wanglab/gogpt-training-data huggingface dataset:
Protein: Transcriptional regulatory protein RcsA (Colanic acid capsular biosynthesis activation protein A) (P0DMC9)
Organism: Escherichia coli (strain K12)
Function: Component of the Rcs signaling system, which controls transcription of numerous genes. Binds, with RcsB, to the RcsAB box to regulate expression of genes involved in colanic acid capsule synthesis.
Interaction partners:
- Transcriptional regulatory protein RcsB
- Phosphotransferase RcsD
- Sensor histidine kinase RcsC
- Outer membrane lipoprotein RcsF
- Transcriptional activator protein BglJ
- Lon protease
- Putative membrane protein IgaA homolog
- Transcriptional regulator GadE
- Putative polysaccharide export protein Wza
Sequence:
MSTIIMDLCSYTRLGLTGYLLSRGVKKREINDIETVDDLAIACDSQRPSVVFINEDCFIHDASNSQRIKLIINQHPNTLFIVFMAIANVHFDEYLLVRKNLLISSKSIKPESLDDILGDILKKETTITSFLNMPTLSLSRTESSMLRMWMAGQGTIQISDQMNIKAKTVSSHKGNIKRKIKTHNKQVIYHVVRLTDNVTNGIFVNMR
Protein: Rho-associated protein kinase (EC 2.7.11.1) (Q9VXE3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Ras-like GTP-binding protein Rho1
- Myosin regulatory light chain sqh
- Dishevelled associated activator of morphogenesis, isoform D
- Segment polarity protein dishevelled
- Protein diaphanous
- Frizzled
- Rho-related BTB domain containing, isoform B
- AT17867p
- Protein prickle
- Protein Shroom
Sequence:
MPAGRETVTKQRSMDVERRRRANTLEREMRDPTSICNVDCLLDTVSALVSDCDHESLRRLKNIEQYAAKYKPLAMQINQLRMNVEDFHFIKLIGAGAFGEVQLVRHKSSSQVYAMKRLSKFEMMKRPDSAFFWEERHIMAHANSEWIVQLHFAFQDAKYLYMVMDFMPGGDIVSLMGDYDIPEKWAIFYTMEVVLALDTIHNMGFVHRDVKPDNMLLDSYGHLKLADFGTCMRMGANGQVVSSNAVGTPDYISPEVLQSQGVDNEYGRECDWWSVGIFLYEMLFGETPFYADSLVGTYGKIMDHKNSLSFPPEVEISEQAKALIRAFLTDRTQRLGRYGIEDIKAHPFFRNDTWSFDNIRESVPPVVPELSSDDDTRNFEDIERDEKPEEVFPVPKGFDGNHLPFIGFTYTGDYQLLSSDTVDAESKEANVANSGAASNNHGHGHNHRHRPSNSNELKRLEALLERERGRSEALEQQDAGLRQQIELITKREAELQRIASEYEKDLALRQHNYKVAMQKVEQEIELRKKTEALLVETQRNLENEQKTRARDLNINDKVVSLEKQLLEMEQSYKTETENTQKLKKHNAELDFTVKSQEEKVRDMVDMIDTLQKHKEELGQENAELQALVVQEKNLRSQLKEMHKEAENKMQTLINDIERTMCREQKAQEDNRALLEKISDLEKAHAGLDFELKAAQGRYQQEVKAHQETEKSRLVSREEANLQEVKALQSKLNEEKSARIKADQHSQEKERQLSMLSVDYRQIQLRLQKLEGECRQESEKVAALQSQLDQEHSKRNALLSELSLHSSEVAHLRSRENQLQKELSTQREAKRRFEEDLTQLKSTHHEALANNRELQAQLEAEQCFSRLYKTQANENREESAERLSKIEDLEEERVSLKHQVQVAVARADSEALARSIAEETVADLEKEKTIKELELKDFVMKHRNEINAKEAALATLKEAENELHKKLGQKAAEYEDLVQQHKKQQEELALMRSSKDEEITKLLDKCKNEVLLKQVAVNKLAEVMNRRDSDLPKQKNKARSTAELRKKEKEMRRLQQELSQERDKFNQLLLKHQDLQQLCAEEQQLKQKMVMEIDCKATEIENLQSKLNETASLSSADNDPEDSQHSSLLSLTQDSVFEGWLSVPNKQNRRRGHGWKRQYVIVSSRKIIFYNSDIDKHNTTDAVLILDLSKVYHVRSVTQGDVIRADAKEIPRIFQLLYAGEGASHRPDEQSQLDVSVLHGNCNEERPGTIVHKGHEFVHITYHMPTACEVCPKPLWHMFKPPAAYECKRCRNKIHKEHVDKHDPLAPCKLNHDPRSARDMLLLAATPEDQSLWVARLLKRIQKSGYKAASYNNNSTDGSKISPSQSTRSSYKPYAVNVQRSATLPANSSLK
Protein: Immunoglobulin lambda variable 1-44 (Ig lambda chain V-I region MEM) (Ig lambda chain V-I region VOR) (P01699)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MASFPLLLTLLTHCAGSWAQSVLTQPPSASGTPGQRVTISCSGSSSNIGSNTVNWYQQLPGTAPKLLIYSNNQRPSGVPDRFSGSKSGTSASLAISGLQSEDEADYYCAAWDDSLNG
Protein: 14-3-3 protein epsilon (14-3-3E) (P62261)
Organism: Bos taurus (Bovine)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner. Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62258}. Cytoplasm {ECO:0000250|UniProtKB:P62258}. Melanosome {ECO:0000250|UniProtKB:P62258}.
Interaction partners:
- non-specific serine/threonine protein kinase
- M-phase inducer phosphatase 3
- 14-3-3 protein theta
- RAF proto-oncogene serine/threonine-protein kinase
- Metalloproteinase inhibitor 1
- Transcriptional coactivator YAP1
- WW domain containing transcription regulator 1
- Forkhead box protein O1
- BCL2 associated agonist of cell death
- 14-3-3 protein zeta/delta
Sequence:
MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ
Protein: Methionine aminopeptidase 1 (MAP 1) (MetAP 1) (EC 3.4.11.18) (Peptidase M 1) (Q4QRK0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03174}.
Interaction partners:
- Methionine aminopeptidase 2
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL22
- Methionine aminopeptidase 2
- Large ribosomal subunit protein uL14
- Zinc-regulated GTPase metalloprotein activator 1
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein uL30
- Ribosomal protein L7-like 1
Sequence:
MAAVETRECETEGCHSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKEDKTNDEEKNCVEKEVNTDPWPGYRYTGKLRPYYPLTPMRLVPSNIQRPDYADHPLGMSESEQTMKGTSQIKILNAEEIEGMRVVCKLAREVLDIAAMMVKPGVTTEEIDHAVHLACTARNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRHLQEGDILNIDITVYHNGYHGDLNETFFVGEVDEGAKRLVQTTYECLMQAIDSVKPGIRYRELGNIIQKHAQANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKPGHVFTIEPMICEGGWQDETWPDGWTAVTRDGKRSAQFEHTLLVTETGCEILTRRLEDNGRAHFLSQM
Protein: V-type proton ATPase subunit G1 (V-ATPase subunit G1) (Vacuolar H(+)-ATPase subunit G isoform 1) (Vacuolar proton pump subunit G1) (O82628)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}. Vacuole membrane {ECO:0000269|PubMed:17151019}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase subunit F
- V-type proton ATPase subunit c''1
- V-type proton ATPase subunit C
- V-type proton ATPase subunit H
- V-type proton ATPase subunit c''2
- V-type proton ATPase subunit d2
- V-type proton ATPase subunit B1
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit c5
Sequence:
MESNRGQGSIQQLLAAEVEAQHIVNAARTAKMARLKQAKEEAEKEIAEYKAQTEQDFQRKLEETSGDSGANVKRLEQETDTKIEQLKNEASRISKDVVEMLLKHVTTVKN
Protein: NADPH-Fe(3+) oxidoreductase subunit alpha (EC 1.-.-.-) (Soluble Fe(3+) reductase alpha subunit) (Q74FU6)
Organism: Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Function: NADPH-dependent Fe(3+) reductase. Probably involved in acetate metabolism and not in the reduction of Fe(3+) chelates. Unable to utilize NADH or formate as electron donors. Unlike formate dehydrogenases, contains no W, Mo or Se. Substrates are Fe(3+)-nitrilotriacetate >> Fe(3+)-citrate or Fe(3+)-EDTA > Fe(3+)-oxyhydroxide. Catalyzes also the reduction of NADP(+) with reduced methyl viologen as electron donor. No activity with menadione as electron acceptor. May be alternatively involved in transferring electrons from reduced ferredoxin to NADP(+) and may serve as a major route for NADP regeneration.
Subcellular location: Cytoplasm. Cell inner membrane {ECO:0000305|PubMed:17906154}; Peripheral membrane protein {ECO:0000269|PubMed:11443080, ECO:0000269|PubMed:17906154}.
Interaction partners:
- NADPH-Fe
- NADH dehydrogenase I, F subunit
- Bidirectional NAD-reducing hydrogenase, diaphorase subunit
- Ech-hydrogenase-related complex, large subunit
- NADH dehydrogenase I, F subunit
- Periplasmically oriented, membrane-bound formate dehydrogenase, iron-sulfur cluster-binding subunit
- NADH-dependent ferredoxin:NADP+ oxidoreductase, alpha subunit
- NADH dehydrogenase I, E subunit
- Ech-hydrogenase-related complex, small subunit
- Iron-sulfur cluster-binding oxidoreductase
Sequence:
MVSLTIDGKDITVAKETTILDAAALLGITIPTLCWLKKVSPTGACRVCAVEIEGVDRPMTACNTPVKDGIKVTTQSEKLSRIRQKIMELMLVNHPLDCPVCDAGGECDLQNACYGLGAAKQEYGAVLERRKIRYDWPLIESDPNRCILCEKCVKVDHEIVGCNAIRVVNRGEATIIDTVDGNPLNCEFCGNCVAACPTGTLISKPFKFRGRPWAFTTTPSVCPFCATGCQIEYHSRNGRVERVTSDDSTYNSGNLCINGRFGYSYINSPDRLAEPMVKGQKADWNTAMGTAATALKQIVASHGADAVAGFGSPRVTNEDNYLFQKLMRSAIGTGNIDSEARLGFAATQKVLREMLGIAGASTTIDAIDRATAVLVVGCDLNAEATGMEYRVIKAATKNNAKLVLAAMRDIKLKKFANSHLKYRPGNETLLINALTKAVLEEGLENKEFCSANISNLSDLTAALAGVSIADAAAATGVTEADLRAAARLVGGKKGVAVIFGAELMRGGNTDAVKALINLALILGATAGDTGGLFPVYEKTNIRGLLDMGVAPDHFPGHQTDGTTFEKAWGKKLPAAAGKDLWQIIEGIEQGSVKALYLLGCDPVASFPEGERIRKALEKLELLIVQDPFPGEAAKMAHVVFPSSVAAEKNGTFTTIDGRVQPLAKAVAPSGDAREDWDILTELYNRLTGESRIHSPAAVLDEVAALVPAYASVGRTGGTITAQPRSGGLALAPVSARAVAGSPTTLLVGTILYHSGTTTTWSKNNLEIIPKGYIEIHPNDAAKLGIAEGGKVRLSAGSVKVEGTAKITPRVQPGLLFAPSHFRGMNVNALLSRDGGVVPVTVEKA
Protein: Polyhomeotic homolog 1 (J3KQH6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
METESEQNSNSTNGSSSSGGSSRPQIAQMSLYERQAVQATIAASRQASSPNTSTTQQQTTTTQASINLATTSAAQLISRSQSVSSPSATTLTQSVLLGNTTSPPLNQSQAQMYLRVNRTLGRNVPLASQLILMPNGAVAAVQQEVPSAQSPGVHADADQVQNLAVRNQQASAQGPQMQGSTQKAIPPGASPVSSLSQASSQALAVAQASSGATNQSLNLSQAGGGSGNSIPGSMGPGGGGQAHGGLGQLPSSGMGGGSCPRKGTGVVQPLPAAQTVTVSQGSQTEAESAAAKKAEADGSGQQNVGMNLTRTATPAPSQTLISSATYTQIQPHSLIQQQQQIHLQQKQVVIQQQIAIHHQQQFQHRQSQLLHTATHLQLAQQQQQQQQQQQQQQQPQATTLTAPQPPQVPPTQQVPPSQSQQQAQTLVVQPMLQSSPLSLPPDAAPKPPIPIQSKPPVAPIKPPQLGAAKMSAAQQPPPHIPVQVVGTRQPGTAQAQALGLAQLAAAVPTSRGMPGTVQSGQAHLASSPPSSQAPGALQECPPTLAPGMTLAPVQGTAHVVKGGATTSSPVVAQVPAAFYMQSVHLPGKPQTLAVKRKADSEEERDDVSTLGSMLPAKASPVAESPKVMDEKSSLGEKAESVANVNANTPSSELVALTPAPSVPPPTLAMVSRQMGDSKPPQAIVKPQILTHIIEGFVIQEGAEPFPVGCSQLLKESEKPLQTGLPTGLTENQSGGPLGVDSPSAELDKKANLLKCEYCGKYAPAEQFRGSKRFCSMTCAKRYNVSCSHQFRLKRKKMKEFQEANYARVRRRGPRRSSSDIARAKIQGKCHRGQEDSSRGSDNSSYDEALSPTSPGPLSVRAGHGERDLGNPNTAPPTPELHGINPVFLSSNPSRWSVEEVYEFIASLQGCQEIAEEFRSQEIDGQALLLLKEEHLMSAMNIKLGPALKICAKINVLKET
Protein: Tubulin beta-2A chain (Q7TMM9)
Organism: Mus musculus (Mouse)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Tubulin alpha-1B chain
- Tubulin alpha-1A chain
- Tubulin alpha-1C chain
- Tubulin alpha-4A chain
- Tubulin alpha-8 chain
- Tubulin alpha chain-like 3
- Tubulin alpha-3 chain
- Microtubule-associated protein
- Gap junction alpha-1 protein
- Cytoplasmic dynein 1 heavy chain 1
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYSIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
Protein: Glyoxylate reductase 1 homolog (K7EQB2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAVSLRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAVEEFLRRAKGKDQDLTIPESSTVKGMMAGPMAAFKWQPTASEPVKDADPHFHHFLLSQTEKETGSTSIQAADSTAVNGSITPTDKKIGFLGLGLMGSGIV
Protein: L-xylulose reductase (XR) (EC 1.1.1.10) (Dicarbonyl/L-xylulose reductase) (Q920P0)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the NADPH-dependent reduction of several pentoses, tetroses, trioses, alpha-dicarbonyl compounds and L-xylulose. Participates in the uronate cycle of glucose metabolism. May play a role in the water absorption and cellular osmoregulation in the proximal renal tubules by producing xylitol, an osmolyte, thereby preventing osmolytic stress from occurring in the renal tubules.
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Probably recruited to membranes via an interaction with phosphatidylinositol. {ECO:0000250}.
Interaction partners:
- Sorbitol dehydrogenase
- aldose reductase
- Aldo-keto reductase family 1 member B7
- Aldo-keto reductase family 1 member B1
Sequence:
MDLGLAGRRALVTGAGKGIGRSTVLALQAAGAQVVAVSRTREDLDSLVRECPGVEPVCVDLADWEATEQALSNVGPVDLLVNNAAVATLQPFLEVTKEACDTSFNVNFRAVVQVSQIVARGMIARGVPGAIVNVSSQASQRALTNHTVYCSTKGALDMLTKVMALELGPHKIRVNAVNPTVVMTPMGRANWSDPHKAKVMLDRIPLGKFAEVENVVDTILFLLSNRSSMTTGSALPVDGGFLAT
Protein: trypsin (EC 3.4.21.4) (B5X8S0)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MRLLALILLVGAAAAVPREDGKIIGGQECEPHSRPWMASLNYGYHFCGAVLINEQWVLSVAHCWYNPYAMQIMLGEHNLRVFEGTEQLMKTQNIIWHPSYDYQTLDYDMMLIKLFHPVEITDYVKPIPLPTSCPHAGLPCSVSGWGNIATGEEVNMPARLQCLDVPILEDEKCEMAYPGMLTRRMVCAGYMDGGRDACNGDSGSGLVCLGEVHGLVSWGQGCAVPGYPGVYVKVCEFLPWIDETMKANM
Protein: G-protein coupled receptor (Q717T5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MASGNNETEPLYCGSGMDNFHTSYKNMHGYVSLVVCILGTIANTLNIIVLTRREMRSPTNAILTGLAVADLAVMLEYIPYTIHDYILTDSLPREEKLSYSWACFIKFHSIFAQVLHTISIWLTVTLAVWRYIAVGYPQKNRVWCGMRTTIITITTAYVVCVLVVSPSLYLITAITEYVDQLDMNGKVINSIPMTQYVIDYRNELMSARTAALNATPTSAPLNETVWLNASTLLTSTTTVAPPTPSPVVRNVTVYRLYHSDLALHNASLQNATFLIYSVVIKLIPCIALTILSVRLILALLEAKRRRKKLTSKPATPAASNGTKSPANGKSADRPRKNSKTLEKEKQTDRTTRMLLAVLLLFLITEFPQGIMGLLNAVLGDVFYLQCYLRLSDLMDILALINSSINFILYCSMSKQFRTTFTLLFRPKFLDKWLPVAQDEMAAARAERSAVAPVLEKGRQQPQVVMASTTTNITQVTNL
Protein: Kunitz-type serine protease inhibitor Hg1 (Delta-KTx 1.1) (P0C8W3)
Organism: Hoffmannihadrurus gertschi (Scorpion) (Hadrurus gertschi)
Function: Dual-function toxin that completely inhibits the activity of trypsin at a molar ratio of 1:1 (dissociation constant of 107 nM) and that inhibits mKv1.3/KCNA3 potassium channel currents with an IC(50) of 6.2 nM (where 1 uM inhibits 80% of currents). Also has weak inhibitory activity against mKv1.1/KCNA1 (where 1 uM inhibits less than 50% of currents), hKv1.2/KCNA2 (where 1 uM inhibits less than 50% of currents), and hKCa2.3/KCNN3.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MIIFYGLFSILVLTSINIAEAGHHNRVNCLLPPKTGPCKGSFARYYFDIETGSCKAFIYGGCEGNSNNFSEKHHCEKRCRGFRKFGGK
Protein: Transcription factor FER-LIKE IRON DEFICIENCY-INDUCED TRANSCRIPTION FACTOR (Basic helix-loop-helix protein 29) (AtbHLH29) (bHLH 29) (FER-LIKE REGULATOR OF IRON UPTAKE) (Transcription factor EN 43) (Transcription factor Fe-DEFICIENCY INDUCED TRANSCRIPTION FACTOR 1) (bHLH transcription factor bHLH029) (Q0V7X4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Essential protein involved in iron uptake responses. Regulates FRO2 at the level of mRNA accumulation and IRT1 at the level of protein accumulation. Confers enhanced iron mobilization responses at low iron supply.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor ORG2
- Transcription factor ORG3
- Fe
- Ferric reduction oxidase 2
- Transcription factor bHLH101
- Transcription factor bHLH100
- Transcription factor bHLH47
- Transcription factor ILR3
- Transcription factor MYB72
- Nicotianamine synthase 2
Sequence:
MEGRVNALSNINDLELHNFLVDPNFDQFINLIRGDHQTIDENPVLDFDLGPLQNSPCFIDENQFIPTPVDDLFDELPDLDSNVAESFRSFDGDSVRAGGEEDEEDYNDGDDSSATTTNNDGTRKTKTDRSRTLISERRRRGRMKDKLYALRSLVPNITKMDKASIVGDAVLYVQELQSQAKKLKSDIAGLEASLNSTGGYQEHAPDAQKTQPFRGINPPASKKIIQMDVIQVEEKGFYVRLVCNKGEGVAPSLYKSLESLTSFQVQNSNLSSPSPDTYLLTYTLDGTCFEQSLNLPNLKLWITGSLLNQGFEFIKSFT
Protein: Sister chromatid cohesion protein 2 (Q04002)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a structural role in chromatin and is involved in sister chromatid cohesion. Forms a complex with SCC4 required for the stable association of the cohesin complex with chromatin, which may act by hydrolyzing ATP from SMC1 and SMC3 heads. Binds to the nucleosome-free promoter regions of ribosomal protein genes and tRNA genes. Involved in transcriptional regulation by cooperating with the RSC complex to maintain nucleosome exhaustion at its binding sites.
Subcellular location: Nucleus {ECO:0000269|PubMed:10882066, ECO:0000269|PubMed:25173104, ECO:0000269|PubMed:26038942}. Chromosome, centromere {ECO:0000269|PubMed:26038942}. Note=Associates with chromatin. {ECO:0000269|PubMed:10882066, ECO:0000269|PubMed:25173104, ECO:0000269|PubMed:26038942}.
Interaction partners:
- Sister chromatid cohesion protein 1
- Structural maintenance of chromosomes protein 1
- Structural maintenance of chromosomes protein 3
- MAU2 chromatid cohesion factor homolog
- Cohesin subunit SCC3
- Meiotic recombination protein REC8
- Structural maintenance of chromosomes protein 5
- Sister chromatid cohesion protein PDS5
- Transcription factor BYE1
- Structural maintenance of chromosomes protein 4
Sequence:
MSYPGKDKNIPGRIIEALEDLPLSYLVPKDGLAALVNAPMRVSLPFDKTIFTSADDGRDVNINVLGTANSTTSSIKNEAEKERLVFKRPSNFTSSANSVDYVPTNFLEGLSPLAQSVLSTHKGLNDSINIEKKSEIVSRPEAKHKLESVTSNAGNLSFNDNSSNKKTKTSTGVTMTQANLAEQYLNDLKNILDIVGFDQNSAEIGNIEYWLQLPNKKFVLTTNCLTKLQMTIKNITDNPQLSNSIEITWLLRLLDVMVCNIKFSKSSLKMGLDDSMLRYIALLSTIVLFNIFLLGKNDSNLHRESYIMEPVNFLSDLIESLKILTIEYGSLKIEFDTFQEALELLPKYIRNGPFLDDNVTAKLVYIFSDLLMNNDIEATTNIQFQSFWDNVKRISSDILVSLFGSFDQQRGFIIEELLSHIEKLPTKRIQKKLRKVGNQNIYITDFTFTLMSMLENINCYSFCNQMKDIAPENIDLLKNEYKKQEEFLFNIVEHINDTILERFFKNPSALRYVIDNFVQDLLLLISSPQWPVTEKILSSLLKRLLSVYSPSMQVSANIETICLQLIGNIGSTIFDIKCSTRDHEDNNLIKMINYPETLPHFFKSFEECIAYNETIKCRRSATRFLWNLRLGTILILEEYTKDAKEQIITVDNELKKILEQIKDGGLGPELENREADFSTIKLDYFSILHAFELLNLYDPYLKLILSLLAKDKIKLRSTAIKCLSMLASKDKVILSNPMVKETIHRRLNDSSASVKDAILDLVSINSSYFEFYQQINNNYNDDSIMVRKHVLRINEKMYDETNDIVTKVYVIARILMKIEDEEDNIIDMARLILLNRWILKVHEVLDQPEKLKEISSSVLLVMSRVAIMNEKCSQLFDLFLNFYLLNKEAHSKEAYDKITHVLTILTDFLVQKIVELNSDDTNEKNSIVDKQNFLNLLAKFADSTVSFLTKDHITALYPYMVSDEKSDFHYYILQVFRCTFEKLANFKQKFLYDLETTLLSRLPKMNVREIDEAMPLIWSVATHRHDTARVAKACSSCLSHLHPYINKANNEEAAIVVDGKLQRLIYLSTGFARFCFPKPSNDKIAFLQEGETLYEHITKCLLVLSKDKITHVIRRVAVKNLTKLCGNHPKLFNSRHVLHLLDKEFQSDQLDIKLVILESLYDLFLLEERKSVRNTGVNSTLSSNSILKKKLLKTNRVEFANDGVCSALATRFLDNILQLCLLRDLKNSLVAIRLLKLILKFGYTNPSHSIPTVIALFASTSQYIRHVAYELLEDLFEKYETLVFSSLSRGVTKAIHYSIHTDEKYYYKHDHFLSLLEKLCGTGKKNGPKFFKVLKRIMQSYLDDITDLTSTNSSVQKSIFVLCTNISNITFVSQYDLVSLLKTIDLTTDRLKEVIMDEIGDNVSSLSVSEEKLSGIILIQLSLQDLGTYLLHLYGLRDDVLLLDIVEESELKNKQLPAKKPDISKFSAQLENIEQYSSNGKLLTYFRKHVKDT
Protein: Early embryogenesis protein zyg-11 (P21541)
Organism: Caenorhabditis elegans
Function: Acts as target recruitment subunit in the E3 ubiquitin ligase complex zyg-11-cul-2-elc-1. Required for metaphase to anaphase transition and M phase exit at meiosis II. Regulates polarity establishment.
Interaction partners:
- Cullin-2
- Elongin-C
- Leucine-Rich Repeat protein
- RING-box protein 1
- RNA polymerase II transcription factor SIII p18 subunit
- Sex-determining protein fem-1
- Elongin-C
- Zyg eleven-related protein 1
- von Hippel-Lindau tumor suppressor homolog
- Protein maternal effect lethal 26
Sequence:
MDHNAALTTCSTSAIPRLARLATERIAELIENDALPEFDHKVIASCSNDIFEVLRQKKKLNHQTLQTMCSTSRFQINKIDLMGNKVELQDLELCSNQNLVSFRLGDIDYFPNTNKIQVADVLDTALNRTSRQQLRHLDLSGRHRITSNWPTYVARKLPRLESLAFANRSTANETLSQIGASLLNLRFLDISSTCVTDISCISSLRNLEVLIMYNLNILKGDVTETLSNLTKLRVLDISRKVNTDYLQETSQDAHLDLALGIYNRSVEAIESGTATPWAELRAIDMSGLSIVQFGTDRALAFVEKIIEAHPKLEQISLLATPLDSSLIEIPNRNLQVINTVSRRSIIFALSHYANLDRPAFITHALHSVYYQLQSGYDKFSQEELKECLRLVCISMQQGLNTLPVQIAGSACLYHLCKMKRIKRLSVKEVNNCIERSLDAAEQYRSMTQLQKNVWLTICNDYLLHLDEIDFYRTCKVALDTMLLNRDASVERMTIAIVSIVTPKMRPSEAKILTTETKYVYHLVKIMNDYLEAYTREHRVGHERDNENALYTLKFTLSALWNLTDECPATCKAFLDAGGVQIAFRILKAFDYHGNVQTKVLGILNNLAEVEELHLGQLCKNEYISVLISCLDGSFNEVDSKGRYREVERSYFAAGILANLLTNTDGWESENQRDEACEKLLELIEQYPTLPSAMVSYKSFIPFSRIVRESNSNGAIMWCLWGVHHVLQHREKNKAPTYEKGYIEMFMDSGLSPIVEDMSHGHSKHIHNLDIRVVHLAREIIDIVSCHSLSSSPVRLVRRV
Protein: Pleiotropic regulator 1 (D6RA26)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEVQKHSVHTLVFRSLKRTHDMFVADNGKPVPLDEESHKRKMAIKLRNEYGPVLHMPTSKENLKEKGPQNATDSYVHKQYPANQGQEVEYFVAGTHPYPPGPGVALTADTKIQRMPSESAAQSLAVALPLQTKADANRTAPSGSEYRHPGASDRPQPTAMNSIVMETGNTKNSALMAKKAPTMPKPQWHPPWKLYRVISGHLGWVRCIAVEP
Protein: Uncharacterized protein, isoform C (Q8IMG1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEYQKRTPKRRSFIERAQKESEELVRTMGGSLELAGGRRTRSSTRGTPTRAAEAVTPPPSKKARTSPASATKASAGKGRGARKLDVGADEPEPELEKEKEKVQTSVKGKGAVKKDKKEVKKQEKATEKYAPEEAKEDVAEAKEEDASPAGVQDQPDGVENLPSVAEAKQNHVDEVKPISEEPGNSSEEVPKAEEPLKSSGETSENGAATETAAAPKEPASVMDVDEDETLVENTPSANKEKALDDEKEPEQKSEEHAAAVLESKEQNEPAKEPTPEPMEVDGSSKGSSDTAQVDTPAIENVSAAPETEAAAKTTESSNDVVEVATEGKETVLEVPAAEPKEAESTVESAEELTETSTVVVTEPKEAASSEEEPSKVVDSAEPKEAESNTDESATPVPIDVSTAPASNDVSKPLEIDTTLVKTADSPAKEPQEICEVKKAEINVNGEPKIVNSSAEVGENAAPKVCN
Protein: Cleavage and polyadenylation specific factor 3-like, isoform CRA_g (Integrator complex subunit 11) (J3QRY6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNLKVPIYFSTGLTEKANHYYKLFIPWTNQKIRKTFVQRNMFEFKHIKAFDRAFADNPGPMVVFATPGMLHAGQSLQIFRKWAGNEKNMVIMPGYCVQGTVGHKILSGQRKLEMEGRQVLEVKMQVEYMSFSAHADAKGIMQLVGQAEPESVLLVHGEAKKMEFLKQKIEQELRVNCYMPANGETVTLPTSPSIPVGISLGLLKREMAQGLLPEAKKPRLLHGTLIMKDSNFRLVSSEQALKELGLAEHQLRFTCRVHLHDTRKEQETALRVYSHLKSVLKDHCVQHLPDGSVTVESVLLQAAAPSEDPGTKVLLVSWTYQDEELGSFLTSLLKKGLPQAPS
Protein: Hypoxia up-regulated protein 1 (Q22515)
Organism: Caenorhabditis elegans
Interaction partners:
- Heat shock 70 kDa protein C
- Endoplasmic reticulum chaperone BiP homolog
- Hypoxia up-regulated protein 1
- Endoplasmin homolog
- DnaJ homolog dnj-10
- J domain-containing protein
- Calreticulin
- DnaJ homolog subfamily C member 10
- Thioredoxin domain-containing protein
- GrpE protein homolog
Sequence:
MKSFILGPLGLLVAICCLYQPADAALAAMSIDLGSQFIKIGLVKPGVPMDIVLNKESRRKTPNVISFKNDERFFAEAAAAMSSSHPQSSYNFLLSMIARKEGDDAFVTFQKTFPFTAFEFDEVRKTVVFPYKEEKYNVETLLAMILWNAKKVTEAYADQTVKDVVITVPIFLNQAERRAIASAAEIAGLNLLQLLNDGSAAALNYGVFRRKEITEKPTHMLIYDMGAVKTTATIVQYVLESTRKDGKDKQPTLRTVGVGFDKTLGGLEITNRLRDHLEKVFRDTVKTSKDISTNARAIGKLHKEAERVKQVLSANKDTYAQVESLFEEQNFRAKVTREELEKMIEDLEPRIAAPILDAIGMAQISTNDIDLVVLMGAGTRVPKVKEILKTILKDKEISNFLNTDEAIAMGAVYQAAHLSKSFKVLPFNVHEKILYPVFVNFLTKTEEGTMKPIRKSLFGENYPVPNRVMHFSSYSDDFKIDIQDADKNPLSTVEISGVKDAIEKEVTDENSVLKGVKTTFSIDLSGIVSVEKASVVVEKVPTPEEKDKYEVDKKEFDEWEKEQEELKKKEKAEKKEKEEKKKTEGEEEKNEDAAGEEKTEEKTEEVEKPVVVKKTKPVEPKAKKINVALTIKETKTDNIDLNEEEVTAAKKVLGDFEQKEKEKHDREEAMNRLEGLLYDLAVRLEDGEEYAEYATEEEKKAILEEVAVLKLWFEDDVSLETKKEEFDEKRAKLEELTAKPNARKQERLDIPKVAEIIEDHFNRSMTFHAMALNLTQFEEGNKTFTDTELEVLTKLIESTTEWWNEKKDLFEKQAKNEDPVVKASEIAEKARDLEREVRYLVNKLKIASSKKSKESEKKKKTKKEKDTVKERKEEETTETTTEDQANEQQTPPPFENDNTKDDESASTEEPKKDTEHDASEL