wanglab/gogpt-training-data huggingface dataset:
Protein: von Willebrand factor A domain-containing protein 1 (von Willebrand factor A domain-related protein) (Q8R2Z5)
Organism: Mus musculus (Mouse)
Function: Promotes matrix assembly. Involved in the organization of skeletal muscles and in the formation of neuromuscular junctions (By similarity).
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:12062410, ECO:0000269|PubMed:16407285, ECO:0000269|PubMed:18757743}.
Interaction partners:
Sequence:
MLFWTAFSMALSLRLALARSSIERGSTASDPQGDLLFLLDSSASVSHYEFSRVREFVGQLVATMSFGPGALRASLVHVGSQPHTEFTFDQYSSGQAIQDAIRVAPQRMGDTNTGLALAYAKEQLFAEEAGARPGVPKVLVWVTDGGSSDPVGPPMQELKDLGVTIFIVSTGRGNLLELLAAASAPAEKHLHFVDVDDLPIIARELRGSITDAMQPQQLHASEVLSSGFRLSWPPLLTADSGYYVLELVPSGKLATTRRQQLPGNATSWTWTDLDPDTDYEVSLLPESNVHLLRPQHVRVRTLQEEAGPERIVISHARPRSLRVSWAPALGPDSALGYHVQLGPLQGGSLERVEVPAGQNSTTVQGLTPCTTYLVTVTAAFRSGRQRALSAKACTASGARTRAPQSMRPEAGPREP
Protein: Solute carrier family 41 member (D6RC02)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU369007}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU369007}.
Interaction partners:
Sequence:
MDGTETRQRRLDSCGKPGELGLPHPLSTGGLPVASEDGALRAPESQSVTPKPLETEPSRETTWSIGLQVTVPFMFAGLGLSWAGMLLDYFQANTGQIDDPQEQHRVISSNLALIQVQATVVGLLAAVAALLLGVVSR
Protein: Transcription initiation factor IIB (EC 2.3.1.48) (General transcription factor TFIIB) (B1APE2)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MASTSRLDALPRVTCPNHPDAILVEDYRAGDMICPECDRVIDVGSEWRTFSNDKATKDPSRVGDSQNPLLSDGDLSTMIGKGTGAASFDEFGNSKYQNRRTMSSSDRAMMNAFKEITTMADRINLPRNIVDRTNNLFKQVYEQKSLKGRANDAIASACLYIACRQEGVPRTFKEICAVSRISKKEIGRCFKLILKALETSVDLITTGDFMSRFCSNLCLPKQVQMAATHIA
Protein: Inositol polyphosphate multikinase (IPMK) (EC 2.7.1.127) (EC 2.7.1.151) (Arginine metabolism regulation protein III) (GLE1 synthetic lethal protein 3) (Inositol polyphosphate kinase 2) (P07250)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Inositol phosphate kinase with both monophosphoinositol and diphosphoinositol polyphosphate synthase activities. Able to phosphorylate inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) on both the carbon-3 and carbon-6 positions to synthesize inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) and inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), and then to subsequently phosphorylate and convert either isomer of InsP4 to inositol 1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5). Its predominant in vivo catalytic function is to convert Ins(1,4,5)P3 to Ins(1,4,5,6)P4 to Ins(1,3,4,5,6)P5 via 6- and 3-kinase activities. It can also use Ins(1,3,4,5,6)P5 as a substrate and act as a diphosphoinositol polyphosphate synthase to generate two different isomers of PP-InsP4. Has also a role in transcription regulation. Forms a complex with ARG80, ARG81 and MCM1 (ArgR-MCM1), which coordinates the expression of arginine anabolic and catabolic genes in response to arginine. Recruits ARG80 and MCM21 to stabilize them. Neither the kinase activity nor inositol phosphates are required for the formation of ArgR-MCM1 transcriptional complexes on DNA promoter elements and the control of arginine metabolism. In contrast, only the catalytic activity is required for PHO gene repression by phosphate and for NCR gene activation in response to nitrogen availability, indicating a role for inositol pyrophosphates in these controls. Inositol polyphosphates may be involved in the regulation of chromatin remodeling of transcription. Regulates nuclear mRNA export via inositol phosphate metabolism. Also has lipid kinase activity, transforming the lipid inositol phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) into phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) in the nucleus. Its kinase activity is necessary for the propagation of most [PSI+] prion variants.
Subcellular location: Nucleus {ECO:0000269|PubMed:10632874, ECO:0000269|PubMed:16123124, ECO:0000269|PubMed:3311884}.
Interaction partners:
- Arginine metabolism regulation protein I
- Pheromone receptor transcription factor
- Arginine metabolism regulation protein II
- Inositol-pentakisphosphate 2-kinase
- Inositol hexakisphosphate kinase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1
- Protein ARG5,6
- Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase
- Acetylornithine aminotransferase, mitochondrial
- Amino-acid acetyltransferase, mitochondrial
Sequence:
MDTVNNYRVLEHKAAGHDGTLTDGDGLLIFKPAFPQELEFYKAIQVRDVSRRKSSADGDAPLCSWMPTYLGVLNEGAKIEQSGDAALLKIDERLSDSTDNLDSIPVKSEKSKQYLVLENLLYGFSKPNILDIKLGKTLYDSKASLEKRERMKRVSETTTSGSLGFRICGMKIQKNPSVLNQLSLEYYEEEADSDYIFINKLYGRSRTDQNVSDAIELYFNNPHLSDARKHQLKKTFLKRLQLFYNTMLEEEVRMISSSLLFIYEGDPERWELLNDVDKLMRDDFIDDDDDDDDNDDDDDDDAEGSSEGPKDKKTTGSLSSMSLIDFAHSEITPGKGYDENVIEGVETLLDIFMKF
Protein: LD45860p (Proteasome regulator dREG) (Proteasome regulator gamma, isoform A) (Proteasome regulator gamma, isoform B) (Q9V3P3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-2
- Proteasome subunit beta type-1
- Proteasome subunit beta
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-4
- Proteasome subunit beta type-4
- Proteasome subunit beta
Sequence:
MPNDTVVKVQEYKDSLILKAELLITKGFPENIVRLNELLATPIFNERNFEEVHQDLNIPVLPPLLVKNELEDRDSLPTKRQRVDVIVSGQPVMGLPAGTVPCNKPLCEMIKVVKPIIRKLVEDSNLLKMWISFMIPKIEDGNNFGVSIQEDTLAEIQTVESEAAAFFDQISRYFLSRAKVVSKVAKYPHIDDYRRAVVELDEKEYLSLWLVVCEVRNRYSSLHDIVIKNLEKLKKPRSSNTESLY
Protein: Regenerating islet-derived protein 3-beta (REG-3-beta) (Pancreatitis-associated protein 1) (Regenerating islet-derived protein III-beta) (Reg III-beta) [Cleaved into: Regenerating islet-derived protein 3-beta 16.5 kDa form; Regenerating islet-derived protein 3-beta 15 kDa form] (P35230)
Organism: Mus musculus (Mouse)
Function: Bactericidal C-type lectin which acts against several intestinal Gram-positive and Gram-negative bacteria. Lacks antibacterial activity against S.typhimurium. May play a role in protection against infection with S.enteritidis by inhibiting its translocation from the gut lumen into intestinal tissues and further extraintestinal tissues.
Subcellular location: Secreted {ECO:0000305|PubMed:34099862}. Note=Found in the apical region of pancreatic acinar cells. {ECO:0000305|PubMed:34099862}.
Interaction partners:
- Regenerating islet-derived protein 3-alpha
- Regenerating islet-derived protein 3-gamma
- Interleukin-22
- Deleted in malignant brain tumors 1 protein
Sequence:
MLPPTACSVMSWMLLSCLMLLSQVQGEDSLKNIPSARISCPKGSQAYGSYCYALFQIPQTWFDAELACQKRPGGHLVSVLNSAEASFLSSMVKRTGNSYQYTWIGLHDPTLGAEPNGGGWEWSNNDVMNYFNWERNPSTALDRAFCGSLSRASGFLKWRDMTCEVKLPYVCKFTG
Protein: Agrin (B3GQ72)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGSADRKAVYWPVWSFALVFVLLIQRCHGGCSEKELEKREEEANVVLTGTVEEILNMDPVHNTYSCKVRVWRYLKGKTMVNGEVLLDGGNKVMIGGFGDPHICDNQVATGDTRIFFVNLAPEYMWPNHKNELMLNSSLMRITLRNLEEVEHCVEDKPVHFTPAPPPDGCRGKLCGFGAVCERDQADPSKGECVCKKIVCTSVVAPVCGSDSSTYSNECELEKAQCNTQRRIKVMRKGPCALKDPCSEVTCSFGSTCIQSSDGLSAKCMCPLSCENVPKHVVCGSDGLDYQSECELNMKACATQKNIRVHHQGRCDPCSDTLNSLSTACRVNPKTYQQITFAPAESCPPDEMPICASDGHTYESMCQMERTALKNNLELKKVSLGSCKEKGGCPNGCKFNAICLLDNGEFRCSCDPIQCDGTYKPLCGKNGKTYPNDCERKLQECRTQKDIPVKQQGPCDLNLESPCLKKTCEFGALCVVKNSEAVCECSDACPQDQDPVCGSDGHTYSSSCQMKAMGCALQKQIQMQHKGPCADESRTNCSFGAICDAQTGRCVCPKGCLETRQPVCGSDGTTYDNECKLNVQACTKQLDLKVVAHGECKTCGSTVCSWGSQCVNNKCECQQCTGQPVKPVCGSDGNTYNNDCELRLASCQKQRKIEVAKPGVCDEDCGSGGSGSGSETCEQERCRRYGGTWDDDMEDERCVCELNCQIVLHSPVCGSDGNTYSSDCELKKTRCEKQIDLSVQSQGPCPTIVSPPPELVASQHCSQTVYGCCEDNKTAALGVGLAGCPSMCQCNHYGSYGGTCDPSTGQCSCKPGVGGLKCDRCEPGFWNFRGIVTENMSGCTPCNCDGLGSVRDDCEQMSGLCSCKPGVKGMKCNVCPDGSKMGVNGCDKGPKAPKSCAELVCHFGSSCVEVNGQAHCECPSPDCDEKNKTKVCGSDGVTYADRCQLKTIACRQDKEIKVEHLGQCKESIELTAKPTPFPTTHRTTPPTAHVKVTKQRHGHRTTTPDSYVVEAMPPPRLDGARKFSSPFTTHRPTTPYKPLRTSSPPLDFDESGSGEPSGDDEMVSGMEESGEEPLGTTVATTTLPTAEERSSCDNTAFGCCPDGKMAAVNSEGTNCPSTMRFSGFLHLDKVEGQEVFYTPEMEDPKSELFGETARSIESAMNELFRKSDVQKDFQSVHVRNLSPSNSIIAHIEAHFDPDTRFNVGDIEGALLKQLKASKDTGIVVKKPEEENIHINNYGLSTVPFFTTTTTTVASVTTPTTTTTTMSPSSAYTTLRPITTRRPFTSHRTTTPALATTTAPHVPKTTVSLMNRLGPHAHSPCDSQPCRHGGTCEEDDNDFTCICPAGRGGAVCEKVIKYFIPSFGGKSYMAFQTMKAYHTVRIAMEFRASEMTGILLYDGQKSKKDFLSLTLIEGYVELRFNTGSGTASVISKVLVKPGRWHQLVVVRNRRNAMLSVDNEPSVEGQSPPGTDGLNLDTDLFIGGVLDDMSADVKERTSVSAGLVGCIRMLDVNNLVYNLQENGGSVLYGSAIGECGNNPCLPNPCKNGASCQVKEAEIFHCKCVNGFSGPTCADAHNPCDPNKCHPPSRCQVLPEGGYKCECPMGREGRHCEKVSDKGGAFIPYFTGDSFLELKGLHTYNQDLRQKFSMTIVLLANDSKGMIFYNGQKTDGKGDFISLSLNDGILEFRYDLGKGPAVIRSKEKIKLNEWNTVNLERASRKGEISINGKDPVRGEAPNQHTDLNLKESLFVGGAPDFRKVARAAAFKDGFKGAIQKITLMGIPILKADNALSSTDVSMYPNHPCSKDVCENGGRCNPQLNSYECACRHGFSGHHCQDTIFEKSAGDTEAIAFDGHTFIEYHNGVTKSEKALLVNKFELSIRTEATHGLILWSGKGVERSDYIALAIVDGRVQMTYDLGSKPVVLRSTVRVNTNHWIRIKASRALRDGSLQVGNEAAVTGSSPLAATQLDTDGALWLGGLEELSVARRLPKAYSTGFIGCVKDVIVDGVELHLVEDALNTPKISHCSAK
Protein: Protein CHLOROPLAST VESICULATION (Q8S8K8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Triggers stress-induced chloroplast degradation, independently of autophagy and senescence-associated vacuoles. After targeting to the chloroplast, triggers its destabilization and subsequent disassembly, inducing the formation of CV-containing vesicles (CCVs) carrying stromal proteins, envelope membrane proteins, and thylakoid membrane proteins which are released from the chloroplasts and mobilized to the vacuole for proteolysis.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:25538186}; Single-pass membrane protein {ECO:0000255}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:25538186}; Single-pass membrane protein {ECO:0000255}. Plastid, chloroplast envelope {ECO:0000269|PubMed:25538186}. Vacuole {ECO:0000269|PubMed:25538186}. Vesicle {ECO:0000269|PubMed:25538186}. Note=Present in vesicle-like spots observed in destabilized chloroplasts; these CV-containing vesicles (CCVs) carrying stromal proteins, envelope membrane proteins, and thylakoid membrane proteins translocate later to the cytosol before being mobilized to the vacuole for proteolysis. {ECO:0000269|PubMed:25538186}.
Interaction partners:
- Uncharacterized protein At5g39520
- At1g09500/F14J9_16
- von willebrand factor A domain protein
- Alanine--glyoxylate aminotransferase 2 homolog 3, mitochondrial
- Phospholipase A1 PLIP3, chloroplastic
- Mitochondrial arginine transporter BAC2
- DNA binding / transcription factor
- Cytochrome P450 76C2
- F18B13.24 protein
- Late embryogenesis abundant protein
Sequence:
MAGRISCCLNLPPLDSNSAQSLASLLKTTSKISCRRTENETEPRKNKCSFVLGVAATVVIGGIQINDVASVEAAVVKSPVEEMAAGVVPPRRWSDKRTCPPWLENSLETIVPENLPRPSAHRRLELAGLAKGDAPPVGVVMTRVNRGGCFSV
Protein: DNA-directed RNA polymerase subunit Rpo3 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit D) (P95989)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00320}.
Interaction partners:
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL16
- DNA-directed RNA polymerase subunit Rpo7
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein uL2
- DNA-directed RNA polymerase subunit Rpo6
- Small ribosomal subunit protein uS17
Sequence:
MSINLLHKDDTRIDLVFEGYPLEFVNAIRRASMLYVPIMAVDDVYFIENNSPLYDEILAHRLALIPFMSEEALDTYRWPEECIECTENCEKCYTKIYIEAEAPNEPRMIYSKDIKSEDPSVVPISGDIPIVLLGTNQKISLEARLRLGYGKEHAKFIPVSLSVVRYYPKVEILANCEKAVNVCPEGVFELKDGKLSVKNELSCTLCEECLRYCNGSIRISFVEDKYILEIESVGSLKPERILLEAGKSIIRKIEELEKKLVEVVK
Protein: Sulfite reductase [ferredoxin] (EC 1.8.7.1) (P72854)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors.
Interaction partners:
- Phosphoadenosine 5'-phosphosulfate reductase
- cysteine synthase
- Cysteine synthase
- Slr0876 protein
- Putative pyruvate-flavodoxin oxidoreductase
- Uroporphyrinogen-III C-methyltransferase
- uroporphyrinogen-III C-methyltransferase
- Probable adenylyl-sulfate kinase
- Thioredoxin
- Sulfate adenylyltransferase
Sequence:
MVTTPTAAPRKPSKVEGIKERSNYLREPLATELLNDANYFTDDAVQILKFHGSYQQDNRDNRVKGQEKDYQFMLRTRNPGGLIPAQLYTALDDLSKTHGNQTLRVTTRQGLQIHGIVKKDLKMAIATVVNNLGSTLGACGDINRNVMAPAAPFRDKPEYGYAWDYANKVADLLSPQSGAYYEIWLDGEKVISGEEAPEVKAARQKDLNGTNLNDPKEPIYGQQFMPRKFKISVTVPGDNSIDVYTHDISLVVITDRHGELRGFNVLAGGGLGRTHNKEETFARAADPIGYVSKDDVYDLVKAIVATQRDYGDRHNRRHARMKYLLADWGVEKFRKQVETYMGKPFQSFKPLPAWRYQDYLGWHEQGDGKLFFGLSVENGRIKDEGDFQLKTALRKVVDQFQLPLRLTANHNILLYDINAQDKAAIEQIFQQHGVVTDPEAIDTLVRYSMACPALPTCGLAVTESERIMPSVNARLRDLLNSLDLPNESIVTRMTGCPNGCARPYMAEIGFVGSAPNSYQVWLGGSPNQERLAAAYTEKMPLEQLESLFEPLFVYFKQSRKGKESFGDFCHRVGFTALREFSHGYTAPAKGGKNRKNQRRVSLSDEMYAQLKARSERDNCPMNQIVQQALTAYLGK
Protein: GDP-mannose:glycolipid 4-beta-D-mannosyltransferase (EC 2.4.1.251) (GlcA-beta-(1->2)-D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 4-beta-mannosyltransferase) (Q56775)
Organism: Xanthomonas campestris pv. campestris
Function: Nonprocessive beta-mannosyltransferase that catalyzes the transfer of a mannose residue from GDP-mannose to glucuronic acid-beta-1,2-mannose-alpha-1,3-glucose-beta-1,4-glucose-PP-polyisoprenyl to form the lipid-linked pentasaccharide repeating unit of xanthan, Man-GlcA-Man-Glc(2)-PP-Pol. Is involved in the biosynthesis of the exopolysaccharide xanthan. To a lesser extent, can also use ADP-Man and even GDP-Glc as sugar donor substrates in vitro. Is unable to transfer a Man residue to the free-tetrasaccharide GlcA-Man-Glc(2) used as an acceptor, which indicates that the diphosphate group and the lipid moiety in the acceptor substrate are of major importance for acceptor binding and catalysis.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:21367879}. Note=Monotopic integral membrane protein, mostly cytoplasmic.
Interaction partners:
Sequence:
MSASASLPVTRAAAAPRITVLFSTEKPNANTNPYLTQLYDALPDAVQPRFFSMREALLSRYDVLHLHWPEYLLRHPSKMGTLAKQACAALLLMKLQLTGTPVVRTLHNLAPHEDRGWRERALLRWIDQLTRRWIRINATTPVRPPFTDTILHGHYRDWFATMEQSTTLPGRLLHFGLIRPYKGVEVLLDVMRDVQDPRLSLRIVGNPATPXMRTLVETACAQDARISALLAYVEEPVLAREVSACELVVLPYKQMHNSGTLLLALSLARPVLAPWSESNAAIADEVGPGWVFLYEGEFDAALLSGMLDQVRAAPRGPAPDLSQRDWPRIGQLHYRTYLEALGKDGDAAL
Protein: Histone H3 (P08898)
Organism: Caenorhabditis elegans
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H4
- Lysine-specific demethylase 7 homolog
- SWI/SNF chromatin remodeling complex core catalytic subunit swsn-4
- Histone H2A
- JmjC domain-containing protein
- Nucleosome-remodeling factor subunit NURF301-like
- Histone H3.3 type 1
- Histone H3.3-like type 2
- Histone H2B 1
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPASGGVKKPHRYRPGTVALREIRRYQKSTELLIRRAPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: MOB kinase activator-like 1 homolog A (Mps one binder kinase activator-like 1 homolog A) (Q54XJ0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNIFGKKSQTFKPKKNIQEGSKQYHLKQYAEATLGSGNLKSAVSLPTGEDINEWLAVNTTDFFNQINMLYGTITEFCTGTDCPVMSAGPKYEYHWADGTTVKKAIKVSAPEYVDFLMTWVQSQLDDENIFPSKIGVPFPKNFQSIVKTIFKRLFRVYAHIYHSHFQKIVSLGEEAHLNTSLKHFIYFIQEFNLVDKKELGPLNELIESLMKNP
Protein: Conserved protein (O69699)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable coiled-coil structural protein
- 1,4-beta-xylanase
- Possible conserved membrane protein
Sequence:
MAVLPACRLGLVVCVATAVITATMVLATPSYACACGAAVTAHGSQATLNHEVALLHWDGTTETIVMQLAMNADTDNVALVVPTPTPAIVTTADQSTFGELDTLSAPLIEHQRHWSLRRGVGASGPQEAAARAPHVLNQVRLGPLEATTLTGGDLSGLQTWLSDNGYAIRPAVSAALDPYVRDGWAFVAIRLTSTDLIVGGLDPVRMTFRSSRLVYPMRLSVAAQEPQHVTIFTLSDHRQQRTDADAATQTTHVRFAGDMSTAVRDPLLRELIGNHGSYLTKVEVDIYQTSRISSDFTFGNAPNDDPYRQVVTVYDDVALPPLLLVVVSAIAVGAAGGAVVVVLRRRRRAHTG
Protein: LIM domain only protein 3 (A9ED84)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MLSVQPDTKPKGCAGCNRKIKDRYLLKALDKYWHEDCLKCACCDCRLGEVGSTLYTKANLILCRRDYLRLFGVTGNCAACSKLIPAFEMVMRAKDNVYHLDCFACQLCNQRFCVGDKFFLKNNMILCQTDYEEGLMKEGYAPQVR
Protein: ESTs C26093(C11622) (Q7F7Z2)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MAECQPLQLQEGKKLQELQPYDGCNPSVYRGPILLPRQANSAPPAVPPEMSSSSGSGRSATEARALKIHSEAERRRRERINAHLTTLRRMIPDTKQMDKATLLARVVDQVKDLKRKASEITQRTPLPPETNEVSIECFTGDAATAATTVAGNHKTLYIKASISCDDRPDLIAGITHAFHGLRLRTVRAEMTSLGGRVQHVFILCREEGIAGGVSLKSLKEAVRQALAKVASPELVYGSSHFQSKRQRILESHCSIMSI
Protein: Nodulin-26 (Q39882)
Organism: Glycine max (Soybean) (Glycine hispida)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MPIRNIAIGRPEEATHPDTLKAGLAEFISTLIFVFAGSGSGIAYNKLTDNGARTPAGLISASIAHAFALFVAVSVGPNISGGHVNPAVTFGAFVGATSPSRGIVYVIAQLLGSIVASLLLAFVTASPVPAFGLSAGVGVGNALVLEIVMTFGLVYTVYATAVDPKKGNLGIIAPIAIGFIVGANILLGGAFSGAAMNPAVTFGPAVVSWTWTNHWIYWAGPLIGGGIAGLIYEVVFISHTHEQRPSTDY
Protein: Disheveled-associated activator of morphogenesis 1 (Q9Y4D1)
Organism: Homo sapiens (Human)
Function: Binds to disheveled (Dvl) and Rho, and mediates Wnt-induced Dvl-Rho complex formation. May play a role as a scaffolding protein to recruit Rho-GDP and Rho-GEF, thereby enhancing Rho-GTP formation. Can direct nucleation and elongation of new actin filaments. Involved in building functional cilia. Involved in the organization of the subapical actin network in multiciliated epithelial cells (By similarity). Together with DAAM2, required for myocardial maturation and sarcomere assembly (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16630611}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:26644512}. Note=Perinuclear. Colocalizes with RHOA and KANK1 around centrosomes. {ECO:0000250|UniProtKB:Q8BPM0}.
Interaction partners:
- Segment polarity protein dishevelled homolog DVL-1
- Transforming protein RhoA
- Segment polarity protein dishevelled homolog DVL-2
- Segment polarity protein dishevelled homolog DVL-3
- Disheveled-associated activator of morphogenesis 2
- Serine/arginine repetitive matrix protein 4
- Rho-related GTP-binding protein RhoC
- Rho guanine nucleotide exchange factor 19
- Profilin-1
- Profilin-4
Sequence:
MAPRKRGGRGISFIFCCFRNNDHPEITYRLRNDSNFALQTMEPALPMPPVEELDVMFSELVDELDLTDKHREAMFALPAEKKWQIYCSKKKDQEENKGATSWPEFYIDQLNSMAARKSLLALEKEEEEERSKTIESLKTALRTKPMRFVTRFIDLDGLSCILNFLKTMDYETSESRIHTSLIGCIKALMNNSQGRAHVLAHSESINVIAQSLSTENIKTKVAVLEILGAVCLVPGGHKKVLQAMLHYQKYASERTRFQTLINDLDKSTGRYRDEVSLKTAIMSFINAVLSQGAGVESLDFRLHLRYEFLMLGIQPVIDKLREHENSTLDRHLDFFEMLRNEDELEFAKRFELVHIDTKSATQMFELTRKRLTHSEAYPHFMSILHHCLQMPYKRSGNTVQYWLLLDRIIQQIVIQNDKGQDPDSTPLENFNIKNVVRMLVNENEVKQWKEQAEKMRKEHNELQQKLEKKERECDAKTQEKEEMMQTLNKMKEKLEKETTEHKQVKQQVADLTAQLHELSRRAVCASIPGGPSPGAPGGPFPSSVPGSLLPPPPPPPLPGGMLPPPPPPLPPGGPPPPPGPPPLGAIMPPPGAPMGLALKKKSIPQPTNALKSFNWSKLPENKLEGTVWTEIDDTKVFKILDLEDLERTFSAYQRQQDFFVNSNSKQKEADAIDDTLSSKLKVKELSVIDGRRAQNCNILLSRLKLSNDEIKRAILTMDEQEDLPKDMLEQLLKFVPEKSDIDLLEEHKHELDRMAKADRFLFEMSRINHYQQRLQSLYFKKKFAERVAEVKPKVEAIRSGSEEVFRSGALKQLLEVVLAFGNYMNKGQRGNAYGFKISSLNKIADTKSSIDKNITLLHYLITIVENKYPSVLNLNEELRDIPQAAKVNMTELDKEISTLRSGLKAVETELEYQKSQPPQPGDKFVSVVSQFITVASFSFSDVEDLLAEAKDLFTKAVKHFGEEAGKIQPDEFFGIFDQFLQAVSEAKQENENMRKKKEEEERRARMEAQLKEQRERERKMRKAKENSEESGEFDDLVSALRSGEVFDKDLSKLKRNRKRITNQMTDSSRERPITKLNF
Protein: EMAP like 2 (A0A0C4DGQ7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSSFGAGKTKEVIFSVEDGSVKMFLRGRPVPMMIPDELAPTYSLDTRSELPSCRLKLEWVYGYRGRDCRANLYLLPTGEIVYFVASVAVLYSVEEQRQRHYLGHNDDIKCLAIHPDMVTIATGQVAGTTKEGKPLPPHVRIWDSVSLSTLHVLGLGVFDRAVCCVGFSKSNGGNLLCAVDESNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPTDPTVLITCGKSHIYFWTLEGGSLSKRQGLFEKHEKPKYVLCVTFLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDYSKLQEVEVPEDFGPVRTVAEGHGDTLYVGTTRNSILQGSVHTGFSLLVQGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWSRIIEMAAAGHGDP
Protein: Adapter protein MecA (Q5M699)
Organism: Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
Function: Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis.
Interaction partners:
- ATP-dependent Clp protease, ATP-binding subunit
- Exopolysaccharide biosynthesis protein, glycosyltransferase
- Septation ring formation regulator EzrA
- Competence protein, transcription factor
- ABC transporter membrane-spanning protein
- DNA methylase adenine-specific domain-containing protein
- ATP-dependent Clp protease
- Tetratricopeptide repeat protein
Sequence:
MEMKQINETTLKIMITMEDLEEHGMELKDFLIPQEKTEEFFYTVMDELDLPDNFKNSGMLSFRVTPRKDRVDVFVTKSDLKEALDFNDLSDMEDYSGLSPEEFLKALEDNFMDKGDIEAHHKLEEHDKTLKEVDETMTEPAKEVAEETIREDYTHYVLAFSDFDQVVTFAQGLKNVSVEGSEFYKLGDVYYMTILLYLADEPDYYANNMYARFLEYANVADRTRPYLQEHATILMEEDALPVLQATKWS
Protein: Transducin beta-like protein 3 (Zgc:101778) (Q5U3Q5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MAGKTLLFKSNYAVSSRIEPFYKGGRVQVSADEQHIFCTYGPKINILQISTGKIIHSIEQEDQEDITAFALSPDDEMLVSASRALLLRQWDWKQQQCRRSWRAVHSVPVASMSFDCTSTLLATGGCDGTIKLWDVIKQYCTHNLKGSSGVVHLVEFHPDISRLQLFSSSSDCAIRIWDLRSSRCVCVLESHYSPVTALAFSPDGHTLVSSGRDKICSVWDLQEQKVKRTIPVYEAVEGVVLLSGSADYSEMGVKSDALHLVTAGSKGVLRVWDSSSSRCVFTQTLPDASSHTEDEDAEDEERLGLLQLLLLPRTGRLITVTAEHNILLYQTPTLAVQQQFVGYNDDVLDVKFVGKDDTHIAVATNSSQLKVFELSTNSCQILHGHTDTILSIDVFRKGSMFATCAKDKSVRVWRMDVSSGRVHCVAQGTGHSNAVGSIACSRMKQQFVVSGSQDCTVKVWDLPETTGAEGVMMMKARSTERAHEKDVNSVCVSPNDKLLASGSQDRTAKLWALSDLRLLGVCRGHRRGVWSVQFSPVDQILGSASADGSVRIWSIQDFSCLKTFEGHDASVLKIIFVSRGTQLVSSGSDGLVKLWTIKTNECVRTLDAHQDKVWALHGGCRDELMVTGSADSTITVWKDVTEVELAEEQAKQEDQVLKQQELQNLLHEHQYVKALGVAISLDQPHTAPRVIREIRQREDGVQELEKTLLKLRKDQKESVLRYCTVWNTNSRSCLDAQAVLKVLLTHLSPEEMLQFQSAHTHLQALVPYTERHMQRINRLLQASMFLDYMWQKMRITGAMDSVNMQEDEDDDGVQSVFITDKQPMQTTEEEEENEEMQCSGDSEQRLHEDEAVCTSKTAAGKLPNTVDQLLDSDEDKEEEEFSCKPAASVLQEIVSVS