wanglab/gogpt-training-data huggingface dataset:
Protein: Agamous-like MADS-box protein AGL23 (O80807)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that controls female gametophyte (megagametogenesis) development and chloroplast biogenesis during embryo development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Agamous-like MADS-box protein AGL80
- AGAMOUS-like 96
- MADS-box transcription factor PHERES 1
- Agamous-like MADS-box protein AGL36
- Transport/golgi organization-like protein, putative
- F-box/kelch-repeat protein At5g03020
- Coatomer subunit zeta-1
- Uncharacterized protein
- Alpha/beta-Hydrolases superfamily protein
- Uncharacterized protein
Sequence:
MVKKTLGRRKVEIVKMTKESNLQVTFSKRKAGLFKKASEFCTLCDAKIAMIVFSPAGKVFSFGHPNVDVLLDHFRGCVVGHNNTNLDESYTKLHVQMLNKSYTEVKAEVEKEQKNKQSRAQNERENENAEEWWSKSPLELNLSQSTCMIRVLKDLKKIVDEKAIQLIHQTNPNFYVGSSSNAAAPATVSGGNISTNQGFFDQNGMTTNPTQTLLFGFDIMNRTPGV
Protein: Actin (Q9NA98)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable dynactin subunit 2
- Actin-related protein 10
- Dynactin subunit 1
- Dynactin subunit 4
- Dynactin subunit 6
- F-actin-capping protein subunit beta
- Dynactin subunit 5
- F-actin-capping protein subunit alpha
- DyNactin Complex component
- Protein sumv-1
Sequence:
MDYDVIANQPVVIDNGSGVIKAGFAGEQQPKVRFANFVGRPKYHRVMAGGLDGDIFIGPKAESNRGLFSIEYPMEHGIVNNWSDMEKIWEYIFGQDQLKIFPEEHPVLLTDAPLNPLKNRERSAEIFFETFNVPALYIQMQAVLSLYATGRTTGVVLDSGDGVTHAVPIVKGFAMKHAIQRMDLAGRDVTEYLRVLLRREGYEFHRSNEFEIVREMKENACYLALDPTKVENNSVKSSYALPDTTKIEISNSLFRAPEVLFKPDLIGTEWPGMAHVVNQSIMKCDVDLRQTLYSNIVLSGGTTLFKGFGDRLLGEMRKIAPADGKIRISASQERNSLTWIGGSIVASLDTFRKMWLGKKEYEDMGASAMHKRFF
Protein: Autism susceptibility gene 2 protein homolog (A0A087WPF7)
Organism: Mus musculus (Mouse)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. The PRC1-like complex that contains PCGF5, RNF2, CSNK2B, RYBP and AUTS2 has decreased histone H2A ubiquitination activity, due to the phosphorylation of RNF2 by CSNK2B. As a consequence, the complex mediates transcriptional activation (By similarity). In the cytoplasm, plays a role in axon and dendrite elongation and in neuronal migration during embryonic brain development. Promotes reorganization of the actin cytoskeleton, lamellipodia formation and neurite elongation via its interaction with RAC guanine nucleotide exchange factors, which then leads to the activation of RAC1.
Subcellular location: Nucleus {ECO:0000269|PubMed:19948250, ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:25533347}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25533347}. Cell projection, growth cone {ECO:0000269|PubMed:25533347}. Note=Detected both in cytoplasm and nucleus (PubMed:25533347). Colocalizes with RAC1 at actin-rich growth cones (PubMed:25533347). Detected on the promoter region of actively transcribed genes (PubMed:25519132). {ECO:0000269|PubMed:25519132, ECO:0000269|PubMed:25533347}.
Interaction partners:
- Polycomb group RING finger protein 5
- YY1-associated factor 2
- Casein kinase II subunit alpha
- RING1 and YY1-binding protein
- Casein kinase II subunit alpha'
- E3 ubiquitin-protein ligase RING2
- Polycomb group RING finger protein 3
- E3 ubiquitin-protein ligase RING1
Sequence:
MDGPTRGHGLRKKRRSRSQRDRERRSRAGLGTGAAGGIGAGRTRAPSLASSSGSDKEDNGKPPSSAPSRPRPPRRKRRESTSAEEDIIDGFAMTSFVTFEALEKDVAVKPQERAEKRQTPLTKKKREALTNGLSFHSKKSRLSHSHHYSSDRENDRNLCQHLGKRKKMPKGLRQLKPGQNSCRDSDSESASGESKGFQRSSSRERLSDSSAPSSLGTGYFCDSDSDQEEKASDASSEKLFNTVLVNKDPELGVGALPEHNQDAGPIVPKISGLERSQEKSQDCCKEPVFEPVVLKDPHPQLPQLPSQAQAEPQLQIPSPGPDLVPRTEAPPQFPPPSTQPAQGPPEAQLQPAPLPQVQQRPPRPQSPSHLLQQTLPPVQSHPSSQSLSQPLSAYNSSSLSLNSLSSRSSTPAKTQPAPPHISHHPSASPFPLSLPNHSPLHSFTPTLQPPAHSHHPNMFAPPTALPPPPPLTSGSLQVPGHPAGSTYSEQDILRQELNTRFLASQSADRGASLGPPPYLRTEFHQHQHQHQHTHQHTHQHTFTPFPHAIPPTAIMPTPAPPMFDKYPTKVDPFYRHSLFHSYPPAVSGIPPMIPPTGPFGSLQGAFQPKTSNPIDVAARPGTVPHTLLQKDPRLTDPFRPMLRKPGKWCAMHVHIAWQIYHHQQKVKKQMQSDPHKLDFGLKPEFLSRPPGPSLFGAIHHPHDLARPSTLFSAAGAAHPTGTPFGPPPHHSNFLNPAAHLEPFNRPSTFTGLAAVGGNAFGGLGNPSVTPNSVFGHKDSPSVQNFSNPHEPWNRLHRTPPSFPTPPPWLKPGELERSASAAAHDRDRDVDKRDSSVSKDDKERESVEKRHPSHPSPAPPVPVSALGHNRSSTDPTTRGHLNTEAREKDKPKEKERDHSGSRKDLTTEEHKAKESHLPERDGHSHEGRAAGEEPKQLSRVPSPYVRTPGVDSTRPNSTSSREAEPRKGEPAYENPKKNAEVKVKEERKEDHDLPTEAPQAHRTSEAPPPSSSASASVHPGPLASMPMTVGVTGIHAMNSIGSLDRTRMVTPFMGLSPIPGGERFPYPSFHWDPMRDPLRDPYRDLDMHRRDPLGRDFLLRNDPLHRLSTPRLYEADRSFRDREPHDYSHHHHHHHHPLAVDPRREHERGGHLDERERLHVLREDYEHPRLHPVHPASLDGHLPHPSLLTPGLPSMHYPRISPTAGHQNGLLNKTPPTAALSAPPPLISTLGGRPGSPRRTTPLSAEIRERPPSHTLKDIEAR
Protein: RING-type domain-containing protein (Q384B6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proliferating cell nuclear antigen
- RuvB-like helicase
- Protein artemis
Sequence:
MLPCPSEGTTRDLQGAWFGAATDCCSDHNPSSVYSDDGQAQNPETNFLDEKSGCAGGSAWAKLTSVIPEFNEGNEELPELPACVEKLGLSPLEQKVFSWMREQEEKPWSCEISTLLPEGASPVGEQVEQDRAKGGILFGIGSDKLMAPLRALREVDHQRSHSTLETTVCIDGGPMLVLCKKRHVRRLMEILHHDGAHSLSRVLAYTGRGNVHLTPTQIGSDYDYVLSTYSTLRREPDPRSELPGKLYLVHWRRVVLFEPYFLCDFTRTESYLCTELQADARWIFCGERFVMQTHKLYGFVRFLNEPSLKSWVFWSERVADKKGVDRSVFDSDKNTELKRVLSTMCRQTRRACLIREGGRGANSMNVIKVNLTEEEKEFYNATFDRAVSSVSSSTDQQTSCLPVLEIINLCRLITLHLYVGRETFQRMSPPPLTPEEREEQLTSFFDLLANDGLRERAFTTELRNKLRSGVLDEECGICFLRINTPGILNCAHYFCVGCIDKIKKSGRPYCPNCRTVLNHRTVVPPGLLKCPEDEPVPSDFSQWGPSSKAEVLVENLKKLSGDHRAIVFGCSSQFFQYLQWYLRQHGMDTYTFGSCKGLQEVKRVQQWLDSGAQGASAERNDESKHLPRVLLVLLTDCDEDVRFKGITHCFFMHATWCPIIEHHALQCIEHCDEEKELEVVKILANVGLEQTIDELCQRKRSDGSDDYITSAEVFEVFNETANVNDFMVRTTTQVPQNEEGENNEEGENNEEGYESDEEYEGDEEDGDNQ
Protein: Zinc finger protein 2 (Q967Y4)
Organism: Trypanosoma brucei rhodesiense
Interaction partners:
Sequence:
MAFNQRFDRGAQPSYAAVQLPPGWQMAYSVEGEVYYIDHNTRTTHWKIPQEVLNEMYHQGQTYRPSRSRRGIDRSKMKTKMCMNIQNGGKCTWGNACAFAHSSEELAAVPHNGGGQRMRMDPGAHQGNDNGLDNNHLQQ
Protein: Integrator complex subunit 9 (Q95TS5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing. Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5. May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:23288851, ECO:0000269|PubMed:39032490}. Cytoplasm, cytosol {ECO:0000269|PubMed:39032490}.
Interaction partners:
- Integrator complex subunit 11
- Integrator complex subunit 5
- Integrator complex subunit 1
- Integrator complex subunit 3
- Integrator complex subunit 4
- Integrator complex subunit 6
- Integrator complex subunit 7
- Integrator complex subunit 12
- Protein asunder
- Integrator complex subunit 2
Sequence:
MRLYCLSGDLAKPCYIITFKGLRIMLDCGLTEQTVLNFLPLPFVQSLKWSNLPNFVPSRDHDPQMDGELKDCCGRVFVDSTPEFNLPMDKMLDFSEVDVILISNYLNMLALPYITENTGFKGKVYATEPTLQIGRFFLEELVDYIEVSPKACTARLWKEKLHLLPSPLSEAFRAKKWRTIFSLKDVQGSLSKVTIMGYDEKLDILGAFIATPVSSGYCLGSSNWVLSTAHEKICYVSGSSTLTTHPRPINQSALKHADVLIMTGLTQAPTVNPDTKLGELCMNVALTIRNNGSALIPCYPSGVVYDLFECLTQNLENAGLNNVPMFFISPVADSSLAYSNILAEWLSSAKQNKVYLPDDPFPHAFYLRNNKLKHYNHVFSEGFSKDFRQPCVVFCGHPSLRFGDAVHFIEMWGNNPNNSIIFTEPDFPYLQVLAPFQPLAMKAFYCPIDTSLNYQQANKLIKELKPNVLVIPEAYTKPHPSAPNLFIEQPDKKIITFKCGEIIRLPLKRKLDRIYITSELAQKISPKEVAAGVTFSTLTGVLQVKDKVHCIQPCADSVKDETISSNSAPTKEDVLKNVKYEYGSIDVDAVMKKLAQDGFSNIKLDRTGGALTLNLVNEDTVIKFEDNETHIICGGKPTTRLKLRDTIMKCLQSF
Protein: Acireductone dioxygenase (Acireductone dioxygenase (Fe(2+)-requiring)) (ARD') (Fe-ARD) (EC 1.13.11.54) (Acireductone dioxygenase (Ni(2+)-requiring)) (ARD) (Ni-ARD) (EC 1.13.11.53) (O94286)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes 2 different reactions between oxygen and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03154}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03154, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Enolase-phosphatase E1
- Methylthioribulose-1-phosphate dehydratase
- Pdp3-interacting factor 1
- Aromatic amino acid aminotransferase C569.07
- Aromatic amino acid aminotransferase C1773.13
- Aromatic amino acid aminotransferase C56E4.03
- Meiotically up-regulated gene 14 protein
- Phosphoglucomutase
- Spermidine synthase
- Methylthioribulose-1-phosphate dehydratase-like protein
Sequence:
MRAYIFQDEGDQRKPNDSKIEVSAEDLEAAKVSYRHHDGDLHTFADGLMKEYGFKNRDEVVVSRKGLGDRYDNMVKKFFEEHLHEDEEIRLILDGNGYFDVRSVDDRWVRIFVEKGDLIILPPGIYHRFTTTTDDYIHAMRLFHENPKWIALSRTDSTSEELDARKSYLNSIKKSVYV
Protein: Cytochrome c oxidase subunit 26, mitochondrial (Q2V2P9)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27083394, ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:27083394, ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome c oxidase subunit 12, mitochondrial
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome c oxidase subunit 2
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MFFSQVLRSSARAAPIKRYTGGRIGESWVITEGRRLIPEIFQWSAVLSVCLGWPGAVYFFSKARKA
Protein: Protein still life, isoform SIF type 1 (P91621)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulates synaptic differentiation through the organization of actin cytoskeleton possibly by activating Rho-like GTPases. Is likely a factor in the cascade of Rac1 or Cdc42 in the neurons. May play a role in maintaining proper septate junction functions. Required for eye development and most likely affects corneal lens-formation.
Subcellular location: Synapse {ECO:0000269|PubMed:8999801}. Note=Localizes to the submembranous region of synaptic terminals. {ECO:0000269|PubMed:8999801}.
Interaction partners:
- Ras-related protein Rac1
- Ras-like GTP-binding protein Rho1
- Amphiphysin
- Cdc42 homolog
- Rho GTPase activating protein at 1A, isoform E
- Tyrosine-protein kinase Src64B
Sequence:
MGNKLSCSCAPLMRKAYRYEDSPWQSSRRRDGHLLSSFRLWAEVFHVSASGAGTVKWQQVSEDLVPVNITCIQDSPECIFHITAYNSQVDKILDVRLVQPGTRIGQASECFVYWKDPMTNDTWGLNFTSPIDAKQFRECCSPSFKFSRKASSSYSLKLDPPGKGKVKAKRKPLSTPASPSRVRQEPQCTCMSAEQYARLRTDPRVRGSSTLPRNVGSHRITDVDGQQQVGSGKVVSAVSSTSLYDNVASGGPGTNQGADTLPRQMKGGQQDRQDVANSGVNTNTPGVIVTGVGNVGSDMCGQNHVGSQVGNDDPAACQMDMDLSKSEGTQAGGGLHQSVGTCTSSSKGTGTRNKDFGDDMTRDAHSHDMHQHNVINNNTRRKTKSTEDMNVDTSTLKRMLKPMPSTESPVTSPEMGRRRYNYYNANAAQTLGHPPHMHQHGMAMGMGGGGGGGHHIMNNNTMGRASSQSSRFSGSRSSHEIGRGYPPRNLYLELERERSCIEGSPPSDNVMFDNQCYATTPSSSNGNSDQDQSYGQQQSSGQHPQQQQGPPQRSSRHQHHHQQAPNVTPTPGSPTSRLLLEYEMHLRNTLAKGMDAESYSLHTFEALLSQSMENLANAKSSTLPLPPHRPLSTIRDKERDRDRDGYYSDRNELIRERERERDRGYLSDHNSSFSNSRCASCIGESARAQWFRHSDGWRSGSSTIGSGSGHGMMTQQIPGSGHKRSPWDSLPSLRQDSSLNDSGYKSARADSLEQRAEFIRQDSLRSEYLSDRESRYGIVQQASIESTDSRMCYLTSSEISDDDRMSLTTAVSDEDDGESVMASPYKAKATGTAASSFNCTGAVRKAGFLSVKKWLLRKKHQIELARKRGWKGYWVCLKGTTLLFYPCDSREGRSVEAAPKHLIIVDGAIMQPIPEHPKRDYIFCLSTAFGDAYLFQAPCQVELENWVNSIHSACAAAFARHRGKTGTLHLLQEEIFRLEKAIESDHKLKHMAELQQSVVTDQETRHQIQTQILQWEENLERLHCEQFRLRCYMASLQSGELPNPKSLLTHVSRPTKNTLNKLGVFTVSSFHAFICARSPSLLNNLLAGRGATKRRPPMLSRSNSGSSRRSMQMNSRDEPEKTFKVAMPDNAYSTVYLRDAMSVEEFLASACARRNLNPMEHFVRVKKRRDMEDHNYFVPHRNDLIENYLHNHEFVEVCMKILYQVELQRTTLEQMWGFSVEAELIENAERQDELCCYVSRVEDKSVAMHNGIIKGDEIMVINGAIVSDLDMMYLESVLQEEQSLSMMMRSSRTEPPDLVGIMRVTDDMIDSLVCPPPPTDPPVMSEEMITGLIVPAPGWNGTSKDLYSPEAESSPATSFVDPAAMAAQLAVGGVGGVVVGGLGVAKPTSRTSSFEIENLLKTAEQETRKSSPTGSVTSSVSTTALTPSRQLTDAEKLRKVVMELVDTERTYVKHLNNLLEHYLEPMKRETFLSNAEINALFGNIHEIVTFQRQFLQNLEESLDLEPDFNKFEHCGQFRNVLFAIGSAFLYYVNHFKLYSSFCASHSKAQKVLHPNEGNHALQEFLAARNPKQQHSSTLESYLIKPIQRILKYPLLLQQMRNLTDTRADEHVHLCEALKGMEKVAEHINEMQRIHEEYGAIFDHLFRQHQKSCKQPIDLSPGDLLYYGGVEWLNISDFLGKIKKGLELHAMCFVFKSAVVFLCKERLRQKKKLMGVSSKNATNEVEIIRYQVLIPVTEVQVRASSAKDMDSHFLWELIHLRSQLQRRSEKVYVLSNSTADFRNAFLKTIRQIIRESVRNMSIPMKNFGGSSGSVSGHSSQGMGSMGYPGNSQTLERPKQQITIVHGSHTLGKPKKKSGSQRHSAGNIDYDNLSGSQEADDLPPSVGVVHYASGHTHGQQMQPAGFRGRSKTVGDVTEITCSSPEPHQQQQQQQQQQQQLMQQGHAHAHPHPHPHPREPPPPPIRQPHLHHHSSDIERIDPGTKSEGEEDSQQGTIRPKATLGRTPNHLTLSTTSTLSVGSTGSQARLIQSSHPPASYQPVLMKDLGSPVWKPRDMINLGTDPQSTTRKDDVKN
Protein: Movement and silencing protein TGBp1 (25 kDa protein) (Silencing suppressor P25) (Triple gene block 1 protein) (TGBp1) (P09396)
Organism: Potato virus X (PVX)
Function: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Increases plasmodesma size exclusion limit. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs.
Subcellular location: Host cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MDILIISLKSLGYSRTHKSLDSGPLVVHAVAGAGKSTALRKLILRHPTFTVHTLGVPDKVSIRTRGIQKPGPIPEGNFAILDEYTLDNTTRNSYQALFADPYQAPEFSLEPHFYLETSFRVPRKVADLIAGCGFDFETNSQEEGHLEITGIFKGPLLGKVIAIDEESETTLSKHGVEFVKPCQVTGLEFKVVTVVSAAPIEEIGQSTAFYNAITRSKGLTYVRAGT
Protein: Monodictyphenone cluster transcription factor (Monodictyphenone synthesis protein E) (Q5BH32)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
Interaction partners:
- NADH-ubiquinone oxidoreductase 30.4 kDa subunit, mitochondrial [Precursor]
- NADH-ubiquinone oxidoreductase chain 1
- NADH-quinone oxidoreductase subunit D domain-containing protein
- 4Fe-4S ferredoxin-type domain-containing protein
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase 24 kDa subunit, mitochondrial [Precursor]
- NADH-ubiquinone oxidoreductase chain 5
- NADH-ubiquinone oxidoreductase chain 2
- NADH-ubiquinone oxidoreductase chain 3
- Cytochrome c oxidase subunit 3
Sequence:
MTSSEGPGIPAIKTPPVKLRGSCHACALSKLKCSQDKPTCSRCVKRGTACQYLASKRAGRKQGSKTGSFKSFYNMKTDYSTSINKDDDRRELMEVSTELMQYALQQDRSLEVYRRNQYHQRTPSYPESIPSLLSSTGPGTSATSPLTLGPPDYDGYLASPISLSLLDVPDMDYFPGADMSANVMDGFPDPPSFFPSGEPIPTLQENILKTSFADSPVPANSPSVPPTPDVTSVGTPRQCFCFPRALTLLRELFPNPSLSCVTPSSESGSASPPTVQQVITKNEQTLRDITEIIECSCSEDGYTITIITLAAFKVLAWYSAVAHISPISEDSQALEEIDRTPAVVRGYNIDGEDQGRMAAQLVLSELHRVQRLVGNLYQRLKDQVSGGKPARLSTTGVNDSNHYSLPFHLLERLAVDLGAQLRSLSSEIVDRLRRG
Protein: Phospholipase D (PLD) (EC 3.1.4.-) (Choline phosphatase) (SM/LPC-specific PLD) (Sphingomyelinase D) (SMaseD) (EC 3.1.4.41) (P20626)
Organism: Corynebacterium pseudotuberculosis
Function: Virulence factor affecting bacterial dissemination and survival within the host. Has magnesium-dependent catalytic activity toward sphingomyelin (SM) and acyl- and alkyl-lysophosphatidylcholine (LPC), but not toward sphingosylphosphorylcholine (SPC) and phosphatidylcholine (PC). Lysophosphatidic acid (LPA), assumed to result from LPC hydrolysis, evokes pathophysiological responses after LPA receptor internalization. Shows hemolytic activity.
Interaction partners:
Sequence:
MREKVVLFLSIIMAIMLPVGNAAAAPVVHNPASTANRPVYAIAHRVLTTQGVDDAVAIGANALEIDFTAWGRGWWADHDGIPTSAGATAEEIFKHIADKRKQGANITFTWLDIKNPDYCRDARSVCSINALRDLARKYLEPAGVRVLYGFYKTVGGPAWKTITADLRDGEAVALSGPAQDVLNDFARSENKILTKQKIADYGYYNINQGFGNCYGTWNRTCDQLRKSSEARDQGKLGKTFGWTIATGQDARVNDLLGKANVDGLIFGFKITHFYRHADTENSFKAIKRWVDKHSATHHLATVADNPW
Protein: Testis-specific gene 13 protein (Q96PP4)
Organism: Homo sapiens (Human)
Interaction partners:
- Coatomer subunit alpha
- Coatomer subunit beta'
- Coatomer subunit beta
- Coatomer subunit gamma-2
Sequence:
MSQKRQTKFQNGKSKTSENSSAKREKGMVVNSKEISDAVGQSKFVLENLRHYTVHPNLAQYYKPLKATALQKFLAQNRKNTSFMLKVTQYDQDKTLLIMTNNPPPCSITQQDKESASKYFSKELLLKVMESHHQHKPTENLWLPRMPQKKKLRSKLKPIFPLILSDDPTSKREQWFRFSTDNDFKSEGKYSKVYALRTQKKMYPQLTFAPVHERDMRKDASKKSASERPISKVIREPLTLASLLEDMPTRTAPGESAFRNGRAPQWIIKKATVIG
Protein: ENHANCED DISEASE RESISTANCE protein (DUF1336) (F4JYC1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- At4g14500
- Adenylate kinase 5, chloroplastic
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
- START
- Transmembrane 9 superfamily member 11
- At3g13062
- Peptidyl-prolyl cis-trans isomerase CYP28, chloroplastic
- Putative methyl-CpG-binding domain protein 12
- Polyketide cyclase/dehydrase and lipid transport superfamily protein
Sequence:
MTSPGSKKVVTTDDGSEKKVSGNLGKVSFSGDLNHSGSHSGSHSRSSSSAGGGEGGTFEYFGWVYHLGVNKIGHEYCNLRFLFIRGKYVEMYKRDPHENPDIKPIRRGVIGPTMVIEELGRRKVNHGDVYVIRFYNRLDESRKGEIACATAGEALKWVEAFEEAKQQAEYALSRGGSTRTKLSMEANIDLEGHRPRVRRYAYGLKKLIRIGQGPESLLRQSSTLVNDVRGDGFYEGGDNGDAIEAHEWKCVRTINVIKRLFGKIVVLKRVRIFEDVANFKAGRGVLVKAVAVVEASADTVFEVLLNIDKHQRYEWDAVTGDSEKIDSYEGHYDVIYCIYDPKYLSRWQSKRDFVFSRQWVRGQDGTYTILQFPAVHKKRPAKSGYRRTEITPRGSRVYLLACDYLPIRLCNTSTWEIKSLKKRSDAETPSCLVTHMLEIHSKRWCKWKRTSYSKFEKTIPYALLLQVAGLKEYIGANPAFKYETSATVVQSKFQDVPNGEYVDEEMEEQFYDATDSSSGEEDEEESDDDDENQDNKEIKVKLKNVSWAIASLSLKRPKAPGASNVLDASVDPVSIDPSQFQGSLRKGNGDKDSNCWNSPSGMGFMIRGKTYLKDNAKVMGGQPLLTLISVDWFKVDSAVDNIALHPKCLIQSEPGKKLPFILVINLQVPAKPNYCLVLYYAADRPVNKTSSLGKFVDGSDSYRDARFKLIPSIVQGYWMVKRAVGTKACLLGKAVTCKYLRQDNFLEIDVDIGSSAVARSVIGLVLGYVTSLIVDLAILIEGKEESDLPEYILGTVRLNRIELDSAVSFEE
Protein: MutL homolog 1 (E7EUC9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLRSQHRSLTLPCLP
Protein: MAR-binding filament-like protein 1 (AtMFP1) (Matrix attachment region-binding filament-like protein 1) (Q9LW85)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds DNA. Interacts with chromatin via matrix attachment regions (MARs). Likely to participate in nuclear architecture by connecting chromatin with the nuclear matrix and potentially with the nuclear envelope (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000255, ECO:0000269|PubMed:12930969, ECO:0000269|PubMed:16331467, ECO:0000269|PubMed:38190535}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:16331467, ECO:0000269|PubMed:29866647}; Single-pass membrane protein {ECO:0000255}; Stromal side {ECO:0000250|UniProtKB:Q9M7J4}. Plastid, chloroplast stroma, chloroplast nucleoid {ECO:0000250|UniProtKB:Q9M7J4}. Nucleus {ECO:0000269|PubMed:16331467}. Nucleus matrix {ECO:0000269|PubMed:16331467}. Note=Is in the membrane-bound (insoluble) protein fraction of the leaves (PubMed:29866647). Forms punctate structures within the chloroplasts of epidermal mature leaf cells and isolated mesophyll protoplasts (PubMed:38190535). Distributed throughout chloroplasts locating to small patches (PubMed:29866647). Associates with thylakoid membranes in mature leaf chloroplasts. Has a direct physical interaction with nucleoids in mature leaf chloroplasts (By similarity). {ECO:0000250|UniProtKB:Q9M7J4, ECO:0000269|PubMed:29866647, ECO:0000269|PubMed:38190535}.
Interaction partners:
- Protein PTST, chloroplastic
- Probable starch synthase 4, chloroplastic/amyloplastic
- Protein PTST homolog 2, chloroplastic
- At1g50450/F11F12_20
- MAR-binding filament-like protein
- Single-stranded DNA-binding protein WHY1, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 16, chloroplastic
- YlmG homolog protein 1-2, chloroplastic
- YlmG homolog protein 1-1, chloroplastic
- Protein involved in starch initiation 1
Sequence:
MGFLIGGSCFVPSVPLHSRFLSSPSSSSSSSPSSSQFGLLCSSNVAKFKRRRPTLASLNQEDGYEYDVASAKRRAFLLVGISVLPFLQLRSPALADERGNEIKTSKVDLETEVAVVSEGTSPNPFLALLNGLGIFSAGVLGALYALARQDTKAAEETIESLKNQLKDRERALVLKEKDFEAKLQHEQEERKKEVEKAKEEQLSLINQLNSAKDLVTELGRELSSEKKLCEKLKDQIESLENSLSKAGEDKEALETKLREKLDLVEGLQDRINLLSLELKDSEEKAQRFNASLAKKEAELKELNSIYTQTSRDLAEAKLEIKQQKEELIRTQSELDSKNSAIEELNTRITTLVAEKESYIQKLDSISKDYSALKLTSETQAAADAELISRKEQEIQQLNENLDRALDDVNKSKDKVADLTEKYEDSKRMLDIELTTVKNLRHELEGTKKTLQASRDRVSDLETMLDESRALCSKLESELAIVHEEWKEAKERYERNLDAEKQKNEISASELALEKDLRRRVKDELEGVTHELKESSVKNQSLQKELVEIYKKVETSNKELEEEKKTVLSLNKEVKGMEKQILMEREARKSLETDLEEAVKSLDEMNKNTSILSRELEKVNTHASNLEDEKEVLQRSLGEAKNASKEAKENVEDAHILVMSLGKEREVLEKKVKKLEEDLGSAKGEILRMRSQPDSVKAVNSTDNKEKSDNTVTVKKVVRRRKSSTSS