wanglab/gogpt-training-data huggingface dataset:
Protein: Mucin related 2B, isoform B (M9MS86)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTHCLWSTLLGLLSVLSTATSRSVRQLPSAYPPVLPTGYYGQPPYAYPPYGYGYQAPPPVYQPYYDNVFGVFKSYPGGGFPVRFDYNNRCSRNYIGIKPHPDQQQYYYVCKPDCVIFSKCRGLESFNASSGRCVQHVPQHRPDHRPPQCQKEGRFPHPHDCKVYYRCDKNRTQPWLFACPAGTIFSPVERKCLPGDQCPSTEISDSGSYIPQNCELKFPECAEEGTFRSPTDCALYYTCRLQESGTYLQTRFKCPGSNSFDLERKLCRPRSEVDCFDFVPGPVQVPYAPQPYYPPYPAAPPLYEEDDYDTGAREQQPALKSEKLQVAAEGFEKPSLNVVVLQTTTLEPSTAYHKYPAYPSYPSYEYSSHHRGKERAAENLELEKEGVPRKLKLSENIVIQPETPATAATTREPLNDINKYQYKRYTYGTDKNDVTEAPEIKSPLKGLHLSENIVILPETTTTTTTTTKPVVLTCPTISPPDTTPKPSTTTAVTKSTPKISSTEQHSTTTAKTTTTKRPTTVTEKTSSATEKPRTTVVTTTTQKRSTTTHNTSPDTKTTIRSTTLSPKTTTTPSTTTPSTTTPSTTTPSTTTPSTTTPSTTTPSTTTTVKVSTHRPRTTSQKTTTASTTTKKTTTSPKTTKTTDIPTSTTSKLSTTTQKTTTTTHKFTAATTSTEKPKTTTEKTSTVSTTTKKSTESSPKPTSSTGKPTTTPKPSTRTTPTTTKVTTTTQITTTTPLRSSTETTSTQPPTTTTPQPTTTTTLTVTPKTSTTTTTTEKPITSSPKPTTTTQKTTSTAPNTTKVAITTQKETTPTQSTSTTIFTRKTTTNNPEPTSTEKPITSTTPKPSTTTPKTSTVASSTEKTTISSPKPTTEKSTENPTTNSVKTSALTSSTQRATSTTSEPTKTTQNITTTTPKPTTLKTSTQEATTSTQKVSTVTITTKKATESSPLTTLSTEEPNTTPKPLRTTTPTTTSVTATTRITTTTISESSTETTSTQKPKSTTPTSTTRTTPKVTTVIVSTQNPTTTTSKTSTVTITTPNPSPSTQRPTTTTRQPTSITASTTSIGTTRIPTTTNPQNSTSSTDLTTVTRPPCPDPDSTSVSSPEDHSTEKVPQLIVKVYEPIDLKIVFCPKSCDQDHDHKFDGV
Protein: Serine hydrolase RBBP9 (EC 3.-.-.-) (B5T-overexpressed gene protein) (Protein BOG) (Retinoblastoma-binding protein 9) (RBBP-9) (O88350)
Organism: Rattus norvegicus (Rat)
Function: Serine hydrolase whose substrates have not been identified yet (By similarity). May negatively regulate basal or autocrine TGF-beta signaling by suppressing SMAD2-SMAD3 phosphorylation (By similarity). May play a role in the transformation process due to its capacity to confer resistance to the growth-inhibitory effects of TGF-beta through interaction with RB1 and the subsequent displacement of E2F1.
Interaction partners:
- Cysteine-rich protein 2-binding protein
- Apoptosis inducing factor BLCAP
Sequence:
MASPTKAVIVPGNGGGDVATHGWYGWVRKGLEQIPGFQCLAKNMPDPITARESIWLPFMETELHCDEKTIIIGHSSGAIAAMRYAETHQVYALILVSAYTSDLGDENERASGYFSRPWQWEKIKANCPHIIQFGSTDDPFLPWKEQQEVADRLDAKLYKFTDRGHFQNTEFHELIRVVKSMLTPAL
Protein: DNA repair protein rad9 (P26306)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts in DNA repair and mutagenesis. Involved in promoting resistance to ionizing radiation and UV light, as well as regulating cell cycle progression after irradiation. Repressor of entry into mitosis that is activated by chromosome breaks.
Interaction partners:
- DNA damage checkpoint control protein rad1
- Checkpoint protein rad17
- Checkpoint protein hus1
- S-M checkpoint control protein rad4
- Replication factor C subunit 2
- Protein kinase rad3
- Replication factor C subunit 4
- DNA repair protein crb2
- Serine/threonine-protein kinase chk1
- Replication factor C subunit 3
Sequence:
MEFTVSNVNLRDLARIFTNLSRIDDAVNWEINKNQIEITCLNSSRSGFSMVTLKKAFFDKYIFQPDSVLLTGLMTPTIRIRTQVKPILSVFRNKIFDFIPTVVTTNSKNGYGSESASRKDVIVENVQISISTGSECRIIFKFLCKHGVIKTYKISYEQTQTLHAVFDKSLSHNNFQINSKILKDLTEHFGQRTEELTIQPLQERVLLTSFTEEVVHNRDILKQPTQTTVSIDGKEFERVALNEGVSVTLSLREFRAAVILAEALGSSICAYYGVPGKPILLTFAKGKNSEIEAQFILATVVGSDEQEVSSMMGNRWQHSSTPASLFNSVERNNSLTAVAHNPPGSIGWQTDQSDSSRMFNSALDRSDETNGIKEPSTTNDAGQSLFLDGIPNESELAAFNNDVNDDAEFGPTQAEQSYHGIFSQED
Protein: Cortexillin-2 (Cortexillin II) (Q550R2)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Actin-bundling protein. When linked to F-actin the actin filaments form preferentially anti-parallel bundles that associate into meshworks. Plays a major role in cytokinesis. Negatively regulates cortical localization of rapgap1 (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Ras GTPase-activating-like protein gapA
- Ras GTPase-activating-like protein rgaA
Sequence:
MDLNKEWEKVQEMAFTSWVNSVLEKRGCDKISDVSTDLSDGVKLIYFLESVSGKKFPKKFDLEPKTRIMRVQNLHLAMLFIDEDLKIKVQGVAAEEFVDNNKKMILGFLWTLYRKYRISVINEGDKSSEEGLLAWCKKTTEGYNNVNITGFKSSFRDGHGFLALAHKYDPTVFKYDEYEGHDNIARLNAAFDFAEKGLGIPKLLEAESLSKGNVDERSIVLYTSLFFHAFRAKEEREALEASQNSLNNKLASLEQSLEGEKHSQEELVKQKKDLEDALNKIREQNDNRNSRITDLQSKIDDALRGLDDEKLAKLDLESRLAKCEKDKAILELKLAEILDEKDRLEKKIDEDKKRAEAERLGLGLIRQHLAAQFSDIHKWQSFLEHPETVPYTGTPVDLDSELSSLSFEEQAKKLASKLESENILIEKYLNGKEEAKAAAKK
Protein: Obg like ATPase 1 (C9JTK6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPPKKGGDGIKPPPIIGRFGTSLKIGIVGLPNVGKSTFFNVLTNSQASAENFPFCTIDPNESRVPVPDERFDFLCQYHKPASKIPAFLNVVDIAGLVKGAHNGQGLGNAFLSHISA
Protein: Choline O-acetyltransferase (CHOACTase) (ChAT) (Choline acetylase) (EC 2.3.1.6) (Q03059)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reversible synthesis of acetylcholine (ACh) from acetyl CoA and choline at cholinergic synapses.
Interaction partners:
- Vesicular acetylcholine transporter
- Glycerophosphocholine phosphodiesterase GPCPD1
- Acetylcholinesterase
- Choline/ethanolamine kinase
- Choline kinase alpha
- Phosphoethanolamine/phosphocholine phosphatase
- Tyrosine 3-monooxygenase
- Ribonuclease P protein subunit p14
- High affinity choline transporter 1
- Cholinesterase
Sequence:
MPILEKVPPKMPVQASSCEEVLDLPKLPVPPLQQTLATYLQCMQHLVPEEQFRKSQAIVKRFGAPGGLGETLQEKLLERQEKTANWVSEYWLNDMYLNNRLALPVNSSPAVIFARQHFQDTNDQLRFAASLISGVLSYKALLDSQSIPTDWAKGQLSGQPLCMKQYYRLFSSYRLPGHTQDTLVAQKSSIMPEPEHVIVACCNQFFVLDVVINFRRLSEGDLFTQLRKIVKMASNEDERLPPIGLLTSDGRSEWAKARTVLLKDSTNRDSLDMIERCICLVCLDGPGTGDLSDTHRALQLLHGGGCSLNGANRWYDKSLQFVVGRDGTCGVVCEHSPFDGIVLVQCTEHLLKHMMTGNKKLVRVDSVSELPAPRRLRWKCSPETQGHLASSAEKLQRIVKNLDFIVYKFDNYGKTFIKKQKCSPDGFIQVALQLAYYRLYQRLVPTYESASIRRFQEGRVDNIRSATPEALAFVQAMTDHKAAVLASEKLQLLQRAIQAQTEYTVMAITGMAIDNHLLALRELARDLCKEPPEMFMDETYLMSNRFILSTSQVPTTMEMFCCYGPVVPNGYGACYNPHAEAITFCISSFHGCKETSSVEFAEAVGASLVDMRDLCSSRQPADSKPPTAKERARGPSQAKQS
Protein: Palmitoyltransferase (EC 2.3.1.225) (Q9W251)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Uncharacterized protein, isoform A
Sequence:
MRIRSNPMPSRMVDILCFLIIAVFLPVVFMFEIVVVLPAFHEPGGFFHTFTFLMAMFLVFNIKGNMIACMMIDTSVNVKKVEPPSDQLNWRECGECQKLAPPRSWHCKACKVCILKRDHHCIYTGCCIGLRNHRFFMGFIFYLFVGSVYALVYNSIYMWVIHGHIYSNWVTVLKLACPMLHLVTGSFWTNMYLVFYSLNILALAYGVLLLAYHVPIVLRGGVSADRTKESKEKYDRGVYQNLRSVFGNRMHLAWLSPLIRSDLPEDGYHWNVPTNKQD
Protein: Large ribosomal subunit protein bL27 (50S ribosomal protein L27) (P9WHB3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein bL9
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein bL21
- Uncharacterized protein Rv0500B
- Large ribosomal subunit protein bL33B
Sequence:
MAHKKGASSSRNGRDSAAQRLGVKRYGGQVVKAGEILVRQRGTKFHPGVNVGRGGDDTLFAKTAGAVEFGIKRGRKTVSIVGSTTA
Protein: Kanadaptin (O54716)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRFGGSTRLFILQGPEEDREAESELTVTQLKELRKQQQILLEKKMLGEDSDEEEEANTTEGKSSRSGQDDELGCTWGMGEDAVEDEAEENPIALDFQQDREAFYIKDPKKALQGFFDREGEELEYEFDEQGHSTWLCRVRLPVDDSTGKQLVAEAIHSGKKKEAMVQCSLEACRVLDTLGLLRQEAVSRKRKAKNWEDEDFYDSDDDTFLDRTGLVEKKRLNRMKKAGKLDEKPETFESLVAKLNDAERELAEISERLKASSKVLSEPSSQDSLDAFMSEMKSGSTLDGVSRKKLHLRTFELRKEQQRLKGLIKLVKPAEIPELKKTELQTTNAENKTKKLALPLFGAMKGGSKFKLKTGTVGKLPPKRPELPPALMQMKDEPEVEEEEEEEEEEEEKVKEEHEERVEDGGVRLLQEPELELEAAVEHPSAPSEPSCSKETKSHAAPANEYKQDRDEPKKKKSPGPGKFPPILSSKYREDDPDYCIWVPREGQSGDGRTHLNDKYGY
Protein: RNA polymerase II transcriptional coactivator KELP (O65155)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. Binds single-stranded DNA (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- RNA polymerase II transcriptional coactivator KIWI
- Peroxisomal membrane protein PEX14
- HEAT repeat-containing protein
- Phosphatidylinositol 3-and 4-kinase family protein
- Symplekin
Sequence:
MEKETKEKIEKTVIEILSESDMKEITEFKVRKLASEKLAIDLSEKSHKAFVRSVVEKFLDEERAREYENSQVNKEEEDGDKDCGKGNKEFDDDGDLIICRLSDKRRVTIQEFKGKSLVSIREYYKKDGKELPTSKGISLTDEQWSTFKKNMPAIENAVKKMESRV
Protein: Galectin (M0R163)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XEELPRRREQCHHYPKDPQLEVNFYTGMDEDSDIAFQFRLHFGHPAIMNSCVFGIWRYEEKCYYLPFEDGKPFELCIYVRHKEYKVMVNGQRIYNFAHRFPPASVKMLQVFRDISLTRVLISD
Protein: Adenylate cyclase type 3 (EC 4.6.1.1) (ATP pyrophosphate-lyase 3) (Adenylate cyclase type III) (AC-III) (Adenylate cyclase, olfactive type) (Adenylyl cyclase 3) (AC3) (Q8VHH7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Participates in signaling cascades triggered by odorant receptors via its function in cAMP biosynthesis. Required for the perception of odorants. Required for normal sperm motility and normal male fertility. Plays a role in regulating insulin levels and body fat accumulation in response to a high fat diet.
Subcellular location: Cell membrane {ECO:0000305|PubMed:11055432}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:11055432, ECO:0000269|PubMed:9768837}. Golgi apparatus {ECO:0000250|UniProtKB:P21932}. Cytoplasm {ECO:0000250|UniProtKB:O60266}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Calmodulin-1
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Calmodulin-4
Sequence:
MPRNQGFSDPEYSAEYSAEYSVSLPSDPDRGVGRTHEISVRNSGSCLCLPRFMRLTFVPESLENLYQTYFKRQRHETLLVLVVFAALFDCYVVVMCAVVFSSDKLAPLMVAGFGLVLDIILFVLCKKGLLPDRVSRKVVPYLLWLLISAQIFSYLGLNFSRAHAASDTVGWQAFFVFSFFITLPLSLSPIVIISVVSCVVHTLVLGVTVAQQQQDELEGMQLLREILANVFLYLCAIIVGIMSYYMADRKHRKAFLEARQSLEVKMNLEEQSQQQENLMLSILPKHVADEMLKDMKKDESQKDQQQFNTMYMYRHENVSILFADIVGFTQLSSACSAQELVKLLNELFARFDKLAAKYHQLRIKILGDCYYCICGLPDYREDHAVCSILMGLAMVEAISYVREKTKTGVDMRVGVHTGTVLGGVLGQKRWQYDVWSTDVTVANKMEAGGIPGRVHISQSTMDCLKGEFDVEPGDGGSRCDYLDEKGIETYLIIASKPEVKKTAQNGLNGSAVPNGAPASSKPSSPALIETKEPNGSAHASGSTSEEAEEQEAQADNPSFPNPRRRLRLQDLADRVVDASEDEHELNQLLNEALLERESAQVVKKRNTFLLTMRFMDPEMETRYSVEKEKQSGAAFSCSCVVLFCTAMVEILIDPWLMTNYVTFVVGEVLLLILTICSMAAIFPRSFPKKLVAFSSWIDRTRWARNTWAMLAIFILVMANVVDMLSCLQYYMGPYNMTAGMELDGGCMENPKYYNYVAVLSLIATIMLVQVSHMVKLTLMLLVTGAVTALNLYAWCPVFDEYDHKRFQEKDSPMVALEKMQVLATPGLNGTDSRLPLVPSKYSMTVMMFVMMLSFYYFSRHVEKLARTLFLWKIEVHDQKERVYEMRRWNEALVTNMLPEHVARHFLGSKKRDEELYSQSYDEIGVMFASLPNFADFYTEESINNGGIECLRFLNEIISDFDSLLDNPKFRVITKIKTIGSTYMAASGVTPDVNTNGFTSSSKEEKSDKERWQHLADLADFALAMKDTLTNINNQSFNNFMLRIGMNKGGVLAGVIGARKPHYDIWGNTVNVASRMESTGVMGNIQVVEETQVILREYGFRFVRRGPIFVKGKGELLTFFLKGRDRPAAFPNGSSVTLPHQVVDNP
Protein: Deoxyhypusine synthase (EC 2.5.1.46) (Q9FI94)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. Also able to produce homospermidine from putrescine (By similarity).
Interaction partners:
- Eukaryotic translation initiation factor 5A-1
- Eukaryotic translation initiation factor 5A-2
- Deoxyhypusine hydroxylase
- Eukaryotic translation initiation factor 5A-3
- Elongation factor P
- Elongation factor P
- ARM repeat superfamily protein
- Deoxyhypusine protein
- At5g44730
- Nascent polypeptide-associated complex subunit beta
Sequence:
MEDDRVFSSVHSTVFKESESLEGKCDKIEGYDFNQGVDYPKLMRSMLTTGFQASNLGEAIDVVNQMLDWRLADETTVAEDCSEEEKNPSFRESVKCKIFLGFTSNLVSSGVRDTIRYLVQHHMVDVIVTTTGGVEEDLIKCLAPTFKGDFSLPGAYLRSKGLNRIGNLLVPNDNYCKFEDWIIPIFDEMLKEQKEENVLWTPSKLLARLGKEINNESSYLYWAYKMNIPVFCPGLTDGSLGDMLYFHSFRTSGLIIDVVQDIRAMNGEAVHANPKKTGMIILGGGLPKHHICNANMMRNGADYAVFINTGQEFDGSDSGARPDEAVSWGKIRGSAKTVKVYCDATIAFPLLVAETFATKRDQTCESKT
Protein: Phosphoribosylformylglycinamidine synthase subunit PurL (FGAM synthase) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase subunit II) (FGAR amidotransferase II) (FGAR-AT II) (Glutamine amidotransferase PurL) (Phosphoribosylformylglycinamidine synthase subunit II) (P9WHL7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}.
Interaction partners:
- Phosphoribosylformylglycinamidine synthase subunit PurQ
- Phosphoribosylformylglycinamidine synthase subunit PurS
- Phosphoribosylformylglycinamidine cyclo-ligase
- Phosphoribosylglycinamide formyltransferase
- Amidophosphoribosyltransferase
- Phosphoribosylglycinamide formyltransferase 2
- Phosphoribosylamine--glycine ligase
- N5-carboxyaminoimidazole ribonucleotide synthase
- N5-carboxyaminoimidazole ribonucleotide mutase
- Bifunctional purine biosynthesis protein PurH
Sequence:
MSPLARTPRKTSVLDTVEHAATTPDQPQPYGELGLKDDEYRRIRQILGRRPTDTELAMYSVMWSEHCSYKSSKVHLRYFGETTSDEMRAAMLAGIGENAGVVDIGDGWAVTFKVESHNHPSYVEPYQGAATGVGGIVRDIMAMGARPVAVMDQLRFGAADAPDTRRVLDGVVRGIGGYGNSLGLPNIGGETVFDPCYAGNPLVNALCVGVLRQEDLHLAFASGAGNKIILFGARTGLDGIGGVSVLASDTFDAEGSRKKLPSVQVGDPFMEKVLIECCLELYAGGLVIGIQDLGGAGLSCATSELASAGDGGMTIQLDSVPLRAKEMTPAEVLCSESQERMCAVVSPKNVDAFLAVCRKWEVLATVIGEVTDGDRLQITWHGETVVDVPPRTVAHEGPVYQRPVARPDTQDALNADRSAKLSRPVTGDELRATLLALLGSPHLCSRAFITEQYDRYVRGNTVLAEHADGGMLRIDESTGRGIAVSTDASGRYTLLDPYAGAQLALAEAYRNVAVTGATPVAVTNCLNFGSPEDPGVMWQFTQAVRGLADGCADLGIPVTGGNVSFYNQTGSAAILPTPVVGVLGVIDDVRRRIPTGLGAEPGETLMLLGDTRDEFDGSVWAQVTADHLGGLPPVVDLAREKLLAAVLSSASRDGLVSAAHDLSEGGLAQAIVESALAGETGCRIVLPEGADPFVLLFSESAGRVLVAVPRTEESRFRGMCEARGLPAVRIGVVDQGSDAVEVQGLFAVSLAELRATSEAVLPRYFG
Protein: Conidiophore development regulator abaA (P20945)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: BrlA, abaA and wetA are pivotal regulators of conidiophore development and conidium maturation. They act individually and together to regulate their own expression and that of numerous other sporulation-specific gene. Controls temporal and spatial specificity in Aspergillus development. Directs the differentiation of phialides and is continuously required for maintenance of their function. Expression of abaA leads to activation of brlA and wetA, cessation of vegetative growth, and accentuated cellular vacuolization. Binds to the sequence 5'-CATTCY-3', where Y is a pyrimidine, making both major- and minor-groove contacts. Multiple abaA binding sites are present in the cis-acting regulatory regions of several developmentally controlled structural genes as well as those of the upstream regulatory gene brlA, the downstream regulatory gene wetA, and abaA itself.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:I1S4T3}. Note=localizes to the nuclei of phialides and terminal cells of mature conidia (By similarity). {ECO:0000250|UniProtKB:I1S4T3}.
Interaction partners:
- C2H2 type master regulator of conidiophore development brlA
- Transcription factor steA
- Developmental regulatory protein wetA
- Spore development regulator vosA
- Cell pattern formation-associated protein stuA
- Protein fluG
- Protein-methionine methyltransferase laeA
- C2H2-type domain-containing protein
- Velvet complex subunit B
- MYB family conidiophore development protein FlbD
Sequence:
MATDWQPECMVSQNQAALESIGAHSDRALQNTSGNVQAYSDSLAHHDTTGRDDPLQHYTLKYPHPPVPVPSHPLPTATANLYHPQLLSHRYQVKKLRRLQSNGSSYAGSRRGRSYLKSQKYLEYRARPRRDTGKDGEPVWSDELEDAFQQALEANPPMGRRKWSERGKSYGRNELIAEYIYKLTGKRRTRKQVSSHLQVLDSFLKGDPDWERLVREQSDRSTAQTQPVGPRWRTSMDHLPSSHYGTHATSSYPEPMRLMPPYSADLQLPQYSPTSTQQDTNNNTIQGLSFDMWVSAPNKPDRIDDAYHLYTRLQGDQRQPPMPLEDLKNWRVSFPHLSSSLSDVNDPLNCEIILLETNLELMDDFPPMGSRLGIHLELDIANPMSGTAPTVNQMENWTCSTYIYEDGRRTMEAYHNLTKPHTTKVKPPFESSWWAKTFTKLTQDKREAESTGHHHAADERTRRYFHSLTAVQEIRATVPPSLRRLQNHYPGSPAEESKRMAIILWKFRQTRPNEVGTTTWRKLITSPDRALTNSPRPSTAIDLPPLSLDSILLSKPTSNLYQAPPQHHDLLHQNAPSQQSWSLYQPSHDHVNSLYHSAGAFDFLNSITKPEEGLSDKTAPTSVLDPFPNLTQQTTSQTAGINVSSGTPVMLQIPDLSLSSNLGTYGLGHESHYVPSHHNAANLHDHSSTTGLGHYFAPSTQSLDEISHSHAPWSAPNTTISGDTSGGNYHHLPFTTSDHSVTVSRESHQNHSFEGLLPSDDLVGIVGGLSGDPNMNGAGPEHTSSAYAEHTAVEAV
Protein: Cyclin-D3-1 (Cyclin-delta-3) (Cyclin-d3) (G1/S-specific cyclin-D3-1) (CycD3;1) (P42753)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the control of the cell cycle at the G1/S (start) transition. Activates the G1/S phase transition in response to cytokinin hormone signal, but declines in response to sucrose starvation leading to G1 arrest. Involved in the induction of mitotic cell division. Plays an important role in the switch from cell proliferation to the final stages of differentiation during plant development. May not be involved in the activation of cell cycle in the root apical meristem (RAM) in the early phase of seed germination. Promotes divisions in the guard cells (GCs) after the guard mother cells (GMC) symmetric division.
Interaction partners:
- Cyclin-dependent kinase A-1
- Retinoblastoma-related protein 1
- Cyclin-dependent kinase B1-1
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase B2-2
- Transcription factor E2FA
- Cyclin-dependent kinase B1-2
- Cyclin-D3-3
- Cyclin-D3-2
Sequence:
MAIRKEEESREEQSNSFLLDALYCEEEKWDDEGEEVEENSSLSSSSSPFVVLQQDLFWEDEDLVTLFSKEEEQGLSCLDDVYLSTDRKEAVGWILRVNAHYGFSTLAAVLAITYLDKFICSYSLQRDKPWMLQLVSVACLSLAAKVEETQVPLLLDFQVEETKYVFEAKTIQRMELLILSTLEWKMHLITPISFVDHIIRRLGLKNNAHWDFLNKCHRLLLSVISDSRFVGYLPSVVAAATMMRIIEQVDPFDPLSYQTNLLGVLNLTKEKVKTCYDLILQLPVDRIGLQIQIQSSKKRKSHDSSSSLNSPSCVIDANPFNSDESSNDSWSASSCNPPTSSSSPQQQPPLKKMRGAEENEKKKPILHLPWAIVATP
Protein: Differentially expressed in FDCP 8 homolog (DEF-8) (Q6ZN54)
Organism: Homo sapiens (Human)
Function: Positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. Involved in bone resorption.
Interaction partners:
Sequence:
MAILSLRAPGPWQAMQVWADRTLLTPHTGVTSQVLGVAAAVMTPLPGGHAAGRTREARWDAMEYDEKLARFRQAHLNPFNKQSGPRQHEQGPGEEVPDVTPEEALPELPPGEPEFRCPERVMDLGLSEDHFSRPVGLFLASDVQQLRQAIEECKQVILELPEQSEKQKDAVVRLIHLRLKLQELKDPNEDEPNIRVLLEHRFYKEKSKSVKQTCDKCNTIIWGLIQTWYTCTGCYYRCHSKCLNLISKPCVSSKVSHQAEYELNICPETGLDSQDYRCAECRAPISLRGVPSEARQCDYTGQYYCSHCHWNDLAVIPARVVHNWDFEPRKVSRCSMRYLALMVSRPVLRLREINPLLFSYVEELVEIRKLRQDILLMKPYFITCREAMEARLLLQLQDRQHFVENDEMYSVQDLLDVHAGRLGCSLTEIHTLFAKHIKLDCERCQAKGFVCELCREGDVLFPFDSHTSVCADCSAVFHRDCYYDNSTTCPKCARLSLRKQSLFQEPGPDVEA
Protein: Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B (Q6PGU9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAGAGGGGNDVQWCFSQVKGAIDDDVAEADIISTVEFNHSGELLATGDKGGRVVIFQQETENKSQPQCRSEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQKNAAQFLLSTNDKTIKLWKISERDKRPEGYNLKEEDGRYRDASTITTLRVPVFRPMDLMVEASPRRVFANAHTYHINSISVNSDNETYLSADDLRINLWHLEITDRSFNIVDIKPANMEDLTEVITAAEFHPHQCNTFVYSSSKGTIRLCDMRASALCDKHSKLFEEPEDPSNRSFFSEIISSISDVKFSHNGRYMMTRVYLPVKIWDLNMENRPVETYQVHEYLRSKLCSLYENDCIFDKFECCWNGNDSVVMTGSYNNFFRMLDRTQRRDVTLEASRESCKPRQVLKPRRVCAGGKRKKDEISVDSLDFNKKILHTAWHPQENIIAVATTNNLYIFQEKVN
Protein: Homeobox-leucine zipper family protein / lipid-binding START domain-containing protein (B3H4G8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MAMSCKDGKLGCLDNGKYVRYTPEQVEALERLYHDCPKPSSIRRQQLIRECPILSNIEPKQIKVWFQNRRCREKQRKEASRLQAVNRKLTAMNKLLMEENDRLQKQVSQLVHENSYFRQHTPNPSLPAKDTSCESVVTSGQHQLASQNPQRDASPAGLLSIAEETLAEFLSKATGTAVEWVQMPGMKPGPDSIGIIAISHGCTGVAARACGLVGLEPTRVAEIVKDRPSWFRECRAVEVMNVLPTANGGTVELLYMQLYAPTTLAPPRDFWLLRYTSVLEDGSLVVCERSLKSTQNGPSMPLVQNFVRAEMLSSGYLIRPCDGGGSIIHIVDHMDLEACSVPEVLRPLYESPKVLAQKTTMAALRQLKQIAQEVTQTNSSVNGWGRRPAALRALSQRLSRGFNEAVNGFTDEGWSVIGDSMDDVTITVNSSPDKLMGLNLTFANGFAPVSNVVLCAKASMLLQNVPPAILLRFLREHRSEWADNNIDAYLAAAVKVGPCSARVGGFGGQVILPLAHTIEHEEFMEVIKLEGLGHSPEDAIVPRDIFLLQLCSGMDENAVGTCAELIFAPIDASFADDAPLLPSGFRIIPLDSAKQEVSSPNRTLDLASALEIGSAGTKASTDQSGNSTCARSVMTIAFEFGIESHMQEHVASMARQYVRGIISSVQRVALALSPSHISSQVGLRTPLGTPEAQTLARWICQSYRGYMGVELLKSNSDGNESILKNLWHHTDAIICCSMKALPVFTFANQAGLDMLETTLVALQDISLEKIFDDNGRKTLCSEFPQIMQQGFACLQGGICLSSMGRPVSYERAVAWKVLNEEENAHCICFVFINWSFV
Protein: 2-heptyl-4(1H)-quinolone synthase subunit PqsC (EC 2.3.1.230) (Q9I4X1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Required for the biosynthesis of the quorum-sensing signaling molecules 2-heptyl-4(1H)-quinolone (HHQ) and 2-heptyl-3-hydroxy-4(1H)-quinolone (Pseudomonas quinolone signal or PQS), which are important for biofilm formation and virulence. The PqsC/PqsB complex catalyzes the condensation of 2-aminobenzoylacetate (2-ABA) and octanoyl-CoA to form HHQ. First, PqsC acquires an octanoyl group from octanoyl-CoA and forms an octanoyl-PqsC intermediate. Then, together with PqsB, it catalyzes the coupling of 2-ABA with the octanoate group, leading to decarboxylation and dehydration, and resulting in closure of the quinoline ring.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24239007}.
Interaction partners:
- 2-heptyl-4
- 2-aminobenzoylacetyl-CoA thioesterase
- Anthranilate--CoA ligase
- Anthraniloyl-CoA anthraniloyltransferase
- 2-heptyl-3-hydroxy-4
- Anthranilate synthase component 2, pyocyanine specific
- Anthranilate synthase component 1, pyocyanine specific
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Malonyl CoA-acyl carrier protein transacylase
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
Sequence:
MHKVKLAAITCELPARSYENDDPVFAAVPDLSESWWQFWGVNRRGYFDPRNGENEFSLVVRAAERLLRSSDTAPDSVDMLICSASSPIMTDAGDVLPDLRGRLYPRMANVLSKQLGLSRALPLDSQMECASFLLNLRLAASMIRQGKAEKVLVVCSEYISNLLDFTSRTSTLFADGCAVALLTRGDDDSCDLLASAEHSDATFYEVATGRWRLPENPTGEAKPRLYFSLFSDGQNKMASFVPTNVPIAMRRALEKAGLGSDDIDYFVFHQPAPFLVKAWAEGIGARPEQYQLTMGDTGVMISVSIPYTLMTGLREGKIRPGDRIVMAGAATGWGFAAQVWQLGEVLVC
Protein: Pinin (F1QT45)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell junction, desmosome {ECO:0000256|ARBA:ARBA00004568}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
- Histone deacetylase complex subunit SAP18
- RNA-binding protein with serine-rich domain 1
- PNN-interacting serine/arginine-rich protein.
- Apoptotic chromatin condensation inducer 1a.
- Eukaryotic initiation factor 4A-III
- Serine/arginine repetitive matrix 1.
- Protein mago nashi homolog
- Zinc finger CCHC domain-containing protein 17
- LUC7-like 3 pre-mRNA-splicing factor.
- Apoptotic chromatin condensation inducer 1b
Sequence:
MAVAVRSLQDQLEKAKEGLKSVDENIRKLTGRDPGELRPGQNRRLTIPGPGGGRGRGINLLRRGLSDSGGGPPAKLRDIDGALLRLAGDQRARRDSRHDSDAEDDDDVKKPALQSSVVATSKERTRRDLIQDQTMDERGKQRNRRMFGLLMGTLQKFKQESTVSTERLKRRQEIEQKLEVQAEQERKKVECERRELFEERRAKQTELRLLEHKVELAQLQEDWNAHNSKLIKFIRTKTKPPIFYLPGRMCSATQKLLEESQKKLNGVFDERREAFAEQINKMEARPRRQSQRTGDKEMEGSRRAEETKKEDQEEGKAGAGRAGNRHVVEMEDEDEDVVEEEAEESSEVRERDEDQEQEQEQGEEKEEKNEESERKAEEDEEEEDEDPGAVEVKEDEEEQMEVTEVVGEVEAQGKLQVESPEATVEEVGNVRIEEEQEVESETQQEVTADSQQTPESQTETQPEESKEPQADAPSPNETQQDSKEEEAAVPESQQLQAEPEPEPEVPSQEPSQELSEEPQAAKTDTKEAGEEADDARGRAKVRAKKSKSRSSSSSSSSSSSSSSSSGSSSSSSGSSSSSSGSSSSSSSRSRSRGRDRENRDHKRRRRPSDRERRRSGSERAHKSSKSSGREGKGSKDKTSKPDRKRTSSEGRRSRSERDRKSDRKDRR