSRDRDREKSRDRDRDRERSKDRQRDRHHRDRHRDRSRERSEKRDDLDDDHHRRSRDRDRRRSRDRDREVRHRRRSRSRSRSRSERRSRSEHRHKSEHRSRSRSRSRSKSKRRSGFDMAPPDMLAATAVAAAGQVPSVPTTATIPGMFSNMFPMVPGQQLGALPVLPVQAMTQQATRHARRVYVGGLPPTANEQSVSTFFSQVMSAIGGNTAGPGDAVVNVYINHEKKFAFVEMRSVEEASNAMALDGIILEGVPVKVRRPTDYNPSLAATLGPSQPNPNLNLGAVGLSSGSTGGLEGPDRIFVGGLPYYFTEVQIRELLESFGPLRGFNLVKDRETGNSKGYAFCVYQDPSVTDIACAALNGIKMGDKTLTVRRAIQGAIQPKPEQEEVLLYAQQQIALQRLMFQPGGTPTKIVCLTQVVTADDLRDDEEYAEIMEDMRQEGGKFGNLVNVVIPRPNPDHDPTPGVGKVFLEYADVDGSSKARSGMNGRKFGGNQVVAVYYPEDKYAQGDYED
Protein: Sentrin-specific protease 1 (EC 3.4.22.-) (Sentrin/SUMO-specific protease SENP1) (Q9P0U3)
Organism: Homo sapiens (Human)
Function: Protease that catalyzes two essential functions in the SUMO pathway. The first is the hydrolysis of an alpha-linked peptide bond at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptides, SUMO1, SUMO2 and SUMO3 leading to the mature form of the proteins. The second is the deconjugation of SUMO1, SUMO2 and SUMO3 from targeted proteins, by cleaving an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein. Deconjugates SUMO1 from HIPK2. Deconjugates SUMO1 from HDAC1 and BHLHE40/DEC1, which decreases its transcriptional repression activity. Deconjugates SUMO1 from CLOCK, which decreases its transcriptional activation activity. Deconjugates SUMO2 from MTA1. Deconjugates SUMO1 from METTL3. Desumoylates CCAR2 which decreases its interaction with SIRT1. Deconjugates SUMO1 from GPS2.
Subcellular location: Nucleus {ECO:0000269|PubMed:14563852, ECO:0000269|PubMed:16253240, ECO:0000269|PubMed:25406032}. Cytoplasm {ECO:0000269|PubMed:14563852, ECO:0000269|PubMed:16253240}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000269|PubMed:14563852}.
Interaction partners:
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 2
- Ran GTPase-activating protein 1
- SUMO-conjugating enzyme UBC9
- SUMO-activating enzyme subunit 1
- SUMO-activating enzyme subunit 2
- Small ubiquitin-related modifier 4
- E3 SUMO-protein ligase PIAS4
- E3 SUMO-protein ligase PIAS3
- E3 ubiquitin-protein ligase RNF4
Sequence:
MDDIADRMRMDAGEVTLVNHNSVFKTHLLPQTGFPEDQLSLSDQQILSSRQGHLDRSFTCSTRSAAYNPSYYSDNPSSDSFLGSGDLRTFGQSANGQWRNSTPSSSSSLQKSRNSRSLYLETRKTSSGLSNSFAGKSNHHCHVSAYEKSFPIKPVPSPSWSGSCRRSLLSPKKTQRRHVSTAEETVQEEEREIYRQLLQMVTGKQFTIAKPTTHFPLHLSRCLSSSKNTLKDSLFKNGNSCASQIIGSDTSSSGSASILTNQEQLSHSVYSLSSYTPDVAFGSKDSGTLHHPHHHHSVPHQPDNLAASNTQSEGSDSVILLKVKDSQTPTPSSTFFQAELWIKELTSVYDSRARERLRQIEEQKALALQLQNQRLQEREHSVHDSVELHLRVPLEKEIPVTVVQETQKKGHKLTDSEDEFPEITEEMEKEIKNVFRNGNQDEVLSEAFRLTITRKDIQTLNHLNWLNDEIINFYMNMLMERSKEKGLPSVHAFNTFFFTKLKTAGYQAVKRWTKKVDVFSVDILLVPIHLGVHWCLAVVDFRKKNITYYDSMGGINNEACRILLQYLKQESIDKKRKEFDTNGWQLFSKKSQEIPQQMNGSDCGMFACKYADCITKDRPINFTQQHMPYFRKRMVWEILHRKLL
Protein: Always early (Q2PNM9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRHQLKKPRKIVAAWQNDELFIKRPNFAPRIRISEKPEIQGRVKPGVASKRIENFTKKPSKISVDVSEDEKAKEKEKEQDPYSNDFILGKRLYNFLKYLSSHRWIWCEFVDSFLDKPTLTMGYDMKRFIAEYCPLLHSCFMPRRGWQLVRRNMGKARRFSAAFIELEREELECQRRIVRQLQQHKFNPKENVGYLDQIPKRVPLPLAKDATVSSFLHGKSFEGIVNGTVMGYDPQDYTYLVRFNRNDNAVVLSLPDSQLYSDEETAAVPLSIIMRGNKSSSVISESAKTEKFGNKRYTKELLESVLRVGKLQDVKHKILMDLARMNEDFETFKEIGSSSSRRDAKVTPQRENLQRRYSASMITLHRVNADILEPLRILHDYLVEYQKQDEEEESKRGRPASEVYQKCRMQAEQDLKTAADEKFLKIESDRTQEFVRNLHTILYLNGKLGRENSSNLETIIADLVTHMVDNIQPSLGRKLKDGVDSLEPLRQQVVQIFKDVKKPERFQITQQAPMQTEDGIYNFVVEAQPDTPS
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit stt3 (Oligosaccharyl transferase subunit stt3) (EC 2.4.99.18) (O94335)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P46978}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P39007}.
Interaction partners:
- Uncharacterized protein C553.06
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit ost2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit wbp1
- Protein transport protein sec61 subunit beta
- Protein transport protein sec61 subunit alpha
- Dol-P-Glc:Glc
- Probable mannosyl-oligosaccharide glucosidase
- Uncharacterized protein C19G7.17
Sequence:
MANSATITSKKGVKSHQKDWKIPLKVLILICIAVASVSSRLFSVIRYESIIHEFDPWFNFRASKILVEQGFYNFLNWFDERSWYPLGRVAGGTLYPGLMVTSGIIFKVLHLLRINVNIRDVCVLLAPAFSGITAIATYYLARELKSDACGLLAAAFMGIAPGYTSRSVAGSYDNEAIAITLLMSTFALWIKAVKSGSSFWGACTGLLYFYMVTAWGGYVFITNMIPLHVFVLLLMGRYTSKLYIAYTTYYVIGTLASMQVPFVGFQPVSTSEHMSALGVFGLLQLFAFYNYVKGLVSSKQFQILIRFALVCLVGLATVVLFALSSTGVIAPWTGRFYSLWDTNYAKIHIPIIASVSEHQPPTWSSLFFDLQFLIWLLPVGVYLCFKELRNEHVFIIIYSVLGTYFCGVMVRLVLTLTPCVCIAAAVAISTLLDTYMGPEVEEDKVSEEAASAKSKNKKGIFSILSFFTSGSKNIGIYSLLSRVLVISSTAYFLIMFVYHSSWVTSNAYSSPTVVLSTVLNDGSLMYIDDFREAYDWLRRNTPYDTKVMSWWDYGYQIAGMADRITLVDNNTWNNTHIATVGKAMSSPEEKAYPILRKHDVDYILIIYGGTLGYSSDDMNKFLWMIRISQGLWPDEIVERNFFTPNGEYRTDDAATPTMRESLLYKMSYHGAWKLFPPNQGYDRARNQKLPSKDPQLFTIEEAFTTVHHLVRLYKVKKPDTLGRDLKQVTLFEEGKRKKLRRPAKTNEIPLRV
Protein: Platelet glycoprotein Ib beta chain (GP-Ib beta) (GPIb-beta) (GPIbB) (Antigen CD42b-beta) (CD antigen CD42c) (P13224)
Organism: Homo sapiens (Human)
Function: Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Platelet glycoprotein Ib alpha chain
- Platelet glycoprotein IX
- von Willebrand factor
- Platelet glycoprotein V
- 14-3-3 protein zeta/delta
- Tyrosine-protein kinase Lyn
- Septin-5
- G protein subunit beta 1 like.
- Filamin-A
- Integrin alpha-IIb
Sequence:
MGSGPRGALSLLLLLLAPPSRPAAGCPAPCSCAGTLVDCGRRGLTWASLPTAFPVDTTELVLTGNNLTALPPGLLDALPALRTAHLGANPWRCDCRLVPLRAWLAGRPERAPYRDLRCVAPPALRGRLLPYLAEDELRAACAPGPLCWGALAAQLALLGLGLLHALLLVLLLCRLRRLRARARARAAARLSLTDPLVAERAGTDES
Protein: Transmembrane protein 229B (Q8NBD8)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MASAEPLTALSRWYLYAIHGYFCEVMFTAAWEFVVNLNWKFPGVTSVWALFIYGTSILIVERMYLRLRGRCPLLLRCLIYTLWTYLWEFTTGFILRQFNACPWDYSQFDFDFMGLITLEYAVPWFCGALIMEQFIIRNTLRLRFDKDAEPGEPSGALALANGHVKTD
Protein: SD07194p (Q95TG6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKMYQNIHLRILGLLNNSFGAPNTERAVTKCFFDIREEVRYNVEAARALITSHFVNLNQFDGMLRDCMDNGNNYVAISFGIALLERLIMDDRVINIVSDNEFMATVELLGRLTQHRHRYPECIVNAIDTLWSGNFNSSSDYSPFNGNDRYLSGASHYIHSGMHHVRSCDTDDPPGLQEKTEFLLKDWVALYTQQNQQSTRDARNFGAFVQKMNTYGILKTDDLITRFFRQATHICTDVVYRMFAEPSLPINQAKNKIFQWIDAFVHLIAMLVRHSGEAGNPTTKINLLNKVLGIVLGTLIKDHEMRGVSFQQVGYHRFFMMLFMELCTADVILESLMHSIVSAFAYTYHLLNPSVAPGFCFAWLELISHRVFLGRILVQIPGQKGWPLYAQLLQDLFKYLAPFLRNTELGKPVQLLYKGTLRVLLVLLHDFPEFLCDYHFGFCDTIPPNCVQMRNIILSAFPRNMRLPDPFTPNLKVDMLSDSSNAPKVLSSYIMNIQPANFKKDLDSYLKARAPVTFLSELRGHLQVTSEPGTRYNMALMNALVMYVGTQAIALIRKKLCAQHLEHSTQRPHGYLPESCC
Protein: N-alpha-acetyltransferase 30 (EC 2.3.1.256) (N-terminal acetyltransferase C complex catalytic subunit mak3 homolog) (NatC catalytic subunit) (O74311)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of the NatC N-terminal acetyltransferase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- N-terminal acetyltransferase A complex catalytic subunit ard1
- N-terminal acetyltransferase B complex catalytic subunit naa20
- N-terminal acetyltransferase B complex subunit arm1
- Uncharacterized N-acetyltransferase C663.13c
- N-terminal acetyltransferase A complex subunit nat1
- N-alpha-acetyltransferase 40
- N-terminal acetyltransferase A complex subunit-like protein C418.02
- Small nuclear ribonucleoprotein E
Sequence:
MVTIVPYSHQYLKDICQLIQKDLSEPYSKYVYRYFVHQWPEFSFVALDNDRFIGAVICKQDVHRGTTLRGYIAMLAIVKEYRGQGIATKLTQASLDVMKNRGAQEIVLETEVDNEAAMSFYERLGFCRYKRLYRYYLNGTDAFRYILYPN
Protein: Nuclear pore complex protein Nup85 (C8VK94)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567, ECO:0000256|RuleBase:RU365073}.
Interaction partners:
- Nuclear pore complex protein An-Nup120
- Peptidase S59 domain-containing protein
- Uncharacterized protein
Sequence:
MSFPTFNFGGNNGLATPGKSRNIFGNGEPPSPSNSFTPQGPPPSTIYGGSQMSARSPANSNPIFNRSELLNDSIFGSSVDSPDFASRTKQTAAAKRFTASESLFDVSRGPSFDESTNWGASNGFQPHMSGGLGADDGKSMEEDEDEDEAEQTGKTRGSGLNFLDSHMSSTGPSSIPAQRKPIYANPGNAKRPKLDEKWANQSPLRNAKLSPKKNSTIPAIVRNFAARTRKATVDEPFDFIIRTEDEISRMYEETRQTQYNNEYLQETIGKICADLSTVWYNSSESKASGTVIGPGDNAANSTKAGFLGALLLQLHHPPATKSTGFPNTFGLAAPRYTFGGRSASAPIPKVLLDWLNVNKPLSDEITALKQVEPDPTASPSFWEIVIAAVLRGQLSEASQILRSADFNYARSALEDGLPQAGYRGVQLQNIQRCINKALQVLEACPSVHNDNWDARDAEWSLYRKRVHTAISDLEEFAEGEEQPAPAPATGNTFQAINFGLGSNPFQGPSFTESARMAESRVPWTIYQNLRSVYRIILGDPAAIMNYAESWVEATIGLTVWWDGEDDEEASPPPFLRRGQSPSNDPYLRRLSLAFKHATSTEKDEKGFRYNSLSGIEVGLAAVFEGDVAGVLELLQTWSLCVAAAVAEISSVGGWLETKSNAKPPGLSDNDLMVLSYNQNDAPAGVSRDDVLSAYATGLSERPSIGNEHEGREGWELALEVLSRLDDSQKMQKSVSELLDKLPLDTAEQMDKVVLLCSELGLNKEGRRVSERYGDLTVSNSEEYGLALVCYARAHNRRKVKSVVDLLISYSLVQSRAYPASSDLDEQLRTLIREPKTCLSAIAHADEEAASILQFYFSGYATLRRFYETRDEAVNLPAGQKPRYKPLARRRAAAQALVAVISSAADSIYGGLYDPDRDSAIQVDGLLALLGEALPFVHQSSSILNPSQQFAILSAIEDLETVTPRVYAQCEECFRSTLLEYYSKQAGKASDSYVLPPSPRALLKKSVSSLTASSTFSIIGSDMLGARTRSSSGSAEGSGVLVPRDCEKTPLVREWDWRAGLPEDTKGEDVLRMLRLGLANGLTLEALGRAY
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial (Complex I-20kD) (NADH-ubiquinone oxidoreductase 20 kDa subunit) (A0A8I6AES7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
VLFSLAPGLLSVRILGLRTGTVAQLRRAHQSVAATGSPSSTQSAVSKAGAGAVVPKPSHLPRSRAEYVVTKLDDLINWARRSSLWPMTFGLACCAVEMMHMAAPRYDMDRFGVVFRASPRQADVMIVAGTLTNKMAPALRKVYDQMPEPRYVVSMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALLYGILQLQRKIKREQKLKIWYRR
Protein: Lysine-specific demethylase 2B (EC 1.14.11.27) (F-box and leucine-rich repeat protein 10) (F-box protein FBL10) (F-box/LRR-repeat protein 10) (JmjC domain-containing histone demethylation protein 1B) ([Histone-H3]-lysine-36 demethylase 1B) (Q6P1G2)
Organism: Mus musculus (Mouse)
Function: Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of histone H3, thereby playing a central role in histone code. Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated H3 'Lys-36' residue while it has weak or no activity for mono- and tri-methylated H3 'Lys-36'. Preferentially binds the transcribed region of ribosomal RNA and represses the transcription of ribosomal RNA genes which inhibits cell growth and proliferation (By similarity). May also serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q8NHM5}. Nucleus {ECO:0000250|UniProtKB:Q8NHM5}. Chromosome {ECO:0000250|UniProtKB:Q8NHM5}.
Interaction partners:
- Polycomb group RING finger protein 1
- S-phase kinase-associated protein 1
- E3 ubiquitin-protein ligase RING2
- RING1 and YY1-binding protein
- E3 ubiquitin-protein ligase RING1
- YY1-associated factor 2
- Polycomb complex protein BMI-1
- Chromobox protein homolog 8
- Polycomb group RING finger protein 6
- BCL-6 corepressor
Sequence:
MEAEKDSGRRLRAIDRQRYDENEDLSDVEEIVSVRGFSLEEKLRSQLYQGDFVHAMEGKDFNYEYVQREALRVPLVFRDKDGLGIKMPDPDFTVRDVKLLVGSRRLVDVMDVNTQKGTEMSMSQFVRYYETPEAQRDKLYNVISLEFSHTKLEHLVKRPTVVDLVDWVDNMWPQHLKEKQTEATNALAEMKYPKVKKYCLMSVKGCFTDFHIDFGGTSVWYHVFRGGKIFWLIPPTLHNLALYEEWVLSGKQSDIFLGDRVERCQRIELKQGYTFFIPSGWIHAVYTPVDSLVFGGNILHSFNVPMQLRIYEIEDRTRVQPKFRYPFYYEMCWYVLERYVYCVTQRSYLTQEYQRELMLIDAPRKTSVDGFSSDSWLDMEEESCEQQPQEEEEEEEDKEEEGDGADKTPKPPTDDPTSPTSTPPEDQDSTGKKPKAPAIRFLKRTLSNESEESVKSTSMPTDDPKTPTGSPATEVSTKWTHLTEFELKGLKALVEKLESLPENKKCVPEGIEDPQALLEGVKNVLKEHVDDDPTLAITGVPVVSWPKKTAKNRVVGRPKGKLGPASAVKLAANRTTAGARRRRTRCRKCEACLRTECGECHFCKDMKKFGGPGRMKQSCIMRQCIAPVLPHTAVCLVCGEAGKEDTVEEEEGKFNLMLMECSICNEIIHPGCLKIKESEGVVNDELPNCWECPKCNHAGKTGKQKRGPGFKYASNLPGSLLKEQKMNRDNKEGQEPAKRRSECEEAPRRRSDEHPKKVPADGILRRKSDDVHLRRKRKYEKPQELSGRKRASSLQTSPGSSSHLSPRPPLGSSLSPWWRSSLTYFQQQLKPGKEDKLFRKKRRSWKNAEDRLSLANKPLRRFKQEPEDDLPEAPPKTRESDQSRSSSPTAGPSTEGAEGPEEKKKVKMRRKRRLVNKELSKELSKELNHEIQKTESTLAHESQQPIKSEPESENDEPKRPLSHCERPHRFSKGLNGTPRELRHSLGPGLRSPPRVMSRPPPSASPPKCIQMERHVIRPPPISPPPDSLPLDDGAAHVMHREVWMAVFSYLSHRDLCVCMRVCRTWNRWCCDKRLWTRIDLNRCKSITPLMLSGIIRRQPVSLDLSWTNISKKQLSWLINRLPGLRDLVLSGCSWIAVSALCSSSCPLLRTLDVQWVEGLKDAQMRDLLSPPTDNRPGQMDNRSKLRNIVELRLAGLDITDVSLRLIIRHMPLLSKLQLSYCNHINDQSINLLTAVGTTTRDSLTEVNLSDCNKVTDLCLSFFKRCGNICHIDLRYCKQVTKEGCEQFIAEMSVSVQFGQVEEKLLQKLS
Protein: Uncharacterized protein (Q57ZM4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Transmembrane protein
- Uncharacterized protein
- Uncharacterized protein
- ATP synthase subunit beta
- ATPase subunit 9, putative
- Uncharacterized protein
- ATP synthase alpha chain
Sequence:
MVYTRWKCDRLPVFQLKLFTQEYPMHAAVGIFTIIFLWKHMSHCSEETERKYGWWAGYPYWRDPIARRNETKYKQMIINNDVDITHPKWTGCSVEQLEELSRVV
Protein: GTP diphosphokinase CRSH3, chloroplastic (EC 2.7.6.5) (Calcium-activated RelA/Spot homolog 3) (OsCRSH3) (ppGpp synthetase CRSH3) (Q75IS2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Possesses calcium-dependent ppGpp (guanosine 3'-diphosphate 5'-diphosphate) synthetase activity in vitro and is able to functionally complement E.coli relA mutants. May be involved in a rapid plant ppGpp-mediated response to pathogens and other stresses.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Nucleoside diphosphate kinase
- Nucleoside diphosphate kinase 1
- Inosine triphosphate pyrophosphatase
- Probable monofunctional riboflavin biosynthesis protein RIBA 3
- Probable bifunctional riboflavin biosynthesis protein RIBA 1, chloroplastic
- Probable bifunctional riboflavin biosynthesis protein RIBA 2, chloroplastic
- Molybdenum cofactor biosynthesis protein 1
- Os04g0662700 protein
- Putative GTP diphosphokinase RSH1, chloroplastic
- Nucleoside diphosphate kinase
Sequence:
MANAGVNETVAVAVAIDAPGVGHDHGAAGEVRRPSTRRLAPAGSGGRLMAELLGVFNGLTERMGEDVATSSSSRLLFRALKLALPALRDGGGDGGGGQSVSRALVVAASLADLQMDAEVISAGMVRGALDTGALAMADVEAQLGASAAGLVEESLKVKRAPSEVDVADEEAASALRKRCLSSYDIRAVILELAVKLDAMKHLDVLPKHQQRTTSLEVLKVFALLAHAVGAGELSLELEDLSFQRLYPQAYAHIDQWLSSQEDDCKRVIAASKEELLRALTADDELRCTVTGVDVMGRYKSRFSTMKKLVKDGRRPEDVNDILGMRVILDPRPGGGGGGDGDGGDRACLRTHEVIKAMWKDVPARTKDYITRPKGNGYRSLHVAVDMSEPGPEGKKRPLMEIQVRTREMDMAAVGGQASHALYKGGLTDPEEAKRLKAIMLAAAEVAAQHLRDEPAGDGGQTTAAASAATAGNVERAFQLLDKNGDGRISMEELTEIMEDLGAGGHDAEELMRLLDANSDGSLSSDEFALFQKRVKLKTKLENKDDEYKEILKQKLQKVDDTGLIHVYRKNLSDKLVLV
Protein: E3 ubiquitin-protein ligase RZFP34 (EC 2.3.2.27) (CHY zinc-finger and RING protein 1) (RING zinc-finger protein 34) (RZFP34 protein homolog) (AtRZPF34) (Q9FFB6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses E3 ubiquitin-protein ligase activity in vitro. Mediates mainly 'Lys-48'-linked polyubiquitination. Promotes abscisic acid (ABA)-induced stomatal closure, reactive oxygen species (ROS) production and drought tolerance. Involved in the regulation of stomatal aperture.
Subcellular location: Nucleus {ECO:0000269|PubMed:26508764}. Cytoplasm {ECO:0000269|PubMed:26508764}. Endoplasmic reticulum {ECO:0000269|PubMed:26508764}.
Interaction partners:
- At1g25400
- Expressed protein)
- BTB/POZ and TAZ domain-containing protein 5
- Uncharacterized protein F12A4.5
Sequence:
MDMGFHENEQNQEFANLMEIGSGHYGCSHYRRRCKIRAPCCDEIFDCRHCHNEAKDSLHIEQHHRHELPRHEVSKVICSLCETEQDVQQNCSNCGVCMGKYFCSKCKFFDDDLSKKQYHCDECGICRTGGEENFFHCKRCRCCYSKIMEDKHQCVEGAMHHNCPVCFEYLFDSTRDITVLRCGHTMHLECTKDMGLHNRYTCPVCSKSICDMSNLWKKLDEEVAAYPMPKMYENKMVWILCNDCGSNTNVRFHLIAHKCSSCGSYNTRQTQRGSDSHSCSSGMPQVVGSTG
Protein: Cytochrome c oxidase subunit 6A2, mitochondrial (Cytochrome c oxidase polypeptide VIa-heart) (COXVIAH) (Cytochrome c oxidase polypeptide VIb) (P07471)
Organism: Bos taurus (Bovine)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules unsing 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. Plays a role in the assembly and stabilization of complex IV (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 7A1, mitochondrial
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome b-c1 complex subunit 9
- Cytochrome b-c1 complex subunit 7
- Cytochrome b
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome c1, heme protein, mitochondrial
Sequence:
MALPLKSLSRGLASAAKGDHGGTGARTWRFLTFGLALPSVALCTLNSWLHSGHRERPAFIPYHHLRIRTKPFSWGDGNHTFFHNPRVNPLPTGYEKP
Protein: Similar to part of disease resistance protein (Toll-Interleukin-Resistance (TIR) domain-containing protein) (Virus resistance protein, putative) (Q9SSN6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Leucine-rich repeat
- Leucine-rich repeat
- Leucine-rich repeat
- Anthocyanin-related membrane protein 2
- Probable methyltransferase PMT15
- Leucine-rich repeat
- AT3g19030/K13E13_15
- Sulfite exporter TauE/SafE family protein 2
- Receptor protein kinase-like protein
- WAT1-related protein At4g01440
Sequence:
MSSATATYNYDVFLSFRGPDTRRKFISFLYKELVGRDIRTFKDDKELENGQMISPELILAIEDSRFAVVVVSVNYAASSWCLDELVKIMDIQKNKGSITVMPIFYGVNPCHLRRQIGDVAEQFKKHEAREKDLEKVLKWRQALAALADISGDCSGEDDSKLVDVIADKISKELMIVTRISNGRNLVGIDKHMNELNRLMDLNSNKGKRMVGIWARGGSCRSALAKYVYQTSCQHFDSHCFLGNVKRICQGNYFESHLHKEFLDNIQGENSSKQSLKKQKVLLVADDVDKLEQLDALAGDFSGFGPGSVVIITTKDKQLLISYGIQLVYEAEFLTFQKFCRSFRSLAFKKRDDISAAFEWALYI