wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein C18B11.11 (Q09716)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- GTP-binding protein rhb1
- Tuberous sclerosis 1 protein homolog
Sequence:
MKALDIDTILTQISNQQSLDKRYKRIKRLINNEQFCKNVILQKLVDSTKDIIENKVHGNILAATISLWTHAAEKHKEMSSDDRALLFNELSKVPNSEYYPATVDALIVITSQGERTESFSNDILKVLSEWLTDLFTIIDDMRAQSRKSFKGSAELRNYTRCFRQIILLLTNMFRVGFNLFDEMEVSSMLANCVWVSKSTTDEEDIALVFSLLNCIISYGRISSAVLYSIVEVVCRAKFGLVASSQSAQQIVEKLLKTATKYEALNSLKRIMEETDEGSYIAIMGGIQIVSALFTDIPRSVYCTRGMLLGFLQRSLKNKSSRIALETTRSLYNALERRSFVEVLYADEWISLLDLLVEISSSLPKSLNYRPGTWQHIEPNIIESIASYQLQHLLLFNEILKPDSNHFVLEKFHEFLKINFSYLTPTLSQKLFTVLDLRSQLPYSEGWLEDQTILLKSYFDTSFSLDFHVYLIGLFRKVLFACPVELRPEVYARMLCPLVKSLDKSSSEVIIDEVISLVCDLSWIYPSNVFHEVKDSLCFYAHNSSNGDLQLRSIQAIVSLTFYYVLLPEFKSVLYDGLVEISCDFKIRRTFRIPVLKLLLQLRINTNDYCFVNLSPAQLELISVYSTQWHNPFISEEAQRCRDNKVKDRDLSFSPVFQKFPLKVNTSATLSKDLMSLPINEWVKNVMYIVTHETDWKVVQYILINFTNQLRNTKMFTKTVEALQLLLNSLRDIINGKQSLNINFSDFFRIEDLLVSLSKILSVLMVYKDVLPPTAHEQFFQLLNRFAEKGDKTMESCIDTLITNCCAMQSFSIMHLPKFFSITMSSNLSERSLVNFLRLLHVVSDNWELNEGLEKETIQSICLFCLKVIRTKKEELDGHKKLVNPNTKVFCLYLVSFSYSIISNLFLGCETTERAQLASFLLKEFLNLKNGSHFEGYERVFYELLLRYTYSDERIESYPSDSRFHFNSSSKSWLYRGCVITINAEYETGDYQMILRRMSGTTIYRFWRNMRDRGAFEKSLMMEQSMVSSELKQKYLQEIAASHVFMETVLSPLDSPDEEPILIKPDARTEELIQSLDATHTKPVINIAVALQAGDVSDINTTVGWQLFYRLLESFGHEKKLDNGETIYVWQSKTIEMIFRYVSDPAEALESSLYSSLIIIGSDDLVGPDSLNWDSVDVPVIIKISLDSHLDALKMFDTLFHVKLEIITTGTDISHQSFWKLDQIISTNSIAPLLHSYLADIGLYQMIFENFAYVHPWLLRQQYIDTLYTIHQVPTTQRESSALPSDKTFDFTLFL
Protein: FI01822p (Q8IMT6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- CCR4-NOT transcription complex subunit 11
- CCR4-NOT transcription complex subunit 10
Sequence:
MTDKLDAEQFNDDELEAPAWLNRQFIEEILSAYEDSPELKVVDLKITPASAQGDHYASVMFRTTAECTTAKGKFSRPLIIKAMPEQDGHKKDMLSESHLFETEIGMYCQVLPEFERILRESGDDTKLFVPCIYHSLEPRKVMIFEDLVPQGYYVIRDRPVAQEELKTAFAKLAKWHAISMKYIKEQPDFLKEFKYGLFEMPTVKTDPFITTGMQSFIEMLDRLPELRKYKPHFEKIKDKYMQRLQAVMKEYHENRKSDAFYVLCHGDFHLRNMMFKNNKGTGAHEDTMLVDFQISNLCPITIDLTYSIYMLMEPEQRREMGKDLINHYLTVLVATLKSIGYPGELPTQAKLWDEIHKNKYYDFFLLSTFLPLILAIKSKSFKVNDLIQDPETRQKTYFLDTYVKDVSKLLPKFEQLGYFKCL
Protein: Supervillin (Archvillin) (p205/p250) (O46385)
Organism: Bos taurus (Bovine)
Function: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation. Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (By similarity).
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, invadopodium {ECO:0000250|UniProtKB:O95425}. Cell projection, podosome {ECO:0000250|UniProtKB:O95425}. Midbody {ECO:0000269|PubMed:20309963}. Cleavage furrow {ECO:0000269|PubMed:20309963}. Note=Tightly associated with both actin filaments and plasma membranes.
Interaction partners:
Sequence:
MKRKERIARRLEGIETDTQPILLQSCTGLVTHRLLEEDTPRYMRATDPASPHIGRSNEEEETSDSSLEKQTRSKQCTETSGIHADSPYSSGIMDTQSLESKAERIARYKAERRRQLAEKYGLTLDPEADSETPSRYSRSRKDPEAAEKRGVRSERSAESSRDAGSSYSRTELSGLRTCVAESKDYGLHRSDGVSDTEVLLNAENQRRGQEPSATGLARDLPLAGEVSSSFSFSGRDSALGEVPRSPKAVHSLPSPSPGQPASPSHSTSDLPLPAEARASIGKPKHEWFLQKDSEGDTPSLINWPSRVKVREKLVREESARSSPELTSESLTQRRHQTAPGHYLAFQSENSAFDRVSGKVASSARQPIRGYVQPAEPVHTITLVTSDTPESISEGSWVGPAPQTVTKPPPSKVLEGERRDTPVLHICESKAEDVLFSDALEKTRKTLAVLEDRGSGRSQEAPSGTEDLSQPAVGIVTAEPQKESESLAHPPMAQQQPTERMGRSEMVMYVQSEAVSQGHRKEVPTRKHRVLTRSLSDYTGPPQLQALKAKAPAPKRDAESQTSKAELELGLLDTKVSVAQLRNAFLESARASRKPELHSRVEGSSEGPGVERERGSRKPRRYFSPGENRKTSERFRTQPITSAERKESDRSTSNSEMPAAEDEEKVDERARLSVAAKRLLFREMEKSFDEKSVPKRRSRNAAVEQRLRRLQDRSHTQPVTTEEVVIAAEPTPASCSVATHPVMTRHPSPTVAKSPVQPARTLQASAHQKALARDQTNESKDSAEQGEPDSSTLSLAEKLALFNKLSQPVSKAISTRNRLDMRQRRMNARYQTQPVTLGEVEQVQSGKLMAFSPTINTSVSTVASTVPPMYAGNLRTKPLPDDSFGATEQKFASSLENSDSPVRSILKSQGWQPSVEGAGSKAMLREFEETERKGGLTGGDGGVTKYGSFEEAELSYPVLSRVREGDNHKEAIYALPRKGSLELAHPPIAQLGDDLKEFSTPKSTMQASPDWKERQLFEEKVDLENVTKRKFSLKAAEFGEPTSEQTGAAAGKPAAPTATPVSWKPQDPSEQPQEKRYQSPCAMFAAGEIKAPAVEGSLDSPSKTMSIKERLALLKKSGEEDWRNRLNRKQEYGKASITSSLHIQETEQSLKKKRVTESRESQMTIEERKHLITVREDAWKTRGKGAANDSTQFTVAGRMVKRGLASPTAITPVASPVSSKARGTTPVSRPLEDIEARPDMQLESDLKLDRLETFLRRLNNKVGGMQETVLTVTGKSVKEVMKPDDDETFAKFYRSVDSSLPRSPVELDEDFDVIFDPYAPRLTSSVAEHKRAVRPKRRVQASKNPLKMLAAREDLLQEYTEQRLNVAFVESKRMKVEKLSANSSFSEVTLAGLASKENFSNVSLRSVNLTEQNSNNSAVPYKKLMLLQVKGRRHVQTRLVEPRAPSLNSGDCFLLLSPHHCFLWVGEFANVIEKAKASELASLIQTKRELGCRATYIQTVEEGINTHTHAAKDFWKLLGGQASYQSAGDPKEDELYETAIIETNCIYRLMDDKLVPDDDYWGKIPKCSLLQSKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGTFDYENCDINPLDPGECNPLIPRKGQGRPDWAIFGRLTEHNETILFKEKFLDWTELKRPNEKNASELAQHKDDARAEVKPYDVTRMVPVPQTTAGTVLDGVNVGRGYGLVEGDDRRQFEIASISVDVWHILEFDYSRLPKQSIGQFHEGDAYVVKWKFIVSTAVGSRQKGEHSVRVAGKEKCVYFFWQGRQSTVSEKGTSALMTVELDEERGAQVQVLQGKEPPCFLQCFQGGMVVHSGRREEEEENTQSEWRLYCVRGEVPVEGNLLEVACHCSSLRSRTSMVVLNVHKALIYLWHGCKAQAHTKEVGRTAANKIKDQCPLEAGLHSSSKVTIHECDEGSEPLGFWDALGRRDRKAYDCMLQDPGNFNFTPRLFILSSSSGDFSATEFMYPARDPSVVNSMPFLQEDLYSAPQPALFLVDNHHEVYLWQGWWPIENKITGSARIRWASDRKSAMETVLQYCRGKNLKKPPPKSYLIHAGLEPLTFTNMFPSWEHREDIAEITEMDTEVSNQITLVEDVLAKLCKTIYPLADLLARPLPEGVDPLKLEIYLTDEDFEFALDMTRDEYNALPAWKQVNLKKAKGLF
Protein: Hoefavidin (A9D857)
Organism: Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43)
Function: The exact role played by hoefavidin in the host organism is still obscure. Forms a strong non-covalent complex with biotin and 2-iminobiotin.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MNKVLAIVLTITVAGFAQTAFADDHAMSPDMKLLAGASNWVNQSGSVAQFVFTPSPTQPQTYEVSGNYINNAQGTGCKGTPYPLSGAYYSGNQIISFSVVWSNASANCQSATGWTGYFDFSGSQAVLKTDWNLAFYSGSTPAIQQGQDDFMQSVATVSESLLTE
Protein: Transcription initiation factor TFIID subunit 8 (Protein prodos) (Q9VWY6)
Organism: Drosophila melanogaster (Fruit fly)
Function: TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors.
Subcellular location: Nucleus.
Interaction partners:
- Transcription initiation factor TFIID subunit 6
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 7
- IP01149p
- Transcription initiation factor TFIID subunit 1
- TBP-associated factor 3
Sequence:
MEKVEAVTVSNVDPYRRILNKVVSQLLLDKGAGQASNHSLETLTQMLQALIWEIGNSAHNYCELSGRTMPTVGDVSLALINMGISISNLDPYMRKETHVPIPLPPQQTQQRPLSLLQAGIKAPHPHYVPSYFPPMPDPHAYIRTPTHKQPVTEYEAIREKAACQKRDIEKALTKFLCKTTETNNLFPTEDNMFPLIACKPAFPPYAAALNPTDQVFDFEELEYHYLVANRTEDEPSKDDGEEGDSENEEMDGDKSKEEKPELDIKPNSNTNKAILENPNIDNPYLRAATLPKRSKNCPTPGTMPSRSLATTAPTIRTPSTLEITKTNL
Protein: Centromere/kinetochore protein zw10 (Mitotic 15 protein) (Q9W4X9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. Required for the assembly of the dynein-dynactin, Mad2 complexes and spindly/CG15415 onto kinetochores. During cytokinesis in male meiotic cells it is required for completion of cleavage furrow ingression, possibly in conjunction with Rint1. Required for maintenance of Golgi stack number and morphology, and acroblast assembly. Its function related to the spindle assembly machinery is proposed to depend on its association in the RZZ complex. Failure to assemble the complex due to the absence of any one of its components, results in the incorrect redistribution of the remaining components to diverse membrane compartments.
Subcellular location: Cytoplasm. Nucleus. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:1339459, ECO:0000269|PubMed:22685323}. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22685323}. Golgi apparatus {ECO:0000269|PubMed:22685323}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:22685323}. Note=Dynamic pattern of localization during the cell cycle (PubMed:22685323). Present in structures resembling Golgi stacks prior to their migration into the nuclear zone during prometaphase (PubMed:1339459, PubMed:22685323). At metaphase, detected at the kinetochores and kinetochore microtubules (PubMed:1339459, PubMed:22685323). During anaphase and telophase accumulates at the spindle envelope midzone and broad areas at the cell poles where they often become concentrated in small structures that resemble small Golgi-derived vesicles (PubMed:22685323). In late telophase they also form compact aggregates at the interior of the equatorial region of the cell (PubMed:22685323). {ECO:0000269|PubMed:1339459, ECO:0000269|PubMed:22685323}.
Interaction partners:
- Rough deal
- RINT1-like protein
- Protein zwilch
- Syntaxin-18
- Vesicle transport protein USE1
- Dynactin subunit 2
- Secretory 22, isoform B
- Spindly
- GH11193p
- Kinetochore protein NDC80
Sequence:
MEEEAPRFNVLEEAFNGNGNGCANVEATQSAILKVLTRVNRFQMRVRKHIEDNYTEFLPNNTSPDIFLEESGSLNREIHDMLENLGSEGLDALDEANVKMAGNGRQLREILLGLGVSEHVLRIDELFQCVEEAKATKDYLVLLDLVGRLRAFIYGDDSVDGDAQVATPEVRRIFKALECYETIKVKYHVQAYMLQQSLQERFDRLVQLQCKSFPTSRCVTLQVSRDQTQLQDIVQALFQEPYNPARLCEFLLDNCIEPVIMRPVMADYSEEADGGTYVRLSLSYATKEPSSAHVRPNYKQVLENLRLLLHTLAGINCSVSRDQHVFGIIGDHVKDKMLKLLVDECLIPAVPESTEEYQTSTLCEDVAQLEQLLVDSFIINPEQDRALGQFVEKYETYYRNRMYRRVLETAREIIQRDLQDMVLVAPNNHSAEVANDPFLFPRCMISKSAQDFVKLMDRILRQPTDKLGDQEADPIAGVISIMLHTYINEVPKVHRKLLESIPQQAVLFHNNCMFFTHWVAQHANKGIESLAALAKTLQATGQQHFRVQVDYQSSILMGIMQEFEFESTHTLGSGPLKLVRQCLRQLELLKNVWANVLPETVYNATFCELINTFVAELIRRVFTLRDISAQMACELSDLIDVVLQRAPTLFREPNEVVQVLSWLKLQQLKAMLNASLMEITELWGDGVGPLTASYKSDEIKHLIRALFQDTDWRAKAITQIV
Protein: Metal transporter cnnm-4 (CNNM family homolog 4) (Q17586)
Organism: Caenorhabditis elegans
Function: Probable metal transporter. Probably acts redundantly with the other metal transport proteins cnnm-1, cnnm-2, cnnm-3 and cnnm-5 to regulate Mg(2+) homeostasis.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- DBD_Tnp_Mut domain-containing protein
- Probable GMP synthase
Sequence:
MELYAAGRYDSEPFKMNEHDIIQLYGEDVQYVKNAFLSSDSTCNNNVYSLEEHELDDDKKNLSGVLVEYKIKISLLQSSDGVKHLFFCTNPKSVDIARMLEIPEGKDKTRVYFMMPLLVLCLGLSATFSGLNLAIMSFSINDLKLIQESDSDKLMKQRAMDVMRLRRNSNFVLVTIIFGNCFCNISITLLMNYFAEFYGFGGFIFVELISTALLLIFTEILPSLIFTKNALAIASRLQYFVIFTMCITSPISYPLAMLLNIILGKENADDSAPLDLDALQIDELEDEEAADGNNFHEMMSVVKKTIKLREKLASDVMTEIDKVGMYSEHQQVTHSFLLDAYEQGHSRLPVYEGETRNKIRGVLNITDMMLLMDDEGRGSDTDLTLGTMLSVLEKRRKHCFVLDTMPVEHFMSELQQGCPMAIVVRYKEVDSEEDGTEIYEVCGIVTLEDCIEEILGEIFDEKDARQE
Protein: Bifunctional purine biosynthetic protein ADE5,7 [Includes: Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (Glycinamide ribonucleotide synthetase) (GAR synthetase) (GARS) (Phosphoribosylglycinamide synthetase); Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIR synthase) (AIR synthetase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase)] (J9VYP5)
Organism: Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii)
Function: Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P20772}.
Interaction partners:
Sequence:
MPEITAFPQPKSDLSILLLGAGGREHALAFKLAQSSRVARIVVCPGNGGTALMGGKVSNLALPWGAPPAFRSIVEWAQKENIDLVVPGPEQPLVDGVEGAFKKVGIPVFGPSPAAAMLEGSKSLSKEFMARHNIPTAAFRSFTSTQYEDAVAYIKSKPFTSGRSVIKASGLAAGKGVLIPETDEEAFAALKSVMVDKEFGDAGDEVVVEEYLSGPEISVLAFSDGYTIVPMPAAQDHKRIGEGDTGLNTGGMGAYAPAPIATKEIMERCVKDVLEPTIKGMREDGYPFVGMLFTGFMITADGPRVLEYNVRFGDPETQALMLLLDEQTDLAEVLLACVERRLDSIKLGYKQGYAVSVVLASEGYPGSYPKGLPMTLNPTPEGVEVFHAGTKRSDNVTVTDGGRVLAVCASAPTLRAAVDLAYSGISQISFQGQTFRRDIAYRALSSEPPAEPKGLTYAAAGVSVDAGNDLVEAIKPVVKATRRPGADSDIGGFGGAFDLAKAGYKDPILVSGTDGVGTKLRVALDHGKHNTVGIDLVAMSVNDLIVQGAEPLYFLDYYACSKLDVPVAADVITGIAEGCLQAGCALIGGETAEMPGMYHGDDYDLAGFAVGVVERAQILPTPDIASGDVLLALSSSGPHSNGFSLIRKIVSLSNLSLHDTAPWDKNTSVGDALLTPTKVYIKPLLPGIKSGLYKGMSHITGGGFTENIPRIFSSASNLGVKLDLTSYSLPAIWKWLMRAGNVEAKEMVRTFNCGVGMIIIVAKDKADAALSSLKENGEEAWVIGEVQEKKGVEYVGLDKFGL
Protein: Galactonate operon transcriptional repressor (HTH-type transcriptional repressor DgoR) (P31460)
Organism: Escherichia coli (strain K12)
Function: Involved in the regulation of D-galactonate metabolism. Represses the expression of the dgoRKADT operon by binding to two closely spaced inverted repeats in the cis-acting element, which overlap with the D-galactonate responsive dgo promoter. Employs a derepression mechanism using D-galactonate as a specific effector molecule.
Interaction partners:
- 2-dehydro-3-deoxygalactonokinase
- D-galactonate dehydratase
- 2-dehydro-3-deoxy-6-phosphogalactonate aldolase
- D-galactonate transporter
- Exu regulon transcriptional regulator
- Uncharacterized protein YjiH
- Uncharacterized protein YidR
Sequence:
MTLNKTDRIVITLGKQIVHGKYVPGSPLPAEAELCEEFATSRNIIREVFRSLMAKRLIEMKRYRGAFVAPRNQWNYLDTDVLQWVLENDYDPRLISAMSEVRNLVEPAIARWAAERATSSDLAQIESALNEMIANNQDREAFNEADIRYHEAVLQSVHNPVLQQLSIAISSLQRAVFERTWMGDEANMPQTLQEHKALFDAIRHQDGDAAEQAALTMIASSTRRLKEIT
Protein: B-cell scaffold protein with ankyrin repeats (Q8NDB2)
Organism: Homo sapiens (Human)
Function: Involved in B-cell receptor (BCR)-induced Ca(2+) mobilization from intracellular stores. Promotes Lyn-mediated phosphorylation of IP3 receptors 1 and 2.
Interaction partners:
- Tyrosine-protein kinase Blk
- B-lymphocyte antigen CD20
- Tyrosine-protein kinase Lyn
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- PX domain-containing protein kinase-like protein
- Tyrosine-protein phosphatase non-receptor type 22
- PHD and RING finger domain-containing protein 1
- Interferon regulatory factor 5
- Protein Niban 3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
Sequence:
MLPAAPGKGLGSPDPAPCGPAPPGNTKDIIMIYEEDAEEWALYLTEVFLHVVKREAILLYRLENFSFRHLELLNLTSYKCKLLILSNSLLRDLTPKKCQFLEKILHSPKSVVTLLCGVKSSDQLYELLNISQSRWEISTEQEPEDYISVIQSIIFKDSEDYFEVNIPTDLRAKHSGEISERKEIEELSEASRNTIPLAVVLPTEIPCENPGEIFIILRDEVIGDTVEVEFTSSNKRIRTRPALWNKKVWCMKALEFPAGSVHVNVYCDGIVKATTKIKYYPTAKAKECLFRMADSGESLCQNSIEELDGVLTSIFKHEIPYYEFQSLQTEICSQNKYTHFKELPTLLHCAAKFGLKNLAIHLLQCSGATWASKMKNMEGSDPAHIAERHGHKELKKIFEDFSIQEIDINNEQENDYEEDIASFSTYIPSTQNPAFHHESRKTYGQSADGAEANEMEGEGKQNGSGMETKHSPLEVGSESSEDQYDDLYVFIPGADPENNSQEPLMSSRPPLPPPRPVANAFQLERPHFTLPGTMVEGQMERSQNWGHPGVRQETGDEPKGEKEKKEEEKEQEEEEDPYTFAEIDDSEYDMILANLSIKKKTGSRSFIINRPPAPTPRPTSIPPKEETTPYIAQVFQQKTARRQSDDDKFCGLPKKQDRARIESPAFSTLRGCLTDGQEELILLQEKVKNGKMSMDEALEKFKHWQMGKSGLEMIQQEKLRQLRDCIIGKRPEEENVYNKLTIVHHPGGKETAHNENKFYNVHFSNKLPARPQVEKEFGFCCKKDH
Protein: Transcription factor MYB7 (Myb-related protein 7) (AtMYB7) (Myb-related protein Y49) (AtY49) (Q42379)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in the negative regulation of flavonol biosynthesis. Represses the early phenylpropanoid genes, phenylalanine ammonia-lyase (PAL), cinnamate 4-hydroxylase (C4H) and 4-coumarate-CoA ligase (4CL), as well as the flavonoid-specific genes, flavonoid 3'-hydroxylase (F3'H) and dihydroflavonol 4-reductase (DFR). Plays a role in seed germination inhibition. Negatively regulates the expression of the abscisic acid (ABA) signaling transcription factor ABI5 in seeds.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:25053018, ECO:0000269|PubMed:26332741}.
Interaction partners:
- Trans-cinnamate 4-monooxygenase
- Dihydroflavonol 4-reductase
- Transcription factor TT8
- NAC domain-containing protein 12
Sequence:
MGRSPCCEKEHMNKGAWTKEEDERLVSYIKSHGEGCWRSLPRAAGLLRCGKSCRLRWINYLRPDLKRGNFTHDEDELIIKLHSLLGNKWSLIAARLPGRTDNEIKNYWNTHIKRKLLSKGIDPATHRGINEAKISDLKKTKDQIVKDVSFVTKFEETDKSGDQKQNKYIRNGLVCKEERVVVEEKIGPDLNLELRISPPWQNQREISTCTASRFYMENDMECSSETVKCQTENSSSISYSSIDISSSNVGYDFLGLKTRILDFRSLEMK
Protein: Ssr2857 protein (P73213)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Probable copper-transporting ATPase PacS
- Cation-transporting ATPase E1-E2 ATPase
- Slr0240 protein
Sequence:
MTIQLTVPTIACEACAEAVTKAVQNEDAQATVQVDLTSKKVTITSALGEEQLRTAIASAGHEVE
Protein: Katanin p80 WD40 repeat-containing subunit B1 (Katanin p80 subunit B1) (p80 katanin) (Q4VFZ4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|HAMAP-Rule:MF_03022}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03022}. Note=Predominantly cytoplasmic. Localized to the interphase centrosome and mitotic spindle poles. Localizes within the cytoplasm, partially overlapping with microtubules, in interphase and to the mitotic spindle and spindle poles during mitosis. {ECO:0000256|HAMAP-Rule:MF_03022}.
Interaction partners:
- Katanin p60 ATPase-containing subunit A1
- Katanin p60 ATPase-containing subunit A-like 1
- Katanin p60 ATPase-containing subunit A-like 2
- Katanin regulatory subunit B1 like 1
- Gamma-tubulin complex component
- Spastin
Sequence:
MATPVVTKTAWKLQEIVAHASNVSSLVLGKASGRLLATGGDDCRVNLWSINKPNCIMSLTGHTSPVESVRLNTPEELIVAGSQSGSIRVWDLEAAKILRTLMGHKANICSLDFHPYGEFVASGSQDTNIKLWDIRRKGCVFRYRGHSQAVRCLRFSPDGKWLASAADDHTVKLWDLTAGKMMSEFPGHTGPVNVVEFHPNEYLLASGSSDRTIRFWDLEKFQVVSCIEGEPGPVRSVLFNPDGCCLYSGCQDSLRVYGWEPERCFDVVLVNWGKVADLAICNDQLIGVAFSQSNVSSYVVDLTRVTRTGTVTQDPVQASQPQTQQTPNPGVSLRRIYERPSTTCSKPQRVKHNSESERRSPSSEDDKDERESRAEIQNAEDYNEIFQPKNSISRTPPRRSEPFPAPPEDDIATAKEASKPSPAMDVQLPVPSQEVPARPSVMTSTPAPKGEPVIIPATRNEPIGLKASDFLPAVKVPQQAELVDEDAMSQIRKGHDTMCVVLTSRHKNLDTVRAVWTTGDIKTSVDSAVAINDLSVVVDLLNIVNQKASLWKLDLCTTVLPQIEKLLQSKYESYVQTGCTSLKLILQRFLPLITDILAAPPSVGVDISREERLHKCRLCFKQLKSISGLVKSRSGLSGRHGSAFRELHLLMASLD
Protein: Centrosomal protein of 162 kDa (Cep162) (Protein QN1 homolog) (Q6ZQ06)
Organism: Mus musculus (Mouse)
Function: Required to promote assembly of the transition zone in primary cilia. Acts by specifically recognizing and binding the axonemal microtubule. Localizes to the distal ends of centrioles before ciliogenesis and directly binds to axonemal microtubule, thereby promoting and restricting transition zone formation specifically at the cilia base. Required to mediate CEP290 association with microtubules (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Nucleus {ECO:0000250}. Note=Localizes to the distal end of centrioles throughout the cell cycle. During ciliogenesis, found at the cilia base. Localizes to spindle microtubules during mitosis (By similarity). {ECO:0000250}.
Interaction partners:
- Centrosomal protein of 290 kDa
Sequence:
MAHYFKVDLDEEFERFMKELSDDSFENSNKTPRQPNEDNKEMKKKDPVPWWIAEDDFEDDGLLGTNVSYLKTKKTYQPVMDTEEESAEKVQFLKSSGTSILSVDSLEANELVVSEPHHSTLGLGLDTLEEQEEKEQFFARLEKGLTSSIDYSKLNQELDSDDSAQLKALHRYPRNTEPAEDGCENESEQEELPETYSDDFEDAEDADDPLITKDEETHPKENSESGKDSFPKQEEEKTGMLANVVLLDSFDSVEDVGLSSQEKATPKAKAPPEITDDGPAETGVPYGQSSGDTEALHQAYCHVAHSLGDTGEPRIEASTVQTVRSSIKDGLQENEESSKNVSTTESDLPTVEELMQPIRIDSYGIRAFDLQPISLKKATDSKEAESVGSLPLKTNTNTVSQDTRHAIQFPHKHDESVVLHRTADEGMGSSCPATEEHLDKMYLEILKKKTSVNPSLLPQDDKMNQTSRSQLGAGEEVPVIGKQVPCKKARSTPSLPKRKPQSGLYASARSSGYGKPSSPLQLFSALEKKTSKDNTKTKSVRSIPTSNQFRKREILSGTKLIKPAASNKPSPHREGSPATPKRPEDPSDDSFVQLQTEPLGSYGGNREKELLMLKRAQDAEEKWTGAQALMEQMKMTFCEKEKELENTVESLKRQQERELFRLNQENYILQAKLSSFEETSRKQRWLQFGETSDPLTGEKLKQIQKEIQEQETLLQGYQQENERLYNQVKDLQEQNKKNEERMFKENQNLFSELASLKEQMHKNHFLSQAVENTEPTKNQSFTDLLAELRAAQKEKNHLMEDIKRLKQDKQALEVDLEKVKRERDQAKDQIAYATGEKLYEIKILEETHKQEVSRLQKRLQWYAENQELLDRDAARLREANEETEKLRLEIEKLKTESGSPATQQRLRSKERALDAKRIQDLERQVKEMEGILKRRYPNSLPALILAASAAGDSVDRNTVEFMERRIKKLEADLEGKDEEAKKSLRTMEQQFQKMKIQYEQRLEEQEQLLAHRQKEAPQSQRNSSSRLKALETELGDIKEAHQITVRKLEAEIDVLKHQNADLEHKKNDKGDQGLQSIEFQVEQAQARAKLARLNEELAAKGREIQDLTKTVERLQKERRMMLSRQIPRSREETAAKRLKKDPNRGHGNAFPETLDGKLYHPHTFTDSHISEVLEENYRLRSELEGLILERSKLKMESEAAVCQLENSMKRVKDDAAAHIASLKASHEREIEKLLCQNAIENSSSKVAELNRKIATQEVLLKHFQGQVNELQGKQESLAVSQVREEILQKQITKLLEELKEAKENHTPEMKHFMGLERKIKQMEMRHRQREQELQQIIQQTRQVVETEQNKEVEKWKRLAQLKNRELDKFRTELDSILDVLRELHRQGVVVPMALAGEENTAEF
Protein: DNA polymerase II subunit 2 (Q38CZ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA polymerase epsilon catalytic subunit
- Transcription factor CBF/NF-Y/archaeal histone domain-containing protein
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM3
- Cell division cycle 45
- GINS subunit domain-containing protein
- Uncharacterized protein
- DNA replication complex GINS protein SLD5
- DNA polymerase
Sequence:
MDYRNDIQQLARAHQFRLHPLALKGLSDYLATLNGNIDAQRNALRDIFALLHRACGLERFVDGEKVKSVVSLHSSKVQGAIDGVVPTVDVLSLDDTPYAYIDEWSGEVRVQSTRQHGDRFTVLNQRYLFARKRCLRSGLFSRDSSKQPIDQGLPSLVPSIALEGIDPSDTVAVLGMLVKHSSATYLEDIYGRVKLIMRGCVHPPVGVVGEGFFVVVKGQWVGGLFVVASVDLPPAERREDTLRVVGSDFDLFGRRPDDVVAAFRREKTSLGSVVIVMSQIHLDQRSTVDSLISFFREMQNRSEAELTDTTLVMVGEFCSSPIHYDDVSHLPEPFEGCDRYRSLMNILATVITVHAPSVAQLTQVVIVPGCGDITGLLGVLPQPPIVSTFGKVLQARLKKVVLAPNPCRLRFFTHEMIVVRRDFSRSLREKERTFEWSRHEASTPVISFESIAKTILDEAHLAPGVTEGILWKADKALCLPVLPHLLVMCDSTEQWECSYKGVRIVNPGPFSLGKTFLWYTPADGECSLSSVDDQV
Protein: Cadherin-10 (T2-cadherin) (P70408)
Organism: Mus musculus (Mouse)
Function: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Cadherin-2
- Cadherin-3
- Cadherin-7
- Cadherin-20
- Cadherin-6
- Cadherin-11
Sequence:
MTIYQFLRLFVLWACLPHFCCPELTFRRTPGIQQMTAESRAPRSDGKILHRQKRGWMWNQFFLLEEYTGSDYQYVGKLHSDQDKGDGSLKYILSGDGAGTLFIIDEKTGDIHATRRIDREEKAFYTLRAQAINRRTLRPVEPESEFVIKIHDINDNEPTFPEEIYTASVPEMSVVGTSVVQVTATDADDPSYGNSARVIYSILQGQPYFSVEPETGIIRTALPNMNRENKEQYQVVIQAKDMGGQMGGLSGTTTVNITLTDVNDNPPRFPQNTIHLRVLESSPVGTAVGSVKATDADTGKNAEVDYRIIDGDGTDMFDIITEKDTQEGIITVKKPLDYENRRLYTLKVEAENTHVDPRFYYLGPFKDTTIVKISIEDVDEPPVFSRSSYLFEVHEDIEVGTIIGTVMARDPDSTSSPIRFTLDRHTDLDRIFNIHSGNGSLYTSKPLDRELSQWHNLTVIAAEINNPKETTRVSVFVRILDVNDNAPQFAVFYDTFVCENARPGQLIQTISAVDKDDPLGGQKFFFSLAAVNPNFTVQDNEDNTARILTRKNGFNRHEISTYLLPVVISDNDYPIQSSTGTLTIRVCACDSQGNMQSCSAEALLLPAGLSTGALIAILLCIIILLVIVVLFAALKRQRKKEPLILSKEDIRDNIVSYNDEGGGEEDTQAFDIGTLRNPAAIEEKKLRRDIIPETLFIPRRTPTAPDNTDVRDFINERLKEHDLDPTAPPYDSLATYAYEGNDSVAESLSSLESGTTEGDQNYDYLREWGPRFNKLAEMYGGGESDKDA