wanglab/gogpt-training-data huggingface dataset:
Protein: Natural resistance-associated macrophage protein 2 isoform 2 (Solute carrier family 11 (Proton-coupled divalent metal ion transporters), member 2, isoform CRA_b) (A0A0X8GKR4)
Organism: Homo sapiens (Human)
Subcellular location: Late endosome membrane {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004107}. Lysosome membrane {ECO:0000256|ARBA:ARBA00004155}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004155}.
Interaction partners:
Sequence:
MVLGPEQKMSDDSVSGDHGESASLGNINPAYSNPSLSQSPGDSEEYFATYFNEKISIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNIESDLQSGAVAGFKLLWILLLATLVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRVILWLMVELAIIGSDMQEVIGSAIAINLLSVGRIPLWGGVLITIADTFVFLFLDKYGLRKLEAFFGFLITIMALTFGYEYVTVKPSQSQVLKGMFVPSCSGCRTPQIEQAVGIVGAVIMPHNMYLHSALVKSRQVNRNNKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFGKTNEQVVEVCTNTSSPHAGLFPKDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTGTYSGQFVMEGFLNLKWSRFARVVLTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQLPFALIPILTFTSLRPVMSDFANGLGWRIAGGILVLIICSINMYFVVVYVRDLGHVALYVVAAVVSVAYLGFVFYLGWQCLIALGMSFLDCGHTCHLGLTAQPELYLLNTMDADSLVSR
Protein: Homeobox protein cut-like 1 (CCAAT displacement protein) (CDP) (Homeobox protein cux-1) [Cleaved into: CDP/Cux p110] (P53564)
Organism: Mus musculus (Mouse)
Function: Transcription factor involved in the control of neuronal differentiation in the brain. Regulates dendrite development and branching, and dendritic spine formation in cortical layers II-III. Also involved in the control of synaptogenesis (Probable). In addition, it has probably a broad role in mammalian development as a repressor of developmentally regulated gene expression. May act by preventing binding of positively-activing CCAAT factors to promoters. Component of nf-munr repressor; binds to the matrix attachment regions (MARs) (5' and 3') of the immunoglobulin heavy chain enhancer. Represses T-cell receptor (TCR) beta enhancer function by binding to MARbeta, an ATC-rich DNA sequence located upstream of the TCR beta enhancer. Binds to the TH enhancer; may require the basic helix-loop-helix protein TCF4 as a coactivator.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00374, ECO:0000269|PubMed:15371550}.
Interaction partners:
- T-box brain protein 1
- B-cell lymphoma/leukemia 11B
- DNA-binding protein SATB2
- Forkhead box protein P2
- Eomesodermin homolog
Sequence:
MLCVAGAKLKRELDATATVLANRQDESEQSRKRLIEQSREFKKNTPEDLRKQVAPLLKSFQGEIDALSKRSKEAEAAFLTVYKRLIDVPDPVPALDVGQQLEIKVQRLHDIETENQKLRETLEEYNKEFAEVKNQEVTIKALKEKIREYEQTLKSQAETIALEKEQKLQNDFAEKERKLQETQMSTTSKLEEAEHKLQTLQTALEKTRTELFDLKTKYDEETTAKADEIEMIMTDLERANQRAEVAQREAETLREQLSSANHSLQLASQIQKAPDVAIEVLTRSSLEVELAAKEREIAQLVEDVQRLQASLTKLRENSASQISQLEQQLNAKNSTLKQLEEKLKGQADYEEVKKELNTLKSMEFAPSEGAGTQDSTKPLEVLLLEKNRSLQSENATLRISNSDLSGSARRKGRDQPESRRPGPLPASPPPQLPRNTGEQVSNTNGTHHFSPAGLSQDFFSSNLASPSLPLASTGKFALNSLLQRQLMQSFYSKAMQEAGSTSTIFSTGPYSTNSISSPSPLQQSPDVNGMAPSPSQSESAGSISEGEEIDTAEIARQVKEQLIKHNIGQRIFGHYVLGLSQGSVSEILARPKPWNKLTVRGKEPFHKMKQFLSDEQNILALRSIQGRQRENPGQSLNRLFQEVPKRRNRSEGNITTRIRASETGSDEAIKSILEQAKRELQVQKTAEPVQTSSTSSSGNSDDAIRSILQQARREMEAQQAALDPALKPAPLSQPDLTILTPKHLSASPMSTVSTYPPLAISLKKTPAAPETSTAALPSAPALKKEAQDVPTLDPPGSADAAQGVLRPMKSELVRGSTWKDPWWSPIQPERRNLTSSEETKADETTASGKERAGSSQPRAERSQLQGPSASAEYWKEWPSAESPYSQSSELSLTGASRSETPQNSPLPSSPIVPMAKPAKPSVPPLTPEQYEVYMYQEVDTIELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREPFIRMQLWLNGELGQGVLPVQGQQQGPVLHSVASLQDPLQQGCVSSESTPKTSASCSPAPESPMSSSESVKSLTELVQQPCPAIETSKEGKPPEPSDPPASDSQPTTPLPLSGHSALSIQELVAMSPELDTYGITKRVKEVLTDNNLGQRLFGETILGLTQGSVSDLLARPKPWHKLSLKGREPFVRMQLWLNDPNNVEKLMDMKRMEKKAYMKRRHSSVSDSQPCEPPSVGIDYSQGASPQPQHQLKKPRVVLAPEEKEALKRAYQQKPYPSPKTIEELATQLNLKTSTVINWFHNYRSRIRRELFIEEIQAGSQGQAGASDSPSARSSRAAPSSEGDSCDGVEATDAEEPGGNIVATKSQGGLAEVAAAPADREEATQPAEKAKAQPLCSGTPGQDDGEDASRPRPLPEGLADAPAPVPSLAAPAAGEDAATSATAPATATEAPGAARAGPAERSSALPSTSAPANAPARRPSSLQSLFGLPEAAGARDNPVRKKKAANLNSIIHRLEKAASREEPIEWEF
Protein: Hydroxamate-type ferrisiderophore receptor (Q0WI86)
Organism: Yersinia pestis
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}.
Interaction partners:
- Previously sequenced as Yersinia pestis yersiniabactin biosynthetic protein Irp2 TR:Q9Z399
- Putative membrane protein
- TonB protein
- Irp1 protein
- Fe/B12 periplasmic-binding domain-containing protein
- Siderophore biosysnthesis protein
- Similar to Pseudomonas aeruginosa hypothetical protein PA1508 TR:AAG04897
- Hypothetical protein
Sequence:
MFMRSTLIPSTFILSTLLLPAVVLAEDTIIVERNRSQTDSYQATTSVTANRSPANIIDTPQNVTVVTHPVLEDYDVTNLGEALYFVSGITQSNTLGGTQDALIKRGFGNNRDGSILHDGIRSIQARNFTPTSERVEVLKGPSSMLYGMNEPGGLINVISKKPQLDPHVHLEANASSFKGGGGQLDVTGPLGESGFAGRLIIDHQETDYWRNFGRNRQTVVAPSLDWYGENTTVHLAWERMEYLVPFDRGTVIDPRTGKPVDTPRDRRFDESYNATRGDQDTVTFSINHDLNEFWSTQLNYAFSRNSYSDNQARATAFNAETGVLTRQSDATANAKSHSQAVQWVVNGDLDWGFTHHQLMFGIDYEARRVFRGDMIRGSKNNGFNVYDPIYGTLPPSTAVSAADSDQRENIDSRALFIQDSMRLNEHWLLLGGLRYDSFDVMAGKGRPFKKNTDSSDSRLVPRAGVVYNLNDWSSLYVSYTESFKPNVSIATAIDALPPEYGKSWEAGYKIDINNRVTGTLAVYDIHKRNIMVSELVDGETVTRTAGKARSRGLELDMAGKVTDSLSLIGSYAYTDARLTEDPDNNGNDLPNVARHTAALFLSRDFGSTSLISGDEVKAGIGARYVGKRAGDAANSFWLDNYTVADAFIAWKMPLSGYQLKWQLNVKNLFDKTYYPSSANNLRIAIGEPRQVVLQGSIDF
Protein: Putative cystathione gamma lyase (EC 4.4.1.1) (E9AFE7)
Organism: Leishmania major
Interaction partners:
- cystathionine beta-synthase
- Putative methylenetetrahydrofolate reductase
- cysteine synthase
Sequence:
MSSQQHLVSDFTAGSGSWLPQSQGFDTLQVHAGVRPDPVTGAILTPIYQSTTFVQESINSYQAKGYSYTRSANPTVAVLEQKLCALENGSYCTVYNTGMAATTTAISSFMNAGDHAILTNCCYGGTNRACRVFFSRLGMEFTFVDMRDPQNVIDSIKPNTKLVISETPANPTLILIDVAAVSKICKERGIVHMCDNTFATAYIMRPLDHGADVTLISTTKYVDGHDMTVGGALVTNSKELDAKVRLTQNILGNVMSPQVAFLQLQTVKTMSLRVTKQSHNAQKIAEFLETHRAVDRVVYPGLASHPQKELADRQHRNNLHGGMLWFEVKGGTAAGRRLMDTVPRPWSLCENLGASESIITCPSVMTHANMTSEDRMKVGITDGFVRVSCGIEDVDDLIAALKVAMDALV
Protein: LIM and senescent cell antigen-like-containing domain protein (A0A8I5ZR99)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|PIRNR:PIRNR038003}. Cell membrane {ECO:0000256|PIRNR:PIRNR038003}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR038003}.
Interaction partners:
Sequence:
LTGVNMANALASATCERCKGGFDPAEKIVNSNGELYHEQCFVCAQCFQQFPEGLFYEFEGRKYCEHDFQMLFAPCCHQCGEFIIGRVIKAMNNSWHPECFRCDLCQEVLADIGFVKNAGRHLCRPCHNREKARGLGKYICQKCHAIIDEQPLIFKNDPYHPDHFNCANCGKELTADARELKGELYCLPCHDKMGVPICGACRRPIEGRVVNAMGKQWHVEHFVCAKCEKPFLGHRHYERKGLAYCETHYNQLFGDVCFHCNRVIEGDGMYLWVDGTTLNKFVEFDMKPVCKKCYEKFPLELKKRLKKLSETLGRK
Protein: WD repeat-containing protein 19 (Intraflagellar transport 144 homolog) (Q8NEZ3)
Organism: Homo sapiens (Human)
Function: As component of the IFT complex A (IFT-A), a complex required for retrograde ciliary transport and entry into cilia of G protein-coupled receptors (GPCRs), it is involved in cilia function and/or assembly. Essential for functional IFT-A assembly and ciliary entry of GPCRs. Associates with the BBSome complex to mediate ciliary transport (By similarity).
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:Q3UGF1}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q3UGF1}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:Q3UGF1}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:32323121}. Note=Localizes to photoreceptor connecting cilia, to the base of motile cilia in brain ependymal cells and to the base of and along primary cilia in kidney cells. Localizes at the sperm neck and flagellum (PubMed:32323121). {ECO:0000250|UniProtKB:Q3UGF1, ECO:0000269|PubMed:32323121}.
Interaction partners:
- WD repeat-containing protein 35
- Intraflagellar transport protein 43 homolog
- Tetratricopeptide repeat protein 21B
- Intraflagellar transport protein 140 homolog
- Intraflagellar transport protein 122 homolog
- Intraflagellar transport protein 27 homolog
- Intraflagellar transport protein 80 homolog
- Tubby-related protein 3
- Intraflagellar transport protein 172 homolog
- Intraflagellar transport protein 52 homolog
Sequence:
MKRIFSLLEKTWLGAPIQFAWQKTSGNYLAVTGADYIVKIFDRHGQKRSEINLPGNCVAMDWDKDGDVLAVIAEKSSCIYLWDANTNKTSQLDNGMRDQMSFLLWSKVGSFLAVGTVKGNLLIYNHQTSRKIPVLGKHTKRITCGCWNAENLLALGGEDKMITVSNQEGDTIRQTQVRSEPSNMQFFLMKMDDRTSAAESMISVVLGKKTLFFLNLNEPDNPADLEFQQDFGNIVCYNWYGDGRIMIGFSCGHFVVISTHTGELGQEIFQARNHKDNLTSIAVSQTLNKVATCGDNCIKIQDLVDLKDMYVILNLDEENKGLGTLSWTDDGQLLALSTQRGSLHVFLTKLPILGDACSTRIAYLTSLLEVTVANPVEGELPITVSVDVEPNFVAVGLYHLAVGMNNRAWFYVLGENAVKKLKDMEYLGTVASICLHSDYAAALFEGKVQLHLIESEILDAQEERETRLFPAVDDKCRILCHALTSDFLIYGTDTGVVQYFYIEDWQFVNDYRHPVSVKKIFPDPNGTRLVFIDEKSDGFVYCPVNDATYEIPDFSPTIKGVLWENWPMDKGVFIAYDDDKVYTYVFHKDTIQGAKVILAGSTKVPFAHKPLLLYNGELTCQTQSGKVNNIYLSTHGFLSNLKDTGPDELRPMLAQNLMLKRFSDAWEMCRILNDEAAWNELARACLHHMEVEFAIRVYRRIGNVGIVMSLEQIKGIEDYNLLAGHLAMFTNDYNLAQDLYLASSCPIAALEMRRDLQHWDSALQLAKHLAPDQIPFISKEYAIQLEFAGDYVNALAHYEKGITGDNKEHDEACLAGVAQMSIRMGDIRRGVNQALKHPSRVLKRDCGAILENMKQFSEAAQLYEKGLYYDKAASVYIRSKNWAKVGDLLPHVSSPKIHLQYAKAKEADGRYKEAVVAYENAKQWQSVIRIYLDHLNNPEKAVNIVRETQSLDGAKMVARFFLQLGDYGSAIQFLVMSKCNNEAFTLAQQHNKMEIYADIIGSEDTTNEDYQSIALYFEGEKRYLQAGKFFLLCGQYSRALKHFLKCPSSEDNVAIEMAIETVGQAKDELLTNQLIDHLLGENDGMPKDAKYLFRLYMALKQYREAAQTAIIIAREEQSAGNYRNAHDVLFSMYAELKSQKIKIPSEMATNLMILHSYILVKIHVKNGDHMKGARMLIRVANNISKFPSHIVPILTSTVIECHRAGLKNSAFSFAAMLMRPEYRSKIDAKYKKKIEGMVRRPDISEIEEATTPCPFCKFLLPECELLCPGCKNSIPYCIATGRHMLKDDWTVCPHCDFPALYSELKIMLNTESTCPMCSERLNAAQLKKISDCTQYLRTEEEL
Protein: Methionine--tRNA ligase, mitochondrial (EC 6.1.1.10) (Methionyl-tRNA synthetase) (MetRS) (P22438)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the attachment of methionine to tRNA(Met) in the mitochondrion.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:2645139}.
Interaction partners:
- tRNA-aminoacylation cofactor ARC1
- Isoleucine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, mitochondrial
- Glutamate--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, mitochondrial
Sequence:
MQCRSIVHRLYSKVSHVTTPIFYPNAKPHLGHLYSSLLSDVYHRWQLFKGNLSFFTTGTDEHGLKIQCASESNGFDQPKKFVDKLYPEFVQLDKIYGINYTRFIRTTDPDHIENVMKLWELCLKNGYIYMGEHKGWYSISDETFYPESKVIKDPKNDGKYLNTESKNEVVYQSETNYFFRLSLFNKKIVDHIRKNPDFIFPASKRDQILKELETGGTLPDLSISRPSARLKWGIPTPNDPSQKVYVWFDALCNYLSSIGGIPSILSNATEVVSRHYSDKSNVKGQLLIPYPKEVQRNTIHVIGKDIAKFHTVYWPSFLLAAGLPLPRQIVVHGHWLCNGMKMSKSLGNVVDPIDMARYYGADIVRWFLLENSKLEEDGDFQEAKLYETRELLVSKWGNLINRCCGSKFNIERAVMKFSDKANFQFQEIFQNEPIVSERIENLAKLLNKSQEVFDEKIAIFQYPQLLRHVWSIINDANTLVQNSKPWERELDQQDNIIFLAMETSRILSILCQSIIPSLSQSFLDRIDVSKEKRTINYARLGSDKTYGKQSNKKGREVPLKKIPFRLQEEQTNMRS
Protein: Actin-2 (EC 3.6.4.-) (Actin II) (Q8ILW9)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm. Polymerizes into longer and more stable actin filaments compared to ACT1/actin-1. Has ATPase activity. ATP hydrolysis leads to the formation of a stable intermediate ADP-inorganic phosphate (Pi) actin, which is followed by the release of Pi. ATP hydrolysis affects filament stability; ADP-bound actin depolymerizes much faster than ATP- or ADP-Pi-bound actin. Plays an essential role in male gametocyte development in the mosquito midgut, functioning in several processes including male gametocyte egress from host erythrocytes, formation of a beating flagellum and relocalization of ACT1/actin-1 to the cytoplasm. On the basal side of the mosquito midgut epithelium, required for the development of ookinetes into sporogonic oocysts.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q4YU79}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8I4X0}. Note=Prior to gametocyte activation in the mosquito midgut, localizes to the cytoplasm. Following gametocyte activation, localizes to a ring around the nucleus. {ECO:0000250|UniProtKB:Q4YU79}.
Interaction partners:
- Cofilin/actin-depolymerizing factor homolog 2
Sequence:
MSEEAVALVVDNGSGMVKSGLAGDDAPKCVFPSIVGRPKMPNIMIGMEQKECYVGDEAQNKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVSPEEHPVLLTEAPLNPKTNREKMTQIMFETFDVPAMYVSIQAILSLYASGRTTGIVLDSGDGVSHTVPIYEGYVLPHAINRIDMAGRDLTYHMMKLFTERGHTFTTTAEREIVRDIKEKLCYIAMDYDEELKRSEEHSDEIEEIYELPDGNLITVGSERFRCPEALFNPTLIGRECPGLHITAYQSIMKCDIDIRKELYNNIVLSGGTTMYNNIGERLTKEMTNLAPSSMKIKVIAPPERKYSVWIGGSILSSLSTFQQMWITKEEYEDSGPSIVHRKCF
Protein: Keratin, type I cuticular Ha1 (Hair keratin, type I Ha1) (Keratin-31) (K31) (Q15323)
Organism: Homo sapiens (Human)
Interaction partners:
- Keratin, type I cuticular Ha3-I
- Keratin, type II cytoskeletal 6A
Sequence:
MPYNFCLPSLSCRTSCSSRPCVPPSCHSCTLPGACNIPANVSNCNWFCEGSFNGSEKETMQFLNDRLASYLEKVRQLERDNAELENLIRERSQQQEPLLCPSYQSYFKTIEELQQKILCTKSENARLVVQIDNAKLAADDFRTKYQTELSLRQLVESDINGLRRILDELTLCKSDLEAQVESLKEELLCLKSNHEQEVNTLRCQLGDRLNVEVDAAPTVDLNRVLNETRSQYEALVETNRREVEQWFTTQTEELNKQVVSSSEQLQSYQAEIIELRRTVNALEIELQAQHNLRDSLENTLTESEARYSSQLSQVQSLITNVESQLAEIRSDLERQNQEYQVLLDVRARLECEINTYRSLLESEDCNLPSNPCATTNACSKPIGPCLSNPCTSCVPPAPCTPCAPRPRCGPCNSFVR
Protein: Importin-4 (Imp4) (Importin-4b) (Imp4b) (Ran-binding protein 4) (RanBP4) (Q8TEX9)
Organism: Homo sapiens (Human)
Function: Nuclear transport receptor that mediates nuclear import of proteins, such as histones, RPS3A, TNP2 and VDR. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates the nuclear import of the histone H3-H4 dimer when in complex with ASF1 (ASF1A or ASF1B). Mediates the ligand-independent nuclear import of vitamin D receptor (VDR). In vitro, mediates the nuclear import of human cytomegalovirus UL84 by recognizing a non-classical NLS.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16207705, ECO:0000269|PubMed:17682055}. Nucleus {ECO:0000269|PubMed:16207705, ECO:0000269|PubMed:17682055}.
Interaction partners:
- Histone H3.1
- GTP-binding nuclear protein Ran
- Histone H4
- Histone chaperone ASF1B
- Histone chaperone ASF1A
- Histone H3.3
- Histone H3.1t
- Histone H3-7
- Histone H3.2
- Histone H3.3C
Sequence:
MESAGLEQLLRELLLPDTERIRRATEQLQIVLRAPAALPALCDLLASAADPQIRQFAAVLTRRRLNTRWRRLAAEQRESLKSLILTALQRETEHCVSLSLAQLSATIFRKEGLEAWPQLLQLLQHSTHSPHSPEREMGLLLLSVVVTSRPEAFQPHHRELLRLLNETLGEVGSPGLLFYSLRTLTTMAPYLSTEDVPLARMLVPKLIMAMQTLIPIDEAKACEALEALDELLESEVPVITPYLSEVLTFCLEVARNVALGNAIRIRILCCLTFLVKVKSKALLKNRLLPPLLHTLFPIVAAEPPPGQLDPEDQDSEEEELEIELMGETPKHFAVQVVDMLALHLPPEKLCPQLMPMLEEALRSESPYQRKAGLLVLAVLSDGAGDHIRQRLLPPLLQIVCKGLEDPSQVVRNAALFALGQFSENLQPHISSYSREVMPLLLAYLKSVPLGHTHHLAKACYALENFVENLGPKVQPYLPELMECMLQLLRNPSSPRAKELAVSALGAIATAAQASLLPYFPAIMEHLREFLLTGREDLQPVQIQSLETLGVLARAVGEPMRPLAEECCQLGLGLCDQVDDPDLRRCTYSLFAALSGLMGEGLAPHLEQITTLMLLSLRSTEGIVPQYDGSSSFLLFDDESDGEEEEELMDEDVEEEDDSEISGYSVENAFFDEKEDTCAAVGEISVNTSVAFLPYMESVFEEVFKLLECPHLNVRKAAHEALGQFCCALHKACQSCPSEPNTAALQAALARVVPSYMQAVNRERERQVVMAVLEALTGVLRSCGTLTLKPPGRLAELCGVLKAVLQRKTACQDTDEEEEEEDDDQAEYDAMLLEHAGEAIPALAAAAGGDSFAPFFAGFLPLLVCKTKQGCTVAEKSFAVGTLAETIQGLGAASAQFVSRLLPVLLSTAQEADPEVRSNAIFGMGVLAEHGGHPAQEHFPKLLGLLFPLLARERHDRVRDNICGALARLLMASPTRKPEPQVLAALLHALPLKEDLEEWVTIGRLFSFLYQSSPDQVIDVAPELLRICSLILADNKIPPDTKAALLLLLTFLAKQHTDSFQAALGSLPVDKAQELQAVLGLS
Protein: DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) (PEP) (Plastid-encoded RNA polymerase subunit beta) (RNA polymerase subunit beta) (P0C502)
Organism: Oryza sativa subsp. indica (Rice)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase RpoA/D/Rpb3-type domain-containing protein
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase subunit
- Uncharacterized protein
- DNA-directed RNA polymerase subunit
- Uncharacterized protein
- DNA-directed RNA polymerase RBP11-like dimerisation domain-containing protein
- DNA-directed RNA polymerase III subunit RPC5
- RNA polymerase Rpb4/RPC9 core domain-containing protein
Sequence:
MLRNGNEGMSTIPGFSQIQFEGFCRFINQGLAEELEKFPTIKDPDHEISFQLFAKGYQLLEPSIKERDAVYESLTYSSELYVSARLIFGFDVQKQTISIGNIPIMNSLGTFIINGIYRIVINQILLSPGIYYRSELDHKGISIYTGTIISDWGGRSELAIDKKERIWARVSRKQKISILVLSSAMGSNLKEILDNVSYPEIFLSFPNAKEKKRIESKEKAILEFYQQFACVGGDLVFSESLCEELQKKFFQQKCELGRIGRRNMNRRLNLDIPQNSTFLLPRDVLAATDHLIGMKFETGILDDDDMNHLKNKRIRSVADLLQDQFGLALGRLQHAVQKTIRRVFIRQSKPTPQTLVTPTSTSILLITTYETFFGTYPLSQVFDQTNPLTQTVHGRKVSCLGPGGLTGRTASFRSRDIHPSHYGRICPIDTSEGINVGLTGSLAIHARIDHWWGSVESPFYEISEKAKKKKERQVVYLSPNRDEYYMIAAGNSLSLNRGIQEEQVVPARYRQEFLTIAWEQIHVRSIFPFQYFSIGGSLIPFIEHNDANRALMSSNMQRQAVPLSRSEKCIVGTGLERQTALDSRVSVIAEREGKIISTNSHKILLSSSGKTISIPLVTHRRSNKNTCMHQKPRVPRGKSIKKGQILAEGAATVGGELALGKNVLVAYMPWEGYNFEDAVLISERLVYEDIYTSFHIRKYEIQTDTTSQGSAEKITKEIPHLEEHLLRNLDRNGVVKLGSWVETGDILVGKLTPQIASESSYIAEAGLLRAIFGLEVSTSKETSLKLPIGGRGRVIDVKWIQRDPLDIMVRVYILQKREIKVGDKVAGRHGNKGIISKILPRQDMPYLQDGTPVDMVFNPLGVPSRMNVGQIFESSLGLAGDLLKKHYRIAPFDERYEQEASRKLVFSELYEASKQTKNPWVFEPEYPGKSRIFDGRTGDPFEQPVLIGKSYILKLIHQVDEKIHGRSTGPYSLVTQQPVRGRAKQGGQRIGEMEVWALEGFGVAHILQEILTYKSDHLIARQEILNATIWGKRVPNHEDPPESFRVLVRELRSLALELNHFLVSQKNFQVNREEV
Protein: Photosystem I chlorophyll a/b-binding protein 2, chloroplastic (Lhca2) (LHCI type III LHCA2) (Q9SYW8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated, here photosystem I.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:10818090}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I chlorophyll a/b-binding protein 3-1, chloroplastic
- Photosystem I reaction center subunit XI, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem I reaction center subunit III, chloroplastic
- Photosystem I reaction center subunit IV A, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A1
- Chlorophyll a-b binding protein 6, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A2
- Chlorophyll a-b binding protein 4, chloroplastic
Sequence:
MASSLCASSAIAAISSPSFLGGKKLRLKKKLTVPAVSRPDASVRAVAADPDRPIWFPGSTPPEWLDGSLPGDFGFDPLGLSSDPDSLKWNVQAEIVHCRWAMLGAAGIFIPEFLTKIGILNTPSWYTAGEQEYFTDKTTLFVVELILIGWAEGRRWADIIKPGSVNTDPVFPNNKLTGTDVGYPGGLWFDPLGWGSGSPAKLKELRTKEIKNGRLAMLAVMGAWFQHIYTGTGPIDNLFAHLADPGHATIFAAFTPK
Protein: Trihelix transcription factor ENAP2 (Trihelix DNA-binding protein ENAP2) (Agrobacterium tumefaciens VirF-interacting protein 5) (EIN2 nuclear associated protein 2) (Q9FFG0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription regulator (By similarity). Promotes histone acetylation during ethylene signaling in an EIN2-dependent manner, thus regulating positively ethylene-responsive genes (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:26571494, ECO:0000269|PubMed:27694846}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q8VZI9}.
Interaction partners:
Sequence:
METTTPQSKSSVSHRPPLGREDWWSEEATATLVEAWGNRYVKLNHGNLRQNDWKDVADAVNSRHGDNSRKKTDLQCKNRVDTLKKKYKTEKAKLSPSTWRFYNRLDVLIGPVVKKSAGGVVKSAPFKNHLNPTGSNSTGSSLEDDDEDDDEVGDWEFVARKHPRVEEVDLSEGSTCRELATAILKFGEVYERIEGKKQQMMIELEKQRMEVTKEVELKRMNMLMEMQLEIEKSKHRKRASASGKKNSH
Protein: Kelch-like protein 10 (Q6JEL2)
Organism: Homo sapiens (Human)
Function: May be a substrate-specific adapter of a CUL3-based E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins during spermatogenesis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Protamine-2
- Cullin-3
- Sperm protamine P1
Sequence:
MEMESAAASTRFHQPHMERKMSAMACEIFNELRLEGKLCDVVIKVNGFEFSAHKNILCSCSSYFRALFTSGWNNTEKKVYNIPGISPDMMKLIIEYAYTRTVPITPDNVEKLLAAADQFNIMGIVRGCCEFLKSELCLDNCIGICKFTDYYYCPELRQKAYMFILHNFEEMVKVSAEFLELSVTELKDIIEKDELNVKQEDAVFEAILKWISHDPQNRKQHISILLPKVRLALMHAEYFMNNVKMNDYVKDSEECKPVIINALKAMYDLNMNGPSNSDFTNPLTRPRLPYAILFAIGGWSGGSPTNAIEAYDARADRWVNVTCEEESPRAYHGAAYLKGYVYIIGGFDSVDYFNSVKRFDPVKKTWHQVAPMHSRRCYVSVTVLGNFIYAMGGFDGYVRLNTAERYEPETNQWTLIAPMHEQRSDASATTLYGKVYICGGFNGNECLFTAEVYNTESNQWTVIAPMRSRRSGIGVIAYGEHVYAVGGFDGANRLRSAEAYSPVANTWRTIPTMFNPRSNFGIEVVDDLLFVVGGFNGFTTTFNVECYDEKTDEWYDAHDMSIYRSALSCCVVPGLANVEEYAARRDNFPGLALRDEVKYSASTSTLPV
Protein: Gex-3-interacting protein 13 (P34478)
Organism: Caenorhabditis elegans
Interaction partners:
- L-serine-phosphatidylethanolamine phosphatidyltransferase
- Uncharacterized protein
- Metallo-beta-lactamase domain-containing protein 1
- TBCC domain-containing protein 1
- G-protein coupled receptors family 1 profile domain-containing protein
Sequence:
MTDCSSTLAALLPTADFTASLGNSDDHVDVSSFTTTSESTSPPYSSSEHHSPTDQRTETPTSDSGNASFSPENVATSFESSDRDASPDNLSTSSAHLNDLQEKGVVVDEELQRQLLRFHQDFKESLMENNQNTINMMSAAFNQQLFKQTLANLNTVTPQLPVNIPTGLPMPASPCTTAASAPSVESTPTKRKRQRRNPVWPYFDVIDGTARCKQCLYSTKSVFSTNLKVHLRSHHRPDYEKVIMAEDALNLNALLLSGNTSKLFNVDANRKRMPPMTSSILMTINKLANQQQNGEENPLNAVLRQTIANNGLQQHLQNVQTQLQAAQAAVQKQQQQQQQQQIQQQQQQQQQGAIPQFALNAANLAALNQLARNQMQPTPPPVPQVSQDNIINTLNFPAHIKQEIMNAPHGTDANGVPQPKRRRLRRHPVWVYFKDLEDRMVGCTNCEFRTGSAFSTNLKMHLKAHHKDDYEKVLQLEEEMRLEEGCFGPGNKFKTELIDYIRGGGNVTTPPTPNSSSFPSTPKTPQLVQQIISQSFARSQSPNVIQNGEIKIKKECEDDMFSGLSSTDKLAALVGIAGQEVKKEEAMPANFEEFRQRLLANSSLSSFLGQSTAQPIAVDLNGSVIASETKSPCSSNEDDRKQERDKALARLWADNETLLTNTHFREFVHCLAPEYEIPDVDILATSLVDQY
Protein: FAD-binding domain-containing protein (G8B709)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
Sequence:
MAVQAPSKTYGFQKAPIQLTFVVVGAGLGGVAASICLRLAGHRVILLEAATELGEVGAGIQIPPPSTKILKAIGVLDAVDKVSIHPHDILVKKYKGELLSTQNLVPYVSEKYDGMYLHIHRADYHKVLVDRAEELGVEIHTNSRVVDIDFEKATVTTATGKQYSGDVIVGYDGVRSQTRALLTGDSSGAYDTGDLAYRALIKVEDMKKVPGLEKFYANPNINFWWGPTMHIVMYFLHEGEICNVVALCPDTLPKGVLKQDASQEELLDLVKGWDQDLTTVFKLITSVSKWRLQDSRELKTWVNSKTGNFIILGDASHSTLPYLASGASQAVEDGAVLAGLFSKIESRDQIPQLLQMTENLRKWRSSQVVRGSHQCQDIYHLPDGELQEIRDSYLYDKQPELGCPNRFADPVFQDFLWGYNAFDEVERAWKEFKAGGNPTYTYPNLYKPKSSGEKDVSGGGAAATLAAGNTPAAPLSASG