wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription initiation factor TFIID subunit 4 (TBP-associated factor 4) (AtTAF4) (Q6SJR1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: TAFs are components of the transcription factor IID (TFIID) complex that is essential for mediating regulation of RNA polymerase transcription.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 12b
- Transcription initiation factor TFIID subunit 13
Sequence:
MDLSIVKLLEEDEEVDSKHSEDDLQMFQDSLIRDIEGSNLKSINNTTGNESEKPQPRYMKLQKMSSKETPWVEKTVDPVNHNLRLARVTDLLRTVVDHQPGKKTHCLNLHYKLKRKELTMEEFMRQLRDLVGDQIIRSVISQLPQLKPGNMGIKVPGRSNHDKVSKSAEFTAQESDPREVHVNQLSSTTSGTLNSSTTVQGLNKHPEQHMQLPSSSFHMDTKSGSLNPYPGTNVTSPGSSSRAKLPDFQHRENNQNVGIASVGGPTKSTINMTTVPKFERPTFVNGPSRVQDGPISDFPKNSSFPLYSAPWQGSVTKDHTVGPSSSVIHVEHKLIDQSFEQAHKPRYLVQQGVTNVPLKQKNAIPISSNDDLEKQSSKMGLFTSTTSASSVFPSMTTQLDSSTMVNMPAPSETIPKIANVTVTPKMPSVGQKKPLEALGSSLPPSRKKQKICGTSSDESIEKFNDVTAVSGINLREEEKQLLDSGPKKNDRVSKAYRRLVHGEEERTLLQKIPLQRKLTEIMGKSGLKHIDHDVERCLSLCVEERMRGLLFNIIRISKQRTDAEKCRNRTFITSDIRKEINEMNQKVKEEWEKKHSGEEKNKENDTEKEDQRSNEVKANKKDEDKERAKAANVAVRAAVGGDDRFSKWKLMAEARQRSSPGPGRNSKKLSGGTQFGKNQGLPKVVRSISVKDVIAVVEKEPQMSRSTLLYRVYNRICSDV
Protein: Neuroguidin (A0A8I6ALQ0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MEAPEVLESEVSSSITLLKNLQEQVMAVTAQVQALTAKVRAGAYSTEKGLSLLEVKDQLLLMYLMDLSHLILDKASGGSLQGHPAVLRLVEIRTVLEKLRPLDQKLKYQIDKLVKTAVTGSLSENDPLRFKPHPSNMMSKLSSEDEEENEAEEDQSEASGKKSVKGASKKYVPPRLVPVHYDETEAEREQKRLEKAKRRALSSSVIRELKEQYSDAPEEIRDVRHPHVTRQSQEDQHRINYEESMMVRLSVSKREKGLRRRASAMSSQLHSLTHFSDISALTGGTAHLDEDQNPVKKRKKMPKKGRKKKGQ
Protein: Endoplasmic reticulum transmembrane helix translocase (EC 7.4.2.-) (P-type ATPase cta4) (P5A-type ATPase cta4) (Sporulation protein essential for vegetative growth 4) (O14072)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Endoplasmic reticulum translocase required to remove mitochondrial transmembrane proteins mistargeted to the endoplasmic reticulum. Acts as a dislocase that mediates the ATP-dependent extraction of mislocalized mitochondrial transmembrane proteins from the endoplasmic reticulum membrane. Specifically binds mitochondrial tail-anchored transmembrane proteins: has an atypically large substrate-binding pocket that recognizes and binds moderately hydrophobic transmembranes with short hydrophilic lumenal domains (By similarity). Involved in controlling nuclear calcium ion levels. Required for cytokinesis and stabilizing microtubules. Required for assembly of the forespore membrane. Involved in calcium transport to the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12058018, ECO:0000269|PubMed:16394583, ECO:0000269|PubMed:22132152}; Multi-pass membrane protein {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12058018}.
Interaction partners:
- Vacuolar calcium ion transporter
- Set1 complex component spp1
- Manganese transporter pdt1
Sequence:
MGSKALITSPDISSGQLYIKLPTFFHLYVWPFALFVYPYIGYVYQNKLYSEEVRYLTYIAVGTIHALFWLAGEWNTKVYCLMTCRKTDKVEQATHILVTPSKIGESSSVEPITKLVLPDSQTIQYSFSFQRKRFIYEPEKGCFANITFPMDEPSTIGTLKKSTGLTNIQSEIFLYRYGKNCFDIPIPTFGTLFKEHAVAPFFVFQIFCCVLWCLDDYWYFSLFSMFMIIALECSVVWQRQRTLTEFRTMSIKPYEIQVYRNKHWFPISTEDLLPNDVVSVLHNKEDSGLPCDLLLLSGSCVVNEAMLSGESTPLVKESIELRPEEAVIDVDELDKNAVLFGGTRVLQVTQSPFCKLKTPDNGVPAIVLRTGFETSQGSLVRTMVFSSEKVTANNRESLYFILFLLVFAIAASGYVWHVGSKTERSRYKLMLDCVMIITSVVPSELPMELSMAVNASLGALSKYYIYCTEPFRIPLSGHLDICCFDKTGTLTEEHMVVQGIAGVNRKDPYSLEKLSDASNDAILAIATAHTLVLLEQEGETPKVVGDPMEKATVENLGWSIEKKNFVSAPEGSVFYKGKVQIIRNFQFSSALKRQSSVSNVRVSGGSFKTFVSVKGAPEVIATMLREVPKDYEKIYKDYGRKGSRVLALGYKYFKNYIPENQVSDLSRESIESDLVFAGFLIFTSPLKEDARQTVQMLNNSSHRCMMITGDNPLTAVYVAEQVGIVEKPTLVLDIKHENEKILEWKSTDDTINLPMNPHKSLEASLYEKYDLCITGRALSQIINPDVIMSIFTHAWVYARVSPSQKEFMISTLKHNGYITLMCGDGTNDVGALKQAHVGVALLNASEEDMLEMQERARNQKLMGVYEKQIQLAKRFNLPTPPVPPALCHAFPPGPNNPHREKTQEGLNKVLEDLETKKASDVQLTEAEKAAERRANLANKMFDTLANASDDEAPKLKLGDASVAAPFTSKLAVVSSITNIVRQGRCTLVALVQMHKILALNCLITAYSLSVLHLDGIKFGDTQYTISGMLMSVCFYCVSRARPLETLSKERPQAGIFNTYIIGSVLGQFAIHIVTLIYITRVVYLYEDPLEKVDLEETFKPSLLNTAIYLLQLIQQVSTFAINYQGRPFREALSENKGMYYGLLGIAFVAIAGVTEFSPELNAKLQLVKMAYNFQIQLLATMVVDYAACWIIEELMKKYFRDNKPKEIVLRN
Protein: Transcriptional regulatory protein DpiA (Destabilizer of plasmid inheritance) (P0AEF4)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system DpiA/DpiB, which is essential for expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. Could be involved in response to both the presence of citrate and external redox conditions. Regulates the transcription of citCDEFXGT, dpiAB, mdh and exuT. Binds specifically to the dpiB-citC intergenic region.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor histidine kinase DpiB
- [Citrate [pro-3S]-lyase] ligase
- Sensor histidine kinase DcuS
- Citrate lyase acyl carrier protein
- Citrate/succinate antiporter
Sequence:
MTAPLTLLIVEDETPLAEMHAEYIRHIPGFSQILLAGNLAQARMMIERFKPGLILLDNYLPDGRGINLLHELVQAHYPGDVVFTTAASDMETVSEAVRCGVFDYLIKPIAYERLGQTLTRFRQRKHMLESIDSASQKQIDEMFNAYARGEPKDELPTGIDPLTLNAVRKLFKEPGVQHTAETVAQALTISRTTARRYLEYCASRHLIIAEIVHGKVGRPQRIYHSG
Protein: Defective in tip formation protein A (Cell surface protein dtfA) (O96668)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Required for correct organization of the actin cytoskeleton and cytokinesis. Also required for apical sorting of prestalk cells, a prerequisite for formation of the tip at the mound stage and subsequent formation of the fruiting body. May be required for cell adhesion.
Subcellular location: Cell surface {ECO:0000269|PubMed:9693138}. Note=Forms a discrete lattice like arrangement at the cell surface.
Interaction partners:
- Putative mediator of RNA polymerase II transcription subunit 18
- Putative mediator of RNA polymerase II transcription subunit 14
- Catalase-B
Sequence:
MKDIEASKKPHTTTVAPPQINFIKNNENIFQPKPISNVTTTTVQPPQIVSPPSPPSPPQTTTIAPPTILPTTKTTTTTTTTTTTTTTVQPPQIVSPPIINNLIIQNNLNTPSLSSTPSPLPNNNNSNENDNDINNLKISKEEYQTQIEIQQQIQRQQILERQQLLQRRNQEQLDLLERHNDYQELINTHQNFVPPNNRFSQQIHVSQLKKQSSQSQLQQQLSSQSLQQIQQKSKQPPPQQQQQQQPPPPPIPLLPQIHQQLKPKQQQEQQQQQEQQQQQTENERINELRRLKRKKEYHNDEYKDDEIYLDNILKGIDIRKLEKLTAVELRKIGKTLGVPMGNNTKGETFQRIKSFIENHKKKKQKYREYQSEKNQQQKSNSKKLVNNSTIYDLPIKDIEHLEQLFWRIFRNIVLFRKIIGNLSRGGFFDQQQQQQQQQQSTMTTTSSSSSPMTSSDDKFFYCYNYIFSKTFKYDQIIHVSWIVDSNYFGLLKYKVSRGDLLVFCNHNTINDGDVNDDEDQNTKYEFCKMFKKIFNSIRSIQDKSFYRDLFTNYSEFIFDRINKRYPIDIYLVGSLAIECNCLVATKLLISEFQFRPVMNHSLQLAIKSGSYKMVKLIVTTIHRQMSLNPNNKPFDIEMFSKINNPSIKIINLLIQLRLFTYSNIINLVIADAKLINDNNENDILQFNKNLKNQIFNYSNLLNSFTFNNNINNNNNNNINNNNNNNNNNNNNNNNNNNNNNSNLSNNTIEYSKIKTKTVFNQFTIKQLINSCKLIVTFDLKNQYQQQYYKRHYEDSDNEEEEEITQASFTINTMAEIEFIETQITKEEKHCFVKKVIQKQLLKDGEKEDYDGIKRLAELYVSLNPHLKVYCNFMYKIIYGNENCYDQDLDDEDLFDYRVTRVFDSNCFKQSLKYGSPGYWIEYKEVEMKYAFLSNKYRNEITPNLLFKYVSPNNLNKQLKFIKKIYNSSIENGNSNGNGNGNGGTVIGGILDRLLLFYLIIENNNLELLSIVIKEFPLISNFCYIAKSNSEIYNLKIPRFIRSIEMLEFCFSNFRDHFYLPQSNSLTADFYGFQNVELLRKYDQLMVLDDMDKGIIVSNKKVRASFDDFHFIFEWGSSLKNYNNYLKMLAYIVEDPYGLYTIVTNEILLLSAILSPTTSSGEPLLNLNIERQLIFQEIISSFSTILEGTELKYYPEQMFQESTHLKRFFDWIFENRSEDLLIGGRCVITQSVQSHMLYRAGRLDIVLRKGYYYDDTNEGSKKIMPVGLALVLDDIGKYGDVVALEKYIRSCIPLMKQQSELLTLLDKDERESRACFSQCQRHFSSLLSKASIYGRINIFQHIFYNHQFIFDKKSLLFARKGFLSKISFKKLILECHYHKQHHILDFIQNVIGLDITPKQIKSN
Protein: XNDC1N-ZNF705EP-ALG1L9P readthrough (XRCC1 N-terminal domain containing 1, N-terminal like) (E9PLZ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPVKISHVVSFSSQDPKYPVENLLNPDSPRRPWLGCPQDKSGQLKVELQLERAVPTGYIDVGNCGCAFLQIDVGHSSWPLDRPFITLLPATTLMSLTDSKQGKNRSGVRMFKDGVVAHACNPSTLGDWDKWII
Protein: Respiratory nitrate reductase 2 alpha chain (EC 1.7.5.1) (P19319)
Organism: Escherichia coli (strain K12)
Function: This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth.
Subcellular location: Cell membrane; Peripheral membrane protein.
Interaction partners:
- Respiratory nitrate reductase 1 beta chain
- Respiratory nitrate reductase 2 beta chain
- Respiratory nitrate reductase 2 gamma chain
- Probable nitrate reductase molybdenum cofactor assembly chaperone NarW
- Nitrate/nitrite transporter NarU
- Respiratory nitrate reductase 1 gamma chain
- Nitrate/nitrite antiporter NarK
- Nitrate reductase molybdenum cofactor assembly chaperone NarJ
- Nitrite reductase large subunit
- Periplasmic nitrate reductase
Sequence:
MSKLLDRFRYFKQKGETFADGHGQVMHSNRDWEDSYRQRWQFDKIVRSTHGVNCTGSCSWKIYVKNGLVTWEIQQTDYPRTRPDLPNHEPRGCPRGASYSWYLYSANRLKYPLIRKRLIELWREALKQHSDPVLAWASIMNDPQKCLSYKQVRGRGGFIRSNWQELNQLIAAANVWTIKTYGPDRVAGFSPIPAMSMVSYAAGTRYLSLLGGTCLSFYDWYCDLPPASPMTWGEQTDVPESADWYNSSYIIAWGSNVPQTRTPDAHFFTEVRYKGTKTIAITPDYSEVAKLCDQWLAPKQGTDSALAMAMGHVILKEFHLDNPSDYFINYCRRYSDMPMLVMLEPRDDGSYVPGRMIRASDLVDGLGESNNPQWKTVAVNTAGELVVPNGSIGFRWGEKGKWNLESIAAGTETELSLTLLGQHDAVAGVAFPYFGGIENPHFRSVKHNPVLVRQLPVKNLTLVDGNTCPVVSVYDLVLANYGLDRGLEDENSAKDYAEIKPYTPAWGEQITGVPRQYIETIAREFADTAHKTHGRSMIILGAGVNHWYHMDMNYRGMINMLIFCGCVGQSGGGWAHYVGQEKLRPQTGWLPLAFALDWNRPPRQMNSTSFFYNHSSQWRYEKVSAQELLSPLADASKYSGHLIDFNVRAERMGWLPSAPQLGRNPLGIKAEADKAGLSPTEFTAQALKSGDLRMACEQPDSSSNHPRNLFVWRSNLLGSSGKGHEYMQKYLLGTESGIQGEELGASDGIKPEEVEWQTAAIEGKLDLLVTLDFRMSSTCLFSDIVLPTATWYEKDDMNTSDMHPFIHPLSAAVDPAWESRSDWEIYKGIAKAFSQVCVGHLGKETDVVLQPLLHDSPAELSQPCEVLDWRKGECDLIPGKTAPNIVAVERDYPATYERFTSLGPLMDKLGNGGKGISWNTQDEIDFLGKLNYTKRDGPAQGRPLIDTAIDASEVILALAPETNGHVAVKAWQALGEITGREHTHLALHKEDEKIRFRDIQAQPRKIISSPTWSGLESDHVSYNAGYTNVHELIPWRTLSGRQQLYQDHPWMRAFGESLVAYRPPIDTRSVSEMRQIPPNGFPEKALNFLTPHQKWGIHSTYSENLLMLTLSRGGPIVWISETDARELTIVDNDWVEVFNANGALTARAVVSQRVPPGMTMMYHAQERIMNIPGSEVTGMRGGIHNSVTRVCPKPTHMIGGYAQLAWGFNYYGTVGSNRDEFIMIRKMKNVNWLDDEGRDQVQEAKK
Protein: Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial (Glu-AdT subunit B) (EC 6.3.5.-) (Cytochrome c oxidase assembly factor PET112 homolog) (O75879)
Organism: Homo sapiens (Human)
Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000269|PubMed:9878253}.
Interaction partners:
- Glutamyl-tRNA
- Aspartate--tRNA ligase, mitochondrial
- Glutamyl-tRNA
- Asparagine--tRNA ligase, cytoplasmic
- Asparaginyl-tRNA synthetase
- Glutamine--tRNA ligase
- Fatty-acid amide hydrolase 1
- Fatty-acid amide hydrolase 2
- Aspartate--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
Sequence:
MAAPMLRWGCRGRRWAFARVDGGSCHRRGAPTGSTSNQIRGESSVAQQPLHTAQKTRKGEHKWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAVMTGLALNCHINKKSLFDRKHYFYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKQSQVIPKTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVVLEPDMSCGEEAATAVRELQLILQALGTSQANMAEGQLRVDANISVHHPGEPLGVRTEVKNLNSIRFLAKAIDYEIQRQINELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATSLPAGADPQQVINIDQIRETLPELPSVTREKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRAEPKKVTSWVLNTFLGYLKQQNLAVSESPVTPSALAELLDLLDSRTISSSAAKQVFEELWKREGKTPGQIVSEKQLELMQDQGALEQLCHSVMEAHPQVVMDVKNRNPRAINKLIGLVRKATQSRADPVMIKEILEKKLSL
Protein: Myelin gene regulatory factor-like A (Q54PT9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Transcription factor which acts as key regulator of pstA (prestalk-A) cells differentiation. Essential for ecmA-specific gene expression.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Extracellular matrix protein A
Sequence:
MDGYNQQQQQQQQQQQQHQMNLGSSGGILHSPQQQQQQQQQQQQQQQQPMNGSNNQLLGISNGGFGTMLQQSASLPINIQGSNSFSTFTPLSADDSNLKKRKIKNEDGTYSEIPYSPNSLVGSNGGLDSSFLMLQQQLQDQQQQIAQFNSSVNSPSFSLNSSQVNNNNNNNNNINNNNNSNNNINNNNSNNNINNNNNNNNNNNNNINNNNINNNNNYNNNNNNNNHNHLQTTTTTTTNNGLTINANNTPSQLSSSSLYPGIIPQISITNTQSGYTPRSISPNPSPNLSPTNSPIQSPHLPTDNYLMIGSENENSDPPSPMTQYNENPPFTWTDYKSEPWYTTFNTNGDEMPVPLLNIMASKGFSYIGGQWIYCRRNHFQLDITAVYPKLFQETQYGHNGVTLSNSSSSVDPTQTPSYMLISGVKTPINGLTLTIKGIKNRADMSQQESEVELFQTNSKREKQGEHAPKPVAIQFGSLVSIQRLHFRKATLNNARRHGQPNPHQEFNQLVVSLYGRCMGQEYCIVSYVSPALIVRTATQVTPPGDLSPVHTPDYAGTSSNNGGGSNNMNCFGPTISNIDFSTMNIVSPGHSPTSPRPLSQLTSQGQTNILRLTQNHNNNNNNNNNNNNNNNNNNNNNNNNNINNNNNSNNNSLGNINNNNSNMLTSSSLLNGRINCFNNNINNNNNNQHNNNNQHNNNNNHHNINNQHNNQNNNNNNNNNNKCHWNSGDTEKSIVYNGKVGINVENPAYALSVQGTIYASEGVYHPSDLRIKYDLKSIDSKSNLDNVNRMKLYDYKYNPQWTHMNGRDPYLDNCDRGVIAQDLQRILPNAVRTIGNKNVNGQEIENLLVIKNEALVMETIGATQELSKQMDEMKLKLITYESKLKNLKKKSKNQTILLIIFMITFLLVALYMYKPSTHHSHHRRHNFDNNDN
Protein: Transcription factor SOX-11 (P35716)
Organism: Homo sapiens (Human)
Function: Transcription factor that acts as a transcriptional activator. Binds cooperatively with POU3F2/BRN2 or POU3F1/OCT6 to gene promoters, which enhances transcriptional activation (By similarity). Acts as a transcriptional activator of TEAD2 by binding to its gene promoter and first intron (By similarity). Plays a redundant role with SOX4 and SOX12 in cell survival of developing tissues such as the neural tube, branchial arches and somites, thereby contributing to organogenesis (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:24886874, ECO:0000269|PubMed:35938035}.
Interaction partners:
- Histone H3.2
- Histone H4
- Histone H2A type 1-B/E
- Histone H2B type 1-K
- Transcription factor SOX-5
Sequence:
MVQQAESLEAESNLPREALDTEEGEFMACSPVALDESDPDWCKTASGHIKRPMNAFMVWSKIERRKIMEQSPDMHNAEISKRLGKRWKMLKDSEKIPFIREAERLRLKHMADYPDYKYRPRKKPKMDPSAKPSASQSPEKSAAGGGGGSAGGGAGGAKTSKGSSKKCGKLKAPAAAGAKAGAGKAAQSGDYGGAGDDYVLGSLRVSGSGGGGAGKTVKCVFLDEDDDDDDDDDELQLQIKQEPDEEDEEPPHQQLLQPPGQQPSQLLRRYNVAKVPASPTLSSSAESPEGASLYDEVRAGATSGAGGGSRLYYSFKNITKQHPPPLAQPALSPASSRSVSTSSSSSSGSSSGSSGEDADDLMFDLSLNFSQSAHSASEQQLGGGAAAGNLSLSLVDKDLDSFSEGSLGSHFEFPDYCTPELSEMIAGDWLEANFSDLVFTY
Protein: C-terminal binding protein 2, like (Ribeye b protein) (Q5BU17)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMAVRGTVPPPDYYPFDIALSAQPPEDLQGFYKANQHMLSRSGSHYGLSRTAWDQTRAATPGPPPPPPPPPPPPPPPPPSAHEISRMYRDSLSIKMIPDTQRIRSRAASPACFGVESGYPGHSIPADLNGYSLESCQPASTCIVVDPTASGMDGNIPRGTLSYGSVVTQRMPYDPAYDPGSAMVHASPAPLNTGMPAHHPSAGVDPKRNVDPSFLALLRSEGLSESTITLLLQQGFDSTSMLAMMEDHDVRSVAPNLGQARVLSRIVLNCKTGATVMRGRSNSFSHRNDLYMQPQSLGMDAQLMQQPPNALQSVSPRMGEFLGRRPSSAPSQHLLETTTYPASRPIGGLPVSPGGYTNALPQSRPLSMYNAHTGLAMSALPAQQQPPMTPGAAPKTFSGTYTPMELMKRPPNLPPLSPAHSPHLSPQLMRKGAAVENAVIPASSAVQTQNINANNKQTRRTGPPVIVSTMASPETSIRPQLVNGPLHPRPLVALLDGRDCTVEMPILKDLATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIVIRIGSGYDNIDIKAAGEMGIAVCNIPSAAVEETADSTLCHVLNLYRRNTWLYRALREGTRVQSVEQIREVASGAARIRGETLGLIGLGRSGQAVAVRAKVFGFNVIFYDPYLQDGLERSLGVQRVYTLQDLLYQSDCVSLHCNLNEHNHHLISDFTIKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFTQGPLKDAPNLICTPHTAWYSEQASLEMREAAATEIRRAITGRIPDSLRNCVNKEFFVTTAPWGVMEQQVHPELNGGAYRVAQPLPAVSPGGLQDKMYT
Protein: APC membrane recruitment protein 2 (Amer2) (XAmer2) (Protein FAM123A) (Q6INC4)
Organism: Xenopus laevis (African clawed frog)
Function: Negative regulator of the canonical Wnt signaling pathway involved in neuroectodermal patterning. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex.
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Note=Translocates to the cell membrane following binding to PtdIns(4,5)P2. {ECO:0000250}.
Interaction partners:
Sequence:
MDLHYDCAESPAAEQPSGKINKTAFKLFGKRRSGSAMPTIFGVKNKGDGKGTGNIGMVRSKTLDGLADVVLESNKKEEPCTNAGAGQLNTEKSPKVVTINPDVSSDSSVAKSHSFFSLLKRNGKSENVKGELAEQKPGSRQKRGLKGLFNSMRWSKKDKSYKDDKEGASENQPGLILPSSLTASLECIKEETQKPLCEKEKSEEDIPADVPSVEHSGDVNTSAEENPLNGCVESPCPALITKEPQLEDPPVIQQVDNLYQLPDPEVETLPDNKDEDVTGDIPVNTVSIVEPECDVGQEIAAPDPTTVDPPSEPSFDRICLMLADVTSLKSFDSLTGCGDVIADQDDDGGSSKGSKVVPGNGKKVTSKKNANIVAYQGGGEEMASPEEADETYVQELFSMIPQSEGASEKPEKVNGTTQVTAREVKCSDSGRDRNTVKPSKLRQVPIRRKERGDQNSKGNEKRQCHRNSDEGYWDSTTLGQEEEEPRSVGKQALPRDSCSGDALYDLYTDPDESIPKAQAEEPPVSHSHSKPLSPVTASCPVKTASSNKESKIPISIKHLPVHTTNQGIDSGSGSAAGHSHPVKSELPRTKIPVSKVLVRRVSNKAITETAAGKRAIHDPARKHH
Protein: Inner kinetochore subunit wip1 (CENP-W homolog) (Constitutive centromere-associated network protein wip1) (Histone-fold domain-containing protein new1) (G2TRL2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q2V2P8}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q2V2P8}.
Interaction partners:
- Probable thymidylate synthase
- Inner kinetochore subunit cnp20
- Inner kinetochore subunit mhf1
- Inner kinetochore subunit mhf2
- Histone H3-like centromeric protein cnp1
- Uncharacterized protein new2
- Vacuolar protein sorting-associated protein vts1
Sequence:
MSYPKARIRRFFRQHCQRSLESSALDLVYLDYCLFLQSLLKEANIEAAKTGERRVQPEHVRSIQRKILAQFKG
Protein: Phosphoethanolamine N-methyltransferase 2 (Phosphomethylethanolamine N-methyltransferase) (AtPMEAMT) (EC 2.1.1.103) (Q944H0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes N-methylation of phosphomonomethylethanolamine and phosphodimethylethanolamine, the two methylation steps required to convert phosphomonoethanolamine to phosphocholine. Unlike NMT1, NMT2 cannot utilize phosphoethanolamine as substrate in vitro.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable choline kinase 2
- Probable choline kinase 3
- Probable choline kinase 1
- Choline-phosphate cytidylyltransferase 2
- Choline-phosphate cytidylyltransferase 1
- Ethanolamine-phosphate cytidylyltransferase
- Probable ethanolamine kinase
- Phosphoethanolamine N-methyltransferase 3
- Phosphoethanolamine N-methyltransferase 1
- Serine decarboxylase
Sequence:
MATPYKEERDIQKSYWMEHSSDLTVEAMMLDSKASDLDKEERPEVLSLIPPYEGKSVLELGAGIGRFTGELAQKAGEVIALDFIESAIQKNESVNGHYKNIKFMCADVTSPDLKIKDGSIDLIFSNWLLMYLSDKEVELMAERMIGWVKPGGYIFFRESCFHQSGDSKRKSNPTHYREPRFYTKVFQECQTRDASGNSFELSMVGCKCIGAYVKNKKNQNQICWIWQKVSVENDKDFQRFLDNVQYKSSGILRYERVFGEGYVSTGGFETTKEFVAKMDLKPGQKVLDVGCGIGGGDFYMAENFDVHVVGIDLSVNMISFALERAIGLKCSVEFEVADCTTKTYPDNSFDVIYSRDTILHIQDKPALFRTFFKWLKPGGKVLITDYCRSAETPSPEFAEYIKQRGYDLHDVQAYGQMLKDAGFDDVIAEDRTDQFVQVLRRELEKVEKEKEEFISDFSEEDYNDIVGGWSAKLERTASGEQKWGLFIADKK
Protein: Aminoaldehyde dehydrogenase ALDH10A9, peroxisomal (EC 1.2.1.-) (4-trimethylammoniobutyraldehyde dehydrogenase ALDH10A9) (EC 1.2.1.47) (Aldehyde dehydrogenase family 10 member A9) (Aminobutyraldehyde dehydrogenase ALDH10A9) (EC 1.2.1.19) (Betaine aldehyde dehydrogenase ALDH10A9) (EC 1.2.1.8) (Gamma-guanidinobutyraldehyde dehydrogenase ALDH10A8) (EC 1.2.1.54) (Q9STS1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Dehydrogenase that catalyzes the oxidation of several aminoaldehydes. Metabolizes and detoxifies aldehyde products of polyamine degradation to non-toxic amino acids (Probable). Catalyzes the oxidation of 4-aminobutanal and 3-aminopropanal to 4-aminobutanoate and beta-alanine, respectively. Production of 4-aminobutinoate by ALDH10A9 may confer tolerance to salt stress. Catalyzes the oxidation of 3-aminopropanal to beta-alanine. Catalyzes the oxidation of 4-(trimethylamino)butanal and 4-guanidinobutanal to 4-trimethylammoniobutanoate and 4-guanidinobutanoate, respectively. Involved in glycine betaine biosynthesis. Catalyzes with low efficiency the oxidation of betaine aldehyde to glycine betaine.
Subcellular location: Peroxisome {ECO:0000269|PubMed:21053011, ECO:0000269|PubMed:27725774}.
Interaction partners:
- Choline monooxygenase, chloroplastic
- Aldehyde dehydrogenase family 7 member B4
- Aminoaldehyde dehydrogenase ALDH10A8, chloroplastic
- Delta-1-pyrroline-5-carboxylate synthase B
- Delta-1-pyrroline-5-carboxylate synthase A
- Ketose-bisphosphate aldolase class-II family protein
- Spermidine synthase 1
- Spermidine synthase 2
- Ornithine aminotransferase, mitochondrial
- Proline dehydrogenase 2, mitochondrial
Sequence:
MAITVPRRQLFIGGQWTEPVLRKTLPVVNPATEDIIGYIPAATSEDVELAVEAARKAFTRNNGKDWARATGAVRAKYLRAIAAKVIERKSELANLEAIDCGKPLDEAAWDMDDVAGCFEYYADLAEGLDAKQKTPLSLPMDTFKGYILKEPIGVVGMITPWNYPLLMAVWKVAPSLAAGCTAILKPSELASLTCLELADICREVGLPPGVLNILTGLGTEAGAPLASHPHVDKIVFTGSTTTGSSIMTSAAKLVKPVSLELGGKSPIIVFDDVDIDKAVEWTMFGCFWTNGQICSATSRLLVHERIADEFLDKLVKWTKNIKISDPFEEGCRLGPVVSKGQYERVLKFVSNARNEGATVLCGGVRPEHLKKGYFVEPAIVSNVTTSMEIWREEVFGPALCVKTFSTEDEAIQLANDSQYGLAGAVLSNDLERCDRVSKAFQAGIVWVNCSQPCFCQAPWGGTKRSGFGRELGEWGLENYLSVKQVTQYISDEPWGWYKPPSKL
Protein: Regulator of chromosome segregation (Q8DQ15)
Organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Function: Required for cell division and chromosome segregation. Binds to DNA and is involved in segregating the origin of replication (oriC) region to new daughter cells.
Subcellular location: Cytoplasm, nucleoid {ECO:0000269|PubMed:31182798}. Cell membrane {ECO:0000269|PubMed:31182798}; Peripheral membrane protein {ECO:0000269|PubMed:31182798}. Note=Localizes at mid-cell at first and then at the future site of division as the cell elongates. Forms one or two bright foci per cell mostly around mid-cell of small cells. Localizes toward the center of the daughter cell as the cell elongates. The bright foci mostly co-localize with origin of replication (oriC). During the cell cycle, very faint, but highly dynamic foci are homogeneously distributed all around the cell periphery. {ECO:0000269|PubMed:31182798}.
Interaction partners:
- Glycosyl hydrolase family 25
- Amphipathic pore-forming peptide
- Chromosome replication initiation protein/membrane attachment protein, Putative
- Transcriptional repressor for Zn
- GP-PDE domain-containing protein
- Septum formation initiator family protein
Sequence:
MSIEMTVSEIAEVLGLSRQAINNRVKELPEEDTDKNDKGVTVVTRSGLIKLEEIYKKTIFEDEPVSEDVKQRELMEILVDEKNAEILRLYEQLKAKDRQLSEKDEQMRIKDRQIAEKDKQLDQQQQLTLQAMKDQENLKLELDQAKEEVQSTKKGFFARLFGG
Protein: 75 kDa invariant surface glycoprotein, putative (Q57VX6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTMPVTLCTTATVFLLCGICALDVTWAEELSVAQKQYVTAHGRQLDGEAAATLCTMKKLLDGVNSRVDTFEQQIYMYVNNANANFRKISDDKVMAASLSGDQHQQMQYMKTRLDDIAYLMNATEGRAKKAAANASAALDEVLKWHCVDRTESRESSYSSTPNANCEPNAYKRDYYYEHSRLDPHKYSILCNYKVVSSTTTQTTFSNMERALEIWNQVKPKPYHMRVMICGAGAPVHQAAPPGRPCTVLENWMRSYEVATHLIARLHRDLDVALFVYRYSEKILESSKESLAQHEERRKAAEARAAEEEAKRQAAEKAAEEARKAFEEAEARRVAAEEQAEARRLEAEKAEKAKEAGQPVSEEKKKMLLEAVEKAEATEKAAEKQAKDSRKAFEEAEEERVKATEDAEAAKQNRDTIGRSEEELKKDVEKLAEELKEESKESGEEDDVNADHDDEGSEAKSGWIGTTKVLVFLIPLLLLLLGLLVFFVIRGRRKAEVKDDINIEEGGAKSKNTKTAAGLDSDI