wanglab/gogpt-training-data huggingface dataset:
Protein: Nitric oxide synthase 3 (EC 1.14.13.39) (Constitutive NOS) (cNOS) (EC-NOS) (NOS type III) (NOSIII) (Nitric oxide synthase, endothelial) (Endothelial NOS) (eNOS) (P70313)
Organism: Mus musculus (Mouse)
Function: Produces nitric oxide (NO) which is implicated in vascular smooth muscle relaxation through a cGMP-mediated signal transduction pathway. NO mediates vascular endothelial growth factor (VEGF)-induced angiogenesis in coronary vessels and promotes blood clotting through the activation of platelets. May play a significant role in normal and abnormal limb development.
Subcellular location: Membrane, caveola {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Specifically associates with actin cytoskeleton in the G2 phase of the cell cycle, which is favored by interaction with NOSIP and results in a reduced enzymatic activity. {ECO:0000250}.
Interaction partners:
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Calmodulin-1
- Calmodulin 5
- Calmodulin-4
- RAC-alpha serine/threonine-protein kinase
- Caveolin-1
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Arginase-2, mitochondrial
Sequence:
MGNLKSVGQEPGPPCGLGLGLGLGLCGKQGPASPAPEPSQAPAPPSPTRPAPDHSPPLTRPPDGPRFPRVKNWEVGSITYDTLSAQAQQDGPCTSRRCLGSLVFPRKLQSRPTQGPSPTEQLLGQARDFINQYYNSIKRSGSQAHEQRLQEVEAEVAATGTYQLRESELVFGAKQAWRNAPRCVGRIQWGKLQVFDARDCRTAQEMFTYICNHIKYATNRGNLRSAITVFPQRCPGRGDFRIWNSQLIRYAGYRQQDGSVRGDPANVEITELCIQHGWTPGNGRFDVLPLLLQAPDEPPELFTLPPEMVLEVPLEHPTLEWFAALGLRWYALPAVSNMLLEIGGLEFPAAPFSGWYMSSEIGMRDLCDPHRYNILEDVAVCMDLDTRTTSSLWKDKAAVEINVAVLHSYQLAKVTIVDHHAATASFMKHLENEQKARGGCPADWAWIVPPISGSLTPVFHQEMVNYFLSPAFRYQPDPWKGSAAKGAGITRKKTFKEVANAVKISASLMGTVMAKRVKATILYGSETGRAQSYAQQLGRLFRKAFDPRVLCMDEYDVVSLEHEALVLVVTSTFGNGDPPENGESFAAALMEMSGPYNSSPRPEQHKSYKIRFNSVSCSDPLVSSWRRKRKESSNTDSAGALGTLRFCVFGLGSRAYPHFCAFARAVDTRLEELGGERLLQLGQGDELCGQEEAFRGWAQAAFQAACETFCVGEDAKAAARDIFSPKRSWKRQRYRLSTQAESLQLLPGLTHVHRRKMFQATILSVENLQSSKSTRATILVRLDTGGQEGLQYQPGDHIGVCPPNRPGLVEALLSRVEDPPPSTEPVAVEQLEKGSPGGPPPGWVRDPRLPPCTLRQALTYFLDITSPPSPRLLRLLSTLAEESSEQQELEALSQDPRRYEEWKWFSCPTLLEVLEQFPSVALPAPLILTQLPLLQPRYYSVSSAPSAHPGEIHLTIAVLAYRTQDGLGPLHYGVCSTWMSQLKAGDPVPCFIRGAPSFRLPPDPNLPCILVGPGTGIAPFRGFWQDRLHDIEIKGLQPAPMTLVFGCRCSQLDHLYRDEVLDAQQRGVFGQVLTAFSRDPGSPKTYVQDLLRTELAAEVHRVLCLEQGHMFVCGDVTMATSVLQTVQRILATEGGMELDEAGDVIGVLRDQQRYHEDIFGLTLRTQEVTSRIRTQSFSLQERQLRGAVPWSFDPPGPEIPGS
Protein: Ninjurin-2 (Nerve injury-induced protein 2) (Q9NZG7)
Organism: Homo sapiens (Human)
Function: Homophilic cell adhesion molecule that promotes axonal growth. May play a role in nerve regeneration and in the formation and function of other tissues.
Subcellular location: Cell membrane {ECO:0000269|PubMed:39667936, ECO:0000305|PubMed:10627596, ECO:0000305|PubMed:38614101}; Multi-pass membrane protein {ECO:0000269|PubMed:39667936}.
Interaction partners:
Sequence:
MESARENIDLQPGSSDPRSQPINLNHYATKKSVAESMLDVALFMSNAMRLKAVLEQGPSSHYYTTLVTLISLSLLLQVVIGVLLVVIARLNLNEVEKQWRLNQLNNAATILVFFTVVINVFITAFGAHKTGFLAARASRNPL
Protein: Caldesmon, smooth muscle (CDM) (P13505)
Organism: Meleagris gallopavo (Wild turkey)
Function: Control of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Inhibits the actin-activated ATPase of myosin this inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, 2 molecules of tropomyosin and with calmodulin.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, myofibril. Cytoplasm, cytoskeleton, stress fiber. Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle).
Interaction partners:
Sequence:
SNLKGAANAEAGSEKLKEKQQEAAVELDELKKRREERRKILEEEEQKKKQEEAERKIREEEEKKRMKEEIERRRAEAAEKRQKMPEDGVSEEKKPFKCFSPKGSSLKIEERAEFLNKSAQKSGMKPAHTTAVVSKIDSRLEQYTSAVVGNKAAKPAKPAASDLPVPAEGVRNIKSMWEKGNVFSSPGGTGTPNKETAGLKVGVSSRINEWLTKTPEGNKSPAPKPSDLRPGDVSGKRNLWEKQSVEKPAASSSKVTATGKKSETDGLRQFEKEP
Protein: Nucleoporin NUP100/NSP100 (Nuclear pore protein NUP100/NSP100) (Q02629)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP100 plays an important role in several nuclear export and import pathways including poly(A)+ RNA and protein transport.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Biased towards cytoplasmic side.
Interaction partners:
- Nucleoporin NUP42
- Nucleoporin NUP57
- mRNA export factor GLE2
- Nucleoporin NUP159
- Nucleoporin NUP1
- Nucleoporin NSP1
- Importin subunit beta-1
- Nucleoporin NUP2
- Nucleoporin NUP60
- mRNA export factor GLE1
Sequence:
MFGNNRPMFGGSNLSFGSNTSSFGGQQSQQPNSLFGNSNNNNNSTSNNAQSGFGGFTSAAGSNSNSLFGNNNTQNNGAFGQSMGATQNSPFGSLNSSNASNGNTFGGSSSMGSFGGNTNNAFNNNSNSTNSPFGFNKPNTGGTLFGSQNNNSAGTSSLFGGQSTSTTGTFGNTGSSFGTGLNGNGSNIFGAGNNSQSNTTGSLFGNQQSSAFGTNNQQGSLFGQQSQNTNNAFGNQNQLGGSSFGSKPVGSGSLFGQSNNTLGNTTNNRNGLFGQMNSSNQGSSNSGLFGQNSMNSSTQGVFGQNNNQMQINGNNNNSLFGKANTFSNSASGGLFGQNNQQQGSGLFGQNSQTSGSSGLFGQNNQKQPNTFTQSNTGIGLFGQNNNQQQQSTGLFGAKPAGTTGSLFGGNSSTQPNSLFGTTNVPTSNTQSQQGNSLFGATKLTNMPFGGNPTANQSGSGNSLFGTKPASTTGSLFGNNTASTTVPSTNGLFGNNANNSTSTTNTGLFGAKPDSQSKPALGGGLFGNSNSNSSTIGQNKPVFGGTTQNTGLFGATGTNSSAVGSTGKLFGQNNNTLNVGTQNVPPVNNTTQNALLGTTAVPSLQQAPVTNEQLFSKISIPNSITNPVKATTSKVNADMKRNSSLTSAYRLAPKPLFAPSSNGDAKFQKWGKTLERSDRGSSTSNSITDPESSYLNSNDLLFDPDRRYLKHLVIKNNKNLNVINHNDDEASKVKLVTFTTESASKDDQASSSIAASKLTEKAHSPQTDLKDDHDESTPDPQSKSPNGSTSIPMIENEKISSKVPGLLSNDVTFFKNNYYISPSIETLGNKSLIELRKINNLVIGHRNYGKVEFLEPVDLLNTPLDTLCGDLVTFGPKSCSIYENCSIKPEKGEGINVRCRVTLYSCFPIDKETRKPIKNITHPLLKRSIAKLKENPVYKFESYDPVTGTYSYTIDHPVLT
Protein: Histone H2B type 1-C/E/G (Q6ZWY9)
Organism: Mus musculus (Mouse)
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
- Histone H3.3
- Histone H3.2
- Histone H3.1
- Histone H2A type 1-B
- Breast cancer type 1 susceptibility protein homolog
- Histone H2A type 3
- Histone H2A type 2-A
- BRCA1-associated RING domain protein 1
- Cyclic GMP-AMP synthase
Sequence:
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Anthranilate synthase alpha subunit 1, chloroplastic (EC 4.1.3.27) (Anthranilate synthase component 1-1) (Anthranilate synthase component I-1) (Protein A-METHYL TRYPTOPHAN RESISTANT 1) (Protein JASMONATE-INDUCED DEFECTIVE LATERAL ROOT 1) (Protein TRYPTOPHAN BIOSYNTHESIS 5) (Protein WEAK ETHYLENE INSENSITIVE 2) (P32068)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS to produce anthranilate. Plays an important regulatory role in auxin production via the tryptophan-dependent biosynthetic pathway.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Anthranilate synthase beta subunit 1, chloroplastic
- Anthranilate phosphoribosyltransferase, chloroplastic
- Anthranilate synthase beta subunit 2, chloroplastic
- anthranilate synthase
- anthranilate synthase
- Indole-3-glycerol phosphate synthase, chloroplastic
- indole-3-glycerol-phosphate synthase
- Chorismate synthase, chloroplastic
- Anthranilate phosphoribosyltransferase
- Tryptophan synthase alpha chain, chloroplastic
Sequence:
MSSSMNVATMQALTFSRRLLPSVASRYLSSSSVTVTGYSGRSSAYAPSFRSIKCVSVSPEASIVSDTKKLADASKSTNLIPIYRCIFSDQLTPVLAYRCLVKEDDREAPSFLFESVEPGSQMSSVGRYSVVGAQPAMEIVAKENKVIVMDHNNETMTEEFVEDPMEIPRKISEKWNPDPQLVQDLPDAFCGGWVGFFSYDTVRYVEKRKLPFSKAPEDDRNLPDMHLGLYDDVVVFDHVEKKAYVIHWIRLDGSLPYEKAYSNGMQHLENLVAKLHDIEPPKLAAGNVNLQTRQFGPSLDNSNVTCEEYKEAVVKAKEHILAGDIFQIVLSQRFERRTFADPFEVYRALRVVNPSPYMGYLQARGCILVASSPEILTKVKQNKIVNRPLAGTSKRGKNEVEDKRLEKELLENEKQCAEHIMLVDLGRNDVGKVTKYGSVKVEKLMNIERYSHVMHISSTVTGELQDGLTCWDVLRAALPVGTVSGAPKVKAMELIDELEPTRRGPYSGGFGGVSFTGDMDIALSLRTIVFPTACQYNTMYSYKDANKRREWVAYLQAGAGVVADSDPQDEHCECQNKAAGLARAIDLAESAFVKK
Protein: Paired box protein Pax-6 (Pax[Zf-a]) (P26630)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor expressed in spatially restricted regions of the neural tube during embryonic development.
Subcellular location: Nucleus.
Interaction partners:
- Six3
- Sine oculis homeobox homolog 3a.
- Oligodendrocyte lineage transcription factor 2.
- Transcription factor Sox-2
- Sonic hedgehog protein
- Insulin gene enhancer protein isl-1
- Neurogenic differentiation factor 1
- Homeobox protein Nkx-2.2a
- Forkhead box protein G1
- Neurog3 protein
Sequence:
MPQKEYYNRATWESGVASMMQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVGKIAQYKRECPSIFAWEIRDRLLSEGVCTNDNIPSVSSINRVLRNLASEKQQMGADGMYEKLRMLNGQTGTWGTRPGWYPGTSVPGQPNQDGCQQSDGGGENTNSISSNGEDSDETQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNSSSHIPISSSFSTSVYQPIPQPTTPVSFTSGSMLGRSDTALTNTYSALPPMPSFTMANNLPMQPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQAHMNSQSMAASGTTSTGLISPGVSVPVQVPGSEPDMSQYWPRLQ
Protein: Kv channel-interacting protein 4 (KChIP4) (A-type potassium channel modulatory protein 4) (Calsenilin-like protein) (Potassium channel-interacting protein 4) (Q6PIL6)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates KCND2 channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. Modulates KCND3/Kv4.3 currents. Isoform 4 does not increase KCND2 expression at the cell membrane. Isoform 4 retains KCND3 in the endoplasmic reticulum and negatively regulates its expression at the cell membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11847232}; Peripheral membrane protein {ECO:0000305|PubMed:11847232}. Cytoplasm {ECO:0000269|PubMed:11847232, ECO:0000269|PubMed:23576435}. Peroxisome {ECO:0000269|PubMed:22057399}.; SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum {ECO:0000269|PubMed:23576435}.
Interaction partners:
- A-type voltage-gated potassium channel KCND3
- A-type voltage-gated potassium channel KCND1
- A-type voltage-gated potassium channel KCND2
- Voltage-gated potassium channel KCNC1
- A-type potassium channel modulatory protein KCNIP1
- A-type potassium channel modulatory protein KCNIP2
- Presenilin-2
- Serine/threonine-protein kinase Kist
- A-type potassium channel modulatory protein DPP6
Sequence:
MNVRRVESISAQLEEASSTGGFLYAQNSTKRSIKERLMKLLPCSAAKTSSPAIQNSVEDELEMATVRHRPEALELLEAQSKFTKKELQILYRGFKNECPSGVVNEETFKEIYSQFFPQGDSTTYAHFLFNAFDTDHNGAVSFEDFIKGLSILLRGTVQEKLNWAFNLYDINKDGYITKEEMLDIMKAIYDMMGKCTYPVLKEDAPRQHVETFFQKMDKNKDGVVTIDEFIESCQKDENIMRSMQLFENVI
Protein: AT03213p (GEO08525p1) (Yellow-emperor, isoform A) (Q9VBQ0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MALRLTTIALLHRAPLLVVPKLKATPPTRTLLLRKNLVPFLDDDPCVFSKKAVMHHWGVLPILFITLVGGILKVGAMIRLALVKDDVFFTKDSAYYMYLETRKGPWYKQKSRKWGGRDEYDMPPGLLLANQGDVSGPSF
Protein: Zinc finger CCCH domain-containing protein 3 (Smad-interacting CPSF-like factor) (Q8IXZ2)
Organism: Homo sapiens (Human)
Function: Required for the export of polyadenylated mRNAs from the nucleus. Enhances ACVR1B-induced SMAD-dependent transcription. Binds to single-stranded DNA but not to double-stranded DNA in vitro. Involved in RNA cleavage (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8CHP0}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 1
- Symplekin
- Pre-mRNA 3'-end-processing factor FIP1
- Cleavage stimulation factor subunit 1
- Cleavage and polyadenylation specificity factor subunit 5
- Cleavage and polyadenylation specificity factor subunit 2
- Pre-mRNA cleavage complex 2 protein Pcf11
- Protein virilizer homolog
- Cleavage stimulation factor subunit 2
- Polyribonucleotide 5'-hydroxyl-kinase Clp1
Sequence:
MEEKEILRRQIRLLQGLIDDYKTLHGNAPAPGTPAASGWQPPTYHSGRAFSARYPRPSRRGYSSHHGPSWRKKYSLVNRPPGPSDPPADHAVRPLHGARGGQPPVPQQHVLERQVQLSQGQNVVIKVKPPSKSGSASASGAQRGSLEEFEETPWSDQRPREGEGEPPRGQLQPSRPTRARGTCSVEDPLLVCQKEPGKPRMVKSVGSVGDSPREPRRTVSESVIAVKASFPSSALPPRTGVALGRKLGSHSVASCAPQLLGDRRVDAGHTDQPVPSGSVGGPARPASGPRQAREASLVVTCRTNKFRKNNYKWVAASSKSPRVARRALSPRVAAENVCKASAGMANKVEKPQLIADPEPKPRKPATSSKPGSAPSKYKWKASSPSASSSSSFRWQSEASSKDHASQLSPVLSRSPSGDRPAVGHSGLKPLSGETPLSAYKVKSRTKIIRRRSSTSLPGDKKSGTSPAATAKSHLSLRRRQALRGKSSPVLKKTPNKGLVQVTTHRLCRLPPSRAHLPTKEASSLHAVRTAPTSKVIKTRYRIVKKTPASPLSAPPFPLSLPSWRARRLSLSRSLVLNRLRPVASGGGKAQPGSPWWRSKGYRCIGGVLYKVSANKLSKTSGQPSDAGSRPLLRTGRLDPAGSCSRSLASRAVQRSLAIIRQARQRREKRKEYCMYYNRFGRCNRGERCPYIHDPEKVAVCTRFVRGTCKKTDGTCPFSHHVSKEKMPVCSYFLKGICSNSNCPYSHVYVSRKAEVCSDFLKGYCPLGAKCKKKHTLLCPDFARRGACPRGAQCQLLHRTQKRHSRRAATSPAPGPSDATARSRVSASHGPRKPSASQRPTRQTPSSAALTAAAVAAPPHCPGGSASPSSSKASSSSSSSSSPPASLDHEAPSLQEAALAAACSNRLCKLPSFISLQSSPSPGAQPRVRAPRAPLTKDSGKPLHIKPRL
Protein: Exosome component CSL4 (Q57VE3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Ribosomal RNA-processing protein 43
- Ribosomal RNA processing protein 4
- Ribosomal RNA processing protein 45
- Exosome complex exonuclease RRP40
- RNasePH-like protein exosome-associated protein 1 Rrp42 homologue
- Elongation factor 1-alpha, putative
- ATP-dependent DEAD/H RNA helicase, putative
- Ribosomal RNA processing protein 6
- CCHC-type domain-containing protein
- Exosome-associated protein 4
Sequence:
MAVIVKTGKCVSPGDVLYATDIYDAIGTIVVAASDTGAVSAGNHADDAIIAGTGCYSRVVSKSDGAVSSQIITTLLGIVQWSGNVVSVRQPTKRARDATTIEVVSLNALKDAGTCGDSATPRLSTPGEATSSVSETPASTAVSTAPKSLWISTSVFGPRMGDNVHLRVVRVSRSFAYGEIIAVNGTWCSNSGSNGGGGGALGGFRGVIRMEDIRPFKPRKDQLTPPPPADAFQDGDVVVATVLSQSDVRQYQLSTVAEHCGVVEAFTVLNSNGRERRVRLRHIPECRDIMKCPLSGNLHRRWCPLIRLV
Protein: Uncharacterized amino-acid permease C74.04 (O74537)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized transporter PB1C11.03
- UPF0654 protein C869.09
- Uncharacterized methyltransferase C70.08c
- Uncharacterized sulfatase PB10D8.02c
- Probable secreted beta-glucosidase C2G2.17c
Sequence:
MAIPILDALTSSSGKKNSAEFSIHSTSNPTNPEEPNITSEADNAEDLAALGYKQEFQRGLSLFSVFSVSFSLLGLLPSVATTLPYSIGYTGTPGLLWGWLIAMVFIICIALSMAELCSAMPTSGGLYYAAAVLAPEGWGPLAAWFTGWSNYIAQLVGGPSINYSTAAMLLGAVNIGNPNYEVQNYQLFLVSIAIQFIHFILASMPTKYIAKLNSVGTYLNTLFLFISMIVILAMSSKNHGFNETSKVWSHIENYTDWPDGFAILMSFCGVIWTMSGYDAPFHMSEETANASVNAPRGIILTAAIGGIMGWVMQIVIAYTVVDQTAVVTGSDSMWATYLSQCLPKRAALGILSLTIVSSFLMGQSNLIASSRIAYSYARDGVLPYSEWVATVNPITKTPIRAVFVNFVIGVLILFLAFAGAITIGAVFSVTAIAAFTAFVAPVAMRVFFVKDADFRTGPFNLGKFSKPIGFCSVSFVALMIPILCFPSVKNPTPAEMNWTCLVFGAPMLAVLIWYAISGRKWFKGPRINLASEGDNSTLEGVELYTGSEELPQKKEKE
Protein: Angiomotin-like protein 2 (Leman coiled-coil protein) (LCCP) (Q9Y2J4)
Organism: Homo sapiens (Human)
Function: Regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Required for proper architecture of actin filaments. Inhibits the Wnt/beta-catenin signaling pathway, probably by recruiting CTNNB1 to recycling endosomes and hence preventing its translocation to the nucleus. Participates in angiogenesis. May play a role in the polarity, proliferation and migration of endothelial cells. Selectively promotes FGF-induced MAPK activation through SRC.
Subcellular location: Recycling endosome {ECO:0000250|UniProtKB:A1YB07}. Cytoplasm {ECO:0000269|PubMed:23911299}. Cell projection, podosome {ECO:0000250|UniProtKB:Q8K371}. Cell junction {ECO:0000269|PubMed:28842668}.
Interaction partners:
- Merlin
- Transcriptional coactivator YAP1
- Angiomotin
- InaD-like protein
- Multiple PDZ domain protein
- Rho GTPase-activating protein 17
- Serine/threonine-protein kinase LATS2
- Angiomotin-like protein 1
- Protein kinase C zeta type
- Protein kinase C iota type
Sequence:
MRTLEDSSGTVLHRLIQEQLRYGNLTETRTLLAIQQQALRGGAGTGGTGSPQASLEILAPEDSQVLQQATRQEPQGQEHQGGENHLAENTLYRLCPQPSKGEELPTYEEAKAHSQYYAAQQAGTRPHAGDRDPRGAPGGSRRQDEALRELRHGHVRSLSERLLQLSLERNGARAPSHMSSSHSFPQLARNQQGPPLRGPPAEGPESRGPPPQYPHVVLAHETTTAVTDPRYRARGSPHFQHAEVRILQAQVPPVFLQQQQQYQYLQQSQEHPPPPHPAALGHGPLSSLSPPAVEGPVSAQASSATSGSAHLAQMEAVLRENARLQRDNERLQRELESSAEKAGRIEKLESEIQRLSEAHESLTRASSKREALEKTMRNKMDSEMRRLQDFNRDLRERLESANRRLASKTQEAQAGSQDMVAKLLAQSYEQQQEQEKLEREMALLRGAIEDQRRRAELLEQALGNAQGRAARAEEELRKKQAYVEKVERLQQALGQLQAACEKREQLELRLRTRLEQELKALRAQQRQAGAPGGSSGSGGSPELSALRLSEQLREKEEQILALEADMTKWEQKYLEERAMRQFAMDAAATAAAQRDTTLIRHSPQPSPSSSFNEGLLTGGHRHQEMESRLKVLHAQILEKDAVIKVLQQRSRRDPGKAIQGSLRPAKSVPSVFAAAAAGTQGWQGLSSSERQTADAPARLTTDRAPTEEPVVTAPPAAHAKHGSRDGSTQTEGPPDSTSTCLPPEPDSLLGCSSSQRAASLDSVATSRVQDLSDMVEILI
Protein: Bone morphogenetic protein 7 (Osteogenic protein 1), isoform CRA_b (cDNA FLJ78019, highly similar to Homo sapiens bone morphogenetic protein 7 (osteogenic protein 1), mRNA) (cDNA, FLJ92758, Homo sapiens bone morphogenetic protein 7 (osteogenic protein 1)(BMP7), mRNA) (A8K571)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MHVRSLRAAAPHSFVALWAPLFLLRSALADFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAMAVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPRYHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLLDSRTLWASEEGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKATEVHFRSIRSTGSKQRSQNRSKTPKNQEALRMANVAENSSSDQRQACKKHELYVSFRDLGWQDWIIAPEGYAAYYCEGECAFPLNSYMNATNHAIVQTLVHFINPETVPKPCCAPTQLNAISVLYFDDSSNVILKKYRNMVVRACGCH
Protein: O-methyltransferase kntB (EC 2.1.1.-) (Kotanin biosynthesis cluster protein B) (A2QK65)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.
Interaction partners:
Sequence:
MTYPEEIDEYSLIQNGLKSLNEAAQRCQQTKHSSQDSSIEGCSARQSARDELVLEALKFLQIAQGPIDAAATCYERTAHLASVRALLEMGVFEALPTGRVSRRTEELARELNVDESLLARLLRNSSLYGPFEETGPGQYRHTPFSEAYLRPEIRGMFRFAMDDHMPAHLKLHEFLQRNGWQEPSSTTDNPYTYAHKTNGKSMFDNLSEKPERMKAFNNGMTVQAMTPLWMIDLFPWRSLAQLKPTAGQVLAVDIGGGKGKAISRIRSFCNGLPGRYILQDQEHVVKSVEGSLDPSIERMAYNFFTEQPIRGAVTYLIRRCLHNWPQDSVVCILQNIAAAMEPGKSRLLIEEIVVPAEKAGVEEGWMDMIMMSLGAKQRTLKEWEMVLGLAGLEVKKVYQIPGNCHGLIEAWLK
Protein: Aphidicolan-16-beta-ol synthase (EC 4.2.3.42) (EC 5.5.1.14) (Q96WT2)
Organism: Neocamarosporium betae (Beet black rot fungus) (Pleospora betae)
Function: Aphidicolan-16-beta-ol synthase; part of the gene cluster that mediates the biosynthesis of aphidicolin, a specific inhibitor of eukaryotic DNA synthesis and DNA polymerase alpha. The geranylgeranyl pyrophosphate synthase GGS is required for supplying a sufficient amount of geranylgeranyl diphosphate (GGDP), the general precursor of diterpenes. The diterpene synthase ACS then catalyzes the conversion of geranylgeranyl diphosphate to aphidicolan-16-beta-ol via the intermediate syn-copalyldiphosphate (syn-CDP). In addition to aphidicolan-16-beta-ol, the enzyme produces also low levels of amphidicol-15-ene and amphidicol-16-ene. The cytochrome P450 monooxygenase P450-2 then catalyzes the two-step hydroxylation from aphidicolan-16-beta-ol to 3-deoxyaphidicolin via a 17,3-deoxyaphidicolin intermediate. Finally, the cytochrome P450 monooxygenase P450-1 converts 3-deoxyaphidicolin to aphidicolin.
Interaction partners:
Sequence:
MVPISTRSEVQDGLIAQARSLITRIVHNSDDVYGFGTLSCTVYDTAWVALVTKHVNGIKHWLFPESFHYILASQCDDGTWCEDKTAQFDGVLNTIAGLLVLKRYRRDPLQLKVDNRDLDSRIKLATSALHSLLEEWDVSTTNNVGFEIIVPTMLDLLVQEDPSLSFELKGREALTEIREAKMNRFQPELLYQGKLMTLTHSLEALLGRIDYDNVARYTVKGSMFASPSSTAAYLMSASTWDDEAETYLRYTITASTGKGSGGVPGVFPTTYFEYTWILSTLFRAGFQSSELDSPELTAMTDTLLKAFKAFSGAIGLDSGIEPDVDDSAKIVTTLNMLGKPAHARYLCDNFEVETHFRVYPRERDPSFSANCNALAAFLHQPDVEVYSSQILKAASYLCERMWNADEKIDDKWNKSHLYSSFLYTQVMTDLMAITEAGRLDGVFTRELLTRVCVTIFQSCLRAMLKQSHDGSWNQSLEETAYAILHLTEARRLCFFEQISEPLENSIYRGITFLTTIDKPPMEYLWSDKVSYGSAYLAETYVLAARRAAESTSVTNLVGSSIWKDNASTKMHKLVGLFHRTPLLKALPKWELQASMIEASIYQGLLQDARLEVLQRPKVDGGEYLSIIPFTWTSCSNSARTNASASHLWELMALSFFTYQVDEFMEAVAGPAFKGRMTHLHAIIDEAVHCSQNRERTPGECENTNHVTSELLQAVRFILDNPTVRKASPYDRNTLLQELRIFLHAHVTQVEDNASFGRERLTGDKALTSYRSQLYRWVHTISSDHIAGPFCFYYATCLLGATLTAHPPNDCFPKSSQKYLAAATCRHLSCMCRMYNDIGSWNRDHREGNLNCLHFPEFSETTSDDAERKASLLTLAQYERKQWCNALQQLEKEMVHGASEPAAARLAKRRACLIDMFCKVTDLYGQIYVLRDVSSVIKDVVRNGE
Protein: Guanine nucleotide-binding protein subunit alpha (Q8T3G5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MRIIHGQGYSEEDKRAHIRLVYQNVFMAIQSMIRAMDTLDIKFGNESEELQEKAAVVREVDFESVTSFEEPYVSYIKELWEDSGIQECYDRRREYQLTDSAKYYLSDLRRLAVPDYLPTEQDILRVRVPTTGIIEYPFDLEQIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVECDNENRMEESKALFRTIITYPWFTNSSVILFLNKKDLLEEKILYSHLADYFPEYDGPPRDPIAAREFILKMFVDLNPDADKIIYSHFTCATDTENIRFVFAAVKDTILQHNLKEYNLV
Protein: WASH complex subunit 4 (A0A087X256)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAVETLSPDWEFDRVDDGSQKIHAEVQLKNYGKFLEEYTSQLRRIEDALDDSIGDVWDFNLDPIALKLLPYEQSSLLELIKTENKVLNKVITVYAALCCEIKKLKYEAETKFYNGLLFYGEGATDASMVEGDCQIQMGRFISFLQELSCFVTRCYEVVMNVVHQLAALYISNKIAPKIIETTGVHFQTMYEHLGELLTVLLTLDEIIDNHITLKDHWTMYKRLLKSVHHNPSKFGIQEEKLKPFEKFLLKLEGQLLDGMIFQACIEQQFDSLNGGVSVSKNSTFAEEFAHSIRSIFANVEAKLGEPSEIDQRDKYVGICGLFVLHFQIFRTIDKKFYKSLLDICKKVPAITLTANIIWFPDNFLIQKIPAAAKLLDRKSLQAIKIHRDTFLQQKAQSLTKDVQSYYVFVSSWMMKMESILSKEQRMDKFAEDLTNRCNVFIQVGFLYAYSISTIIKTTMNLYMSMQKPMTKTSVKALCRLVELLKAIEHMFYRRSMVVADSVSHITQHLQHQALHSISVAKKRVISDKKYSEQRLDVLSALVLAENTLNGPSTKQRRLIVSLALSVGTQMKTFKDEELFPLQVVMKKLDLISELRERVQTQCDCCFLYWHRAVFPIYLDDVYENAVDAARLHYMFSALRDCVPAMMHARHLESYEILLDCYDKEIMEILNEHLLDKLCKEIEKDLRLSVHTHLKLDDRNPFKVGMKDLALFFSLNPIRFFNRFIDIRAYVTHYLDKTFYNLTTVALHDWATYSEMRNLATQRYGLVMTEAHLPSQTLEQGLDVLEIMRNIHIFVSRYLYNLNNQIFIERTSNNKHLNTINIRHIANSIRTHGTGIMNTTVNFTYQFLKKKFYIFSQFMYDEHIKSRLIKDIRFFREIKDQNDHKYPFDRAEKFNRGIRKLGVTPEGQSYLDQFRQLISQIGNAMGYVRMIRSGGLHCSSNAIRFVPDLEDIVNFEELVKEEGLAEETLKAARHLDSVLSDHTRNSAEGTEYFKMLVDVFAPEFRRPKNIHLRNFYIIVPPLTLNFVEHSISCKEKLNKKNKIGAAFTDDGFAMGVAYILKLLDQYREFDSLHWFQSVREKYLKEIRAVAKQQNVQSASQDEKLLQTMNLTQKRLDVYLQEFELLYFSLSSARIFFRADKTAAEENQEKKEKEEETKTSNGDLSDSTVSADPVVK