wanglab/gogpt-training-data huggingface dataset:
Protein: Agamous-like MADS-box protein AGL18 (Q9M2K8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in the negative regulation of flowering, probably through the photoperiodic pathway. Prevents premature flowering. Downstream regulator of a subset of the MIKC* MADS-controlled genes required during pollen maturation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
Interaction partners:
- Agamous-like MADS-box protein AGL80
- COP1-interacting protein-like protein
- Homeodomain-like superfamily protein
- F-box protein AFR
Sequence:
MGRGRIEIKKIENINSRQVTFSKRRNGLIKKAKELSILCDAEVALIIFSSTGKIYDFSSVCMEQILSRYGYTTASTEHKQQREHQLLICASHGNEAVLRNDDSMKGELERLQLAIERLKGKELEGMSFPDLISLENQLNESLHSVKDQKTQILLNQIERSRIQEKKALEENQILRKQVEMLGRGSGPKVLNERPQDSSPEADPESSSSEEDENDNEEHHSDTSLQLGLSSTGYCTKRKKPKIELVCDNSGSQVASD
Protein: Promoter binding protein (A4GXB6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
RRKPPPGSLFSSPYGRLSSSIIENGSRGGSFIVDFSAYPRLSGRDAWPAARSLECITGNRSTATGSSFSHPRQNNSSKPPHDHFLQGSPCGTSFSSTGISPGECFTGSGDSSCALSLLSNQPWGSRNQALNFSVNGVISTEGSSASP
Protein: Ras-related protein rab7 (H9BW96)
Organism: Epinephelus coioides (Orange-spotted grouper) (Epinephelus nebulosus)
Function: Key regulator in endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades. Plays important roles in microbial pathogen infection and survival, as well as in participating in the life cycle of viruses (By similarity).
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:P51149}; Lipid-anchor {ECO:0000305}. Lysosome membrane {ECO:0000269|PubMed:24161772}; Lipid-anchor {ECO:0000305}. Note=Aggregates into the viral factories in cells infected by Singapore grouper iridovirus (SGIV) in the late stages of the infection. {ECO:0000269|PubMed:24161772}.
Interaction partners:
Sequence:
MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVTTKRAQAWCQSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPIKLDRNERAKPSAETCSC
Protein: Regulatory protein B-Peru-like (Q657A4)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRVPTSWGFVYSRVNKVSEEPNVVNRITTAFWELQLPACSDEPISSGTPSSPSSPPTKETGDANTVVIDDLFLAHSDAILPAGGDQKEEHQLGDDLGQQQAATAMEIDDDVIYSLIRNWDNDSSSSWIELLDHAIVSPASCFVPWKRTELDKEAVAGGEAAQRLLKKVVGGGGAWMNRAAGSCSIKNHVMSERRRREKLNEMFLILKSLVPSIDKVDKASILSETIAYLKELERRVQELESGKKVSRPAKRKPCSETIIGGGGGGGGAGAVKEHHHWVLSESQEGTPSDVRVIVMDKDELHLEVQCRWKELMMTRVFDAIKSLRLDVVSVQASAPDGLLGLKIRAKYASSAAVVPAMISETLRTAVAGY
Protein: ATP-dependent DNA helicase tlh2 (EC 5.6.2.4) (DNA 3'-5' helicase thl2) (Sub-telomeric helicase RecQ homolog 2) (Telomere-linked helicase 2) (Q1RKN3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Exhibits ATP-dependent 3' to 5' DNA helicase activity and has a role in telomerase-independent telomere maintenance. Represses ade6 at an ectopic site.
Interaction partners:
- DNA repair protein rhp51
- DNA topoisomerase 3
- Putative MutL protein homolog 1
- ATP-dependent DNA helicase srs2
- Replication factor A protein 1
- RecQ-mediated genome instability protein 1
- Uncharacterized protein CPT2R1.03
- UPF0494 membrane protein C212.04c
- Exodeoxyribonuclease 1
- ATP-dependent DNA helicase II subunit 1
Sequence:
MVVASEIAKVASKTARDIAGCFTCQCGTQFDNVERIVQHFKECRYRDETCKDDDIVVYEPSSFVQDEKKDKPIIVEAASEATSEEACNSSKERQLPALSALSALSTLTTSANDDLWTARLIWQSTNDTKLDNSPSSNYTDLNHKLANYGLSILSIHALMCVECECLLNVIHTAQHMQIVHKLELNEDLLWFQELRTLKLKSPTNVLQTHSSQTHVYPYIRGLPVLLNGYECVPCTKNGTGFVHAIMDTFRHHVRRTHGKVIKLENCIRRTALQTVKNKYAQRCQFFKVDYVPLNGGEEEEEEEGEEKEDAQNIKERMVDFCFSKFMEKNQQRREQQDKGENKKRQDDVDQATDNNTNTILEDDEKDNDEEEEEEIVNAREKNLLNQQFNWTAIVKKLGENWDQLVRFEYTNGIVTLDTIVNQLIRYYYRGFRHLSGMTMGMRRMFTQGGSYSAQERGLCRLEQKDTVVRYAQSAALYLIFLLRRPSADSGIRRHLEAMCGATVERKEGGSNSSSNISNVANFDSAEDDNDNDNDNDRDSNNNNNNNNTNTDDDDKLAYLELHEALKLAFLQQYDFSKNVQDLEIMEFLACMSLHKDGTSKYAYEISACFAPLIYTCRLVAACELQRLIDEKQIDLLSIPSFQTAGSIAYAHVFCFITLGQRNLYDVLYETQKVVRDIIRTEGYANTLQGLSPSTVLFQPRSNSMYPCIGDAFNNMVRLDLSELTALYEGMFAKVQDLLKELCFDMNVEKLLPISLLRSIGDDINNSKLGYSFFKESIEIRSSHSVLLRTILKNSELCHRFFPSMSKKDLTKLFGGVSDQQRNECDNYSNHYNDNSNDNDNDVFLKLHWSKSAIKKYETKASIFNELLFCLVYISAGQPARAQEMVYWTLRNGKYKTRELYLMFGRLMIYSRYDKTRNMKFAEKPIPRFLSEPLSILALRYYVLVRPLEALMKYVTTADRSKVAVYLDFMFVIAGERLQRDLPYRIFPKATYQCIQKPLGFRNYRHIAHYFKEKNIEEEMTRESYFDLQAGHTRNTALYIYGRTMDNLHYLPSDYFANFFRASYKWQELLQIRDNPTHGLLVETKHPFIKRVDQLEEALNEKLARLVGEQMVEGDKEKDKTNEEKNKDEVKAEMTQPVVNQDSHDLQDQLATTPTAPTAFHYRPGLLQPSQTSVQHCCWALSQYYGLEAKFRSLKQFQSVYFSLLNRMNLITVLPTGGGKSLSFLIPALIEKKRQTPGKVMNMVTLVLVPMMSLRQDMMLRVNEKGLLVCSGNWTAFKDVRLTLETQLPDLFILTYESALTNSGLRFFESLATLGRLARVVIDEAHLLLTSGAWRTALSRASRLSGLYAPLHLLSATFPRQLEMVARQTFCTNFYVLRETSTARENIFYFLHPYDNTEFLLDLRTLMKRTKVFEGDGRAIIFCRTKKDVEYIHRRLHQSDLFAHTHVTIYTGDVSDEERQMNFDAFRNANGKTRIMIATKAFGLGINYMGVRLVVHYGLPASSMDYVQETGRAGRDGKYAIAALFYEKYDSTWSSYVEDSMKNFLNDNTMCVRSFLASEMDGECVCCASFANCVYCSRCSDSLLGEESTVSTMYGVKPTLPETPKPAIATHSRYNASFSSSPPPQPGNSSGMSAMNTNTTSTTPVSLSELSEITLFPSSVSPTWKKSFGNANTNLKYGLEDMSLSHRRGHKRTYDEHLNNVQQGVNHDMNRVHGSVGGMSGIVGIGIGIGDGDGDGDVDSRTIHFAEYKSRVQAVKKQWVDSTDISAQLERFFRVYKDECLSCTLGNPDTEIRAHTGKACPVRLSTCYKCGKADHNLRECKLRIRFQGLCLFCGLTKFEHADSDMAYTSDCRSWARKANLISLVYYAWNNVQYRRTIADKFLQGDVRDQAFYGFVCCSTTTNSAFVLVIHYLLSDVLQIM
Protein: Carboxynorspermidine/carboxyspermidine decarboxylase (CANS DC/CAS DC) (CANSDC/CASDC) (EC 4.1.1.96) (Q9KRL4)
Organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Function: Catalyzes the decarboxylation of carboxynorspermidine and carboxyspermidine. Essential for biofilm formation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Carboxynorspermidine synthase
- Bifunctional aspartokinase/homoserine dehydrogenase
- Bifunctional aspartokinase/homoserine dehydrogenase
- Glutamate-pyruvate aminotransferase AlaA
Sequence:
METLQDIGTNMLKDELRTPYFMIDEAKLIANLEIAKHLKEISGVKMVLALKCFSTWGVFDIIKPYLDGTTSSGPFEVKLGYETFGGETHAYSVGYSEEDVKEVIDICDKMIFNSQSQLAAYRHLVEGKASLGLRINPGVSYAGQDLANPARQFSRLGVQADHIDESVFDSINGVMFHMNCENKDVDAFIGLLDAISERFGRYLDKLDWVSLGGGVFFTWPGYDVEKLGAALKAFAERHAVQLYLEPGEAIITKTTDLVVTVVDIVENGMKTAIVDSATEAHRLDTLIYKEPASVLEASDKGQHEYVIGSCSCLAGDQFCVAKFDEPLQVGQKLHILDSAGYTMVKLNWFNGLKMPSVYCERKNGQIQKINQFGYEDFKRTLSLWSIE
Protein: Calcium uptake protein 1, mitochondrial (Calcium-binding atopy-related autoantigen 1 homolog) (Q8VCX5)
Organism: Mus musculus (Mouse)
Function: Key regulator of mitochondrial calcium uniporter (MCU) that senses calcium level via its EF-hand domains. MICU1 and MICU2 form a disulfide-linked heterodimer that stimulates and inhibits MCU activity, depending on the concentration of calcium. MICU1 acts both as an activator or inhibitor of mitochondrial calcium uptake (By similarity). Acts as a gatekeeper of MCU at low concentration of calcium, preventing channel opening (By similarity). Enhances MCU opening at high calcium concentration, allowing a rapid response of mitochondria to calcium signals generated in the cytoplasm. Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake (By similarity). Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG (By similarity).
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:30504268}. Mitochondrion inner membrane {ECO:0000269|PubMed:30504268}. Note=Recruited to the mitochondrial inner membrane by EMRE/SMDT1 (By similarity). Also localizes to mitochondrial cristae junctions (By similarity). {ECO:0000250|UniProtKB:Q9BPX6}.; SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion intermembrane space {ECO:0000305|PubMed:27818145}. Mitochondrion inner membrane {ECO:0000305|PubMed:27818145}.
Interaction partners:
- Calcium uniporter protein
- Calcium uptake protein 2, mitochondrial
- Mitochondrial calcium uniporter regulator 1
- Essential MCU regulator, mitochondrial
- Calcium uniporter regulatory subunit MCUb, mitochondrial
- Mitochondrial adenyl nucleotide antiporter SLC25A23
- Calcium uptake protein 3, mitochondrial
- Mitochondrial proton/calcium exchanger protein/H
- Mitochondrial sodium/calcium exchanger protein
- Prohibitin-2
Sequence:
MFRLNTLSALAELAVGSRWYHGASQPTQTKRRLMLVAFLGASAVTASTGLLWKKAHAESPPCVNSKKPDTEDKERNKDSGEVSSREGRAADAAAEPYPEDKKKKRSGFRDRKVMEYENRIRAYSTPDKIFRYFATLKVINEPGETEVFMTPQDFVRSITPNEKQPEHLGLDQYIIKRFDGKKIAQEREKFADEGSIFYSLGECGLISFSDYIFLTTVLSTPQRNFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRPTTGNTLKSGLCSALTTYFFGADLKGKLTIKNFLEFQRKLQHDVLKLEFERHDPVDGRISERQFGGMLLAYSGVQSKKLTAMQRQLKKHFKDGKGLTFQEVENFFTFLKNINDVDTALSFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQRLMRGLEKPKDMGFTRLMQAMWKCAQETAWDFALPK
Protein: Dret protein (Q7JQD5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
SPPTVDYDKDVSVYRSAASNFRVVQPDSFLDLMRLRSIRFDIVEDKLGAFGITSTSGIVFVKNPQVLEEAPETIYFLNVTWIDQQRLSHVRVINVHLVHGRPENTSCELKVKSRSQTCAQIKYQSQCVRYCGLATGGGSCQWRGSNSAMFGTRYGSCVPESRYCPDHVCDPLEELNPMACPQDCTPAGRIVGPHSSNENKRGIYSASGTCICEDNGKCSCAPLDEEPKMKKPRKRKNETEAEPLLGVRRGTPPNQPLQDPMLLGVLNAAGFECDRSCMFFVITCPLLFVLLLLCLLIAQRKMLQRRLGKQSMTTSSKQALPESGGGDFALMPLQSGFRFESGDAKWEFPREKLQLDTVLGEGEFGQVLKGFATEIAGLPGITTVAVKMLKKGSNSVEYMALLSEFQLLQEVSHPNVIKLLGACTSSEAPLLIIEYARYGSLRSYLRLSRKIECAGVDFADGVEPVNVKMVLTFAWQICKGMAYLSELKLVHRDLAARNVLLADGKICKISDFGLTRDVYEDDAYLKRSRDRVPVKWMAPESLADHVYTSKSDVWSFGVLCWELITLGASPYPGIAPQNLWSLLKTGYRMDRPENCSEAVYSIVRTCWADEPNGRPSFKFLASEFEKLLGNNAKYIDLETNAVSNPLYCGDDSALITTELGEPESLQHLWSPPKIAYDIHDQATSYDQSEEEMPVTSTAPPGYDLPRPLLDATANGQVLRYENDLRFPLNIRKSSCTPSYSNMTSEPPATTSLPHYSVPVKRGRSYLDMTNKSLIPDNLDSREFEKHLSKTISFRFSSLLNLSETKEVSPGWQAEDAV
Protein: UPF0496 protein At3g28270 (Q9LHD9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MALSKDLMLKCSEDMMSAYKSACEEHPKLKSFDASLQQRTNKMIDSLTVEDKNGSSSPHDAHMELSKHLVEVTQGVADFITEIEDDVWDNQALKYLVLAYFENTKKTLEIFKTIENCVENAEMGQLLIREALAEFEKESAEKDVGGKKKKYEKTLEDLKSFKEMGDPFDGKVLTTQFERIKKQQESLLEEVSETRKKIQDEISNLEKKTLITNVVFGAAFAIVAVASIALIATGVGAAAGFGALAAPLLAAGWAGVYTTLDKKKDALNKQLEGLKKVEEIEESVEKGIKTNEEATETVSILVDGLEDRIKNMLKLVDNAIDHEDNEAATRIVLTQISKKVEKLTKKITEVGESVEDHSKLIAKARLQVLQKINR
Protein: Serine/threonine-protein kinase BRSK1 (EC 2.7.11.1) (EC 2.7.11.26) (Brain-specific serine/threonine-protein kinase 1) (BR serine/threonine-protein kinase 1) (Serine/threonine-protein kinase SAD-B) (B2DD29)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine-protein kinase that plays a key role in polarization of neurons and centrosome duplication. Phosphorylates CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following phosphorylation and activation by STK11/LKB1, acts as a key regulator of polarization of cortical neurons, probably by mediating phosphorylation of microtubule-associated proteins such as MAPT/TAU at 'Thr-523' and 'Ser-573'. Also regulates neuron polarization by mediating phosphorylation of WEE1 at 'Ser-642' in postmitotic neurons, leading to down-regulate WEE1 activity in polarized neurons. Also acts as a positive regulator of centrosome duplication by mediating phosphorylation of gamma-tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation of gamma-tubulin and its associated proteins to the centrosome. Involved in the UV-induced DNA damage checkpoint response, probably by inhibiting CDK1 activity through phosphorylation and activation of WEE1, and inhibition of CDC25B and CDC25C (By similarity). In neurons, localizes to synaptic vesicles and plays a role in neurotransmitter release, possibly by phosphorylating RIMS1.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Synapse {ECO:0000269|PubMed:16630837}. Presynaptic active zone {ECO:0000269|PubMed:16630837}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:16630837}. Note=Nuclear in the absence of DNA damage. Translocated to the nucleus in response to UV- or MMS-induced DNA damage (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MSSGSKEGGGGSPAYHLPHPHPHPPQHAQYVGPYRLEKTLGKGQTGLVKLGVHCITGQKVAVKIVNREKLSESVLMKVEREIAILKLIEHPHVLKLHDVYENKKYLYLVLEHVSGGELFDYLVKKGRLTPKEARKFFRQIVSALDFCHSYSICHRDLKPENLLLDEKNNIRIADFGMASLQVGDSLLETSCGSPHYACPEVIKGEKYDGRRADMWSCGVILFALLVGALPFDDDNLRQLLEKVKRGVFHMPHFIPPDCQSLLRGMIEVEPEKRLSLEQIQKHPWYLGGKHEPDPCLEPAPGRRVAMRSLPSNGELDPDVLESMASLGCFRDRERLHRELRSEEENQEKMIYYLLLDRKERYPSCEDQDLPPRNDVDPPRKRVDSPMLSRHGKRRPERKSMEVLSITDAGSGGSPVPTRRALEMAQHSQRSRSVSGASTGLSSSPLSSPRSPVFSFSPEPGVGDEARGGGSPTSKTQTLPSRGPRGGGAGEQPPPPSARSTPLPGPPGSPRSSGGTPLHSPLHTPRASPTGTPGTTPPPSPGGGVGGAAWRSRLNSIRNSFLGSPRFHRRKMQVPTAEEMSSLTPESSPELAKRSWFGNFISLDKEEQIFLVLKDKPLSSIKADIVHAFLSIPSLSHSVLSQTSFRAEYKASGGPSVFQKPVRFQVDISSSEGPEPSPRRDGSSGGGIYSVTFTLISGPSRRFKRVVETIQAQLLSTHDQPSVQALADEKNGAQTRPAGTPPRSLQPPPGRPDPDLSSSPRRGPSKDKKLLATNGTPLP
Protein: Tetraspanin-5 (Q84WF6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the regulation of cell differentiation.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- MLO-like protein 8
- Protein HIGH ARSENIC CONTENT 1, mitochondrial
- MLO-like protein 10
- MLO-like protein 15
- MLO-like protein 3
- Succinate dehydrogenase assembly factor 2, mitochondrial
Sequence:
MNRMSNTVIGFLNILTLISSIVLLGSALWMGRSKTTCEHFLQKPLLILGLAILILSVAGLVGACCDVAWVLWVYLFFMVFIIVALMGLTLFGFIVTSHSGGVVVDGRVYKEFKLEAYHPWLKTRVVDTNYWVTIKTCLLGSVTCSKLALWTPLDYLQKDLSPLQSGCCKPPTSCVYNTDTVIQQDPDCYRWNNAATVLCYDCDTCRAGVLETVRRDWHKLSLVNVIVVIFLIAVYCVGCCAFKNAKRPQHYGFPYGRYGMSKSRPGWEQSWSRWWHGRDRY
Protein: Bifocal, isoform B (LP10077p) (Q8IR86)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus membrane {ECO:0000256|ARBA:ARBA00004232}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004232}. Rough endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004269}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004269}.
Interaction partners:
Sequence:
MESQKRPSLDLHTDVPAGLAAGGSGLGAAAEMSPTSGFLPDMPQWKKDLIQRRKTNVARTQAASITSPTDGSCGALAEANAAPGAIADFTEPATISSTSQKRNMIGSEEKSEKSSISNTNSDSTGGHHSVVAVSLSPDAAATTNVTVTPIPKQRSSLLNTRSQEREMVRYILSESGERDGELESGEQPAGVVSNSRCGEVETGTIGSPSSSANQNPNPNHLKTKCKPGQSVAEGKPSAKETIVDNSKSCSKTKSISDKLQSNKFIIQQQQQQQQQQQQQQQLSPTKVTVKPTMVAMQEMKKTTKQNGQHRHLAGKIGSVAGGDVDPQHPPTNPIPDSLDTGEDLSYGPGIVSKLRCRYLSLALRESRQQSSKQRLQRSTSLNTLLDRDDDEVEVEEPEMTNSQVRAKSTPPPILGAKPTPKPSSQHQRPVSLGANGAGSAVNPPSNSDQAQTGAVANGGAGSGQRSRHFKRGNEVMKRARSVEALLCEKSPWNSQRISTAGAAAAAAPSPPAPKATAAAPSPVTSPTCVTIEDKIHNARERLHSGTDTAPPKRLTSIIDDTERPPPDLVKQTLKMFEASANRRPRAAHRSNGVGGVASKVANYKSIIKDQKQPSSAAATPPPTGMGFASSTPLRHVHPDIIPRQVDSPVSALSVMMRRMELQEPETPERETRDAEATPQSEALSETERNDRDEGDGEVDDDNHNNNDDDHDDGDDGSDNNEQRDKMGAAAAGDKPKPPAESAAGGAQRSFAASTENAHVASGSSSSTSASVRKLSNNNDSSSGPAVTKQIGVIRPLFNSQGAGSTPLTSREIEKNRINEMKKSTATDAGGSVSGSGTVAGAGSGTSPTTSLDSVINTKEAASSETDASASPLWTLRKLRNQSQTAGGGSGPSSSLHSTENTSMVFNFSKSTKEVPDYIESDVVIYRRKRELPKPNEPGFVLLGDLSVETSTDTDYDDYSMCPPSPCDVEFENANIVIDGKSSIRQKPKESSFRVQFNDTLTSTFEYPSEASMTIEDPPYADPFGHVSKHHQMLLAEQMHLLQHQEQLELEQMHQLGLAPEQHHHVTVDEIIELPTSTAGHGHGIGLGHRSGAAGGGGTMLGNLPLGSTALGFYTPMKGTAMDNLFQLGVTRYALPESSSSGSSNGSHSPGSNGSSPAGAAGSRLMFNGNGSIMGIGEGLIKEGDLAATEAGPGTADGAGASKKGSAVDEDDYHLTATPGAEVVYSEGTQKTDLLY
Protein: KN motif and ankyrin repeat domain-containing protein 4 (Ankyrin repeat domain-containing protein 38) (Q5T7N3)
Organism: Homo sapiens (Human)
Function: May be involved in the control of cytoskeleton formation by regulating actin polymerization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17996375, ECO:0000269|PubMed:25961457}.
Interaction partners:
- Trafficking protein particle complex subunit 1
- Cytosolic carboxypeptidase 4
- Trafficking protein particle complex subunit 3
- Trafficking protein particle complex subunit 5
Sequence:
MEKTDAKDQSSQGDEEKDPPKSHPYSVETPYGFHLDLDFLKYVDDIEKGNTIKRIPIHRRAKQAKFSTLPRNFSLPDSGARPPAAPPLQNWSPVVPREASLGTQEQNQSPPLGNAPQASTSRSEVSYHRKALLAEATRQLEAAEPEDAELTFGSGRPQLLRASSMPATLLHSRASEEPGLSLGPPAPPALPPLQGEGSVCDGTFEPAEGLAGFHSSSPRASTRIPELVQEGAEPPEGVVKVPNHLPLPGPPFSFQNVLVVLEDKEDEHNAREAEVLFTPGSPTPSPPPLPSPIPENELLLEEIELNISEIPPPPPVEVDMRSIGIRVTEESLGLARVDPGSISSLKQQVSALEGELSGRTEELAQVRTALQQQEEEIKAREQRIRELEFTVAQLEGQFHQENAKDTQGQTDVMVNTDPVHGLLTRESCDKGIEVNLLGSMESESWGHRGEENGLLWGPDGHKQGNQSPAERVLLPQLSLPQGPEQVLTSSVHSFLSTELRIEEAGTEQEGGPQGGTRGAGGFLWGSDRKTPPAGREETSSNLPGKEHPGRPPSSPTDATIGQYVKKIQELLQEQWNCLEHGYPELASAIKQPASKLSSIQSQLLSSLNLLLSAYSAQAHPPKEPPASSSSPPVEISPSTSLKSIMKKKDYGFRAGGNGTKKNLQFVGVNGGYETTSSEETSGEDSTPEDLSDSEAEKKCDGPDHKHVKDAHLTCEAGQGIPEGTCHAAQESGPGEEVPHSKAERYKPSEEFLNACRALSQHLPETGTTTDQLLRQSLNTISQEWFRVSSRKSSSPAVVASYLHEVQPHSPHFLKLLVNLADHNGNTALHYSVSHSNFSIVKLLLETGVCNVDHQNKAGYTAVMITPLASAETNEDMAVVWKLLREGNVNIQATQGGQTALMLGVSHDREDMVQALLSCQADVNLQDHDGSSALMVACHHGNVDLVRLLLAHPACDSSLTDKAGRTALSIALKSPTHMEIAGLLRAHAEQGRSLGL
Protein: LD25919p (Q961A5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLKKTTDERAVKEREEQIEAAKQELEQAQFAEQAVSSQIEEIQNQYDTLRNESVKPVEAKIKKVNSQIEKLAANVRSLNVGLATADRNITKITGNNNNLRENIKAAEEKLKSLNEDRNKAKEKKEELEKEIEESEASIEGAKSQSSDIKKEIDEITKEENKRNIERIEIDTKLQAAAGKMNKVKNDIPGWQAQLAPLKLNEIPGETEPQAPLKELNEEELEAETLEALQYKQTMLEEDLKTKKPNLSCIKEFNEKRLVYLDRVRVLEDITSKRNEMRDKYEEVRKRRYKEFMDGFSIITRKLKEMYQMITLGGDAELELVDSMDPFTEGVNFTVRPPKKSWKYISNLSGGEKTLSSLALVFALHYYKPSPLYFMDEIDAALDFKNVSIVGHYIKERTKNAQFIIVSLRVNMFELANFLVGIYKVSDCTDSITMLNYPPTLPTQSPVVANSQYVGGTIEGDNTIAAENQDDTPTKKSQSPPSEQIVRLISELGRDTTFAPPLESTVRDTILAQNLKQAATEVAAQPSDATGRVTTDVSLASPPSSPAILNV
Protein: GATA-type sexual development transcription factor NsdD (Q4WYQ4)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Camp independent regulatory protein
- COP9 subunit 3, putative
- C6 transcription factor, putative
- C6 finger domain transcription factor nosA
- C2H2 zinc finger protein
- C2H2 type master regulator of conidiophore development brlA
Sequence:
MGSLEATHRQRDHLPTISFFTKDGSGYTSRNSTVSSPTPLVSPTTMYPSQPSPYSYQPSAASAPPQPGYISPPESRRALEEEKEKQLQPQRQSLPSIHEALRNDSPLPYPAPPTSGPLPQAHPHPPHALVGRSAGDGPAGPPNPFSNGAPAGPYMREPAYSQLQTEASRSSLASITTQESRNPSLQSLNSSKSPTHSAKTGLTSIAGSQTGSGYEYSAPTSAGSIASPNGYTAYSQPFTFQSQPPPNAPTYPLAHHDTRPYAATPWKPGAPEPPRVEELKNGLAGRPAVPVQPQGDSAKRHLDIYEVETSLNEIVEVSTRTLDFSRHYATRAHQTQRSGPMLGTLPPLHEIEDMINLQRRNQDALMRLRTAVLNQEHALAEQMAQRKAFSAGGVHDSDHMAMYQEEFKGSGGFAGPDTKKRRGKAAPPGRCHSCNRAETPEWRRGPDGARTLCNACGLHYAKLTRKMGASKAASLGSNLKPKAALDPTPPGTR
Protein: Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A (EC 3.1.3.36) (Inositol polyphosphate 5-phosphatase J) (Phosphatidylinositol 1,3,4,5-tetrakisphosphate 5-phosphatase) (EC 3.1.3.56) (Phosphatidylinositol 1,4,5-trisphosphate 5-phosphatase) (EC 3.1.3.56) (Q15735)
Organism: Homo sapiens (Human)
Function: Inositol 5-phosphatase, which converts inositol 1,4,5-trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate-binding proteins that are present at membranes ruffles.
Subcellular location: Cytoplasm {ECO:0000250}. Note=Predominantly localized to membrane ruffles. {ECO:0000250}.
Interaction partners:
- Inositol polyphosphate-5-phosphatase A
- Inositol polyphosphate 1-phosphatase
- Inositol-tetrakisphosphate 1-kinase
- Inositol-trisphosphate 3-kinase B
- Inositol polyphosphate multikinase
- Inositol-trisphosphate 3-kinase A
- Inositol-trisphosphate 3-kinase C
- Multiple inositol polyphosphate phosphatase 1
- Inositol polyphosphate 5-phosphatase K
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
Sequence:
MEGQSSRGSRRPGTRAGLGSLPMPQGVAQTGAPSKVDSSFQLPAKKNAALGPSEPRLALAPVGPRAAMSASSEGPRLALASPRPILAPLCTPEGQKTATAHRSSSLAPTSVGQLVMSASAGPKPPPATTGSVLAPTSLGLVMPASAGPRSPPVTLGPNLAPTSRDQKQEPPASVGPKPTLAASGLSLALASEEQPPELPSTPSPVPSPVLSPTQEQALAPASTASGAASVGQTSARKRDAPAPRPLPASEGHLQPPAQTSGPTGSPPCIQTSPDPRLSPSFRARPEALHSSPEDPVLPRPPQTLPLDVGQGPSEPGTHSPGLLSPTFRPGAPSGQTVPPPLPKPPRSPSRSPSHSPNRSPCVPPAPDMALPRLGTQSTGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPTWKSDPGFRITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGADMIAIGLQEVNSMLNKRLKDALFTDQWSELFMDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNKGGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAQGILDHDLVFWFGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKFDVGTNKYDTSAKKRKPAWTDRILWKVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSDHKPVAAQFLLQFAFRDDMPLVRLEVADEWVRPEQAVVRYRMETVFARSSWDWIGLYRVGFRHCKDYVAYVWAKHEDVDGNTYQVTFSEESLPKGHGDFILGYYSHNHSILIGITEPFQISLPSSELASSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPGLALRPSSRERRGASRSPSPQSRRLSRVAPDRSSNGSSRGSSEEGPSGLPGPWAFPPAVPRSLGLLPALRLETVDPGGGGSWGPDREALAPNSLSPSPQGHRGLEEGGLGP
Protein: Atrial natriuretic peptide receptor 1 (EC 4.6.1.2) (Atrial natriuretic peptide receptor type A) (ANP-A) (ANPR-A) (NPR-A) (Guanylate cyclase A) (GC-A) (P18910)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand.
Subcellular location: Membrane {ECO:0000269|PubMed:2563900}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Natriuretic peptides A
- Natriuretic peptides B
- C-type natriuretic peptide
- Atrial natriuretic peptide receptor 2
- Pro-opiomelanocortin
- VIP peptides
- Pro-glucagon
- Pituitary adenylate cyclase-activating polypeptide
- Inosine triphosphate pyrophosphatase
- Neuroendocrine secretory protein 55
Sequence:
MPGSRRVRPRLRALLLLPPLLLLRGGHASDLTVAVVLPLTNTSYPWSWARVGPAVELALARVKARPDLLPGWTVRMVLGSSENAAGVCSDTAAPLAAVDLKWEHSPAVFLGPGCVYSAAPVGRFTAHWRVPLLTAGAPALGIGVKDEYALTTRTGPSHVKLGDFVTALHRRLGWEHQALVLYADRLGDDRPCFFIVEGLYMRVRERLNITVNHQEFVEGDPDHYPKLLRAVRRKGRVIYICSSPDAFRNLMLLALNAGLTGEDYVFFHLDVFGQSLKSAQGLVPQKPWERGDGQDRSARQAFQAAKIITYKEPDNPEYLEFLKQLKLLADKKFNFTVEDGLKNIIPASFHDGLLLYVQAVTETLAQGGTVTDGENITQRMWNRSFQGVTGYLKIDRNGDRDTDFSLWDMDPETGAFRVVLNYNGTSQELMAVSEHKLYWPLGYPPPDVPKCGFDNEDPACNQDHFSTLEVLALVGSLSLISFLIVSFFIYRKMQLEKELVSELWRVRWEDLQPSSLERHLRSAGSRLTLSGRGSNYGSLLTTEGQFQVFAKTAYYKGNLVAVKRVNRKRIELTRKVLFELKHMRDVQNEHLTRFVGACTDPPNICILTEYCPRGSLQDILENESITLDWMFRYSLTNDIVKGMLFLHNGAICSHGNLKSSNCVVDGRFVLKITDYGLESFRDPEPEQGHTLFAKKLWTAPELLRMASPPARGSQAGDVYSFGIILQEIALRSGVFYVEGLDLSPKEIIERVTRGEQPPFRPSMDLQSHLEELGQLMQRCWAEDPQERPPFQQIRLALRKFNKENSSNILDNLLSRMEQYANNLEELVEERTQAYLEEKRKAEALLYQILPHSVAEQLKRGETVQAEAFDSVTIYFSDIVGFTALSAESTPMQVVTLLNDLYTCFDAVIDNFDVYKVETIGDAYMVVSGLPVRNGQLHAREVARMALALLDAVRSFRIRHRPQEQLRLRIGIHTGPVCAGVVGLKMPRYCLFGDTVNTASRMESNGEALKIHLSSETKAVLEEFDGFELELRGDVEMKGKGKVRTYWLLGERGCSTRG
Protein: Unc-13 homolog D (K7EMK8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATLLSHPQQRPPFLRQAIKIRRRRVRDLQDPPPQMAPETGTTEWFHLKQQHHQPMVQGIPEAGKALLGLVQDVIGDLHQCQRTWDKIFHNTLKIHLFSMAFRELQWLVAKRVQDHTTVVGDVVSPEMGESLFQLYISLKELCQLRMSSSERDGVLALDNFHRWFQPAIPSWLQKTYNEALARVQRAV