wanglab/gogpt-training-data huggingface dataset:
Protein: Tetrahydroberberine oxidase (THB oxidase) (EC 1.3.3.8) ((S)-tetrahydroprotoberberine oxidase) (BwSTOX) (F1BVB6)
Organism: Berberis wilsoniae (Mrs Wilson's barberry)
Function: Catalyzes the oxidation of different tetrahydroprotoberberines, such as (S)-canadine, (S)-scoulerine and (S)-corypalmine. Catalyzes the oxidation of (S)-coreximine and (S)-tetrahydropalmatine. Catalyzes the oxidation of different 1-benzylisoquinoline alkaloids, such as (S)-norreticuline, (S)-nororientaline, (S)-coclaurine and (S)-norisoorientaline. Exhibits strict specificity for the (S)-enantiomer of tetrahydroprotoberbirines and 1-benzylisoquinoline alkaloids.
Interaction partners:
Sequence:
MSKMASSIFATFSLLSSLLPTSLASSDANYEDFLQCLDLYSQNSIPVYTRNTSSYTSILESTIKNLVFLSPTTPKPNFIVTPMQESHVQTSVICCRMHGLQMRIRSGGHDFEGLSYVSNVPFVVLDLIHLKTINVDIEENSAWVQTGATIGELYYRIAEKVGVHAFPAGLCPTVGVGGHISGAGYGVLMRKYGVSADHVIDARIVNVDGEILDRESMGEDLFWAIRGGGGASFGVILAWKIRLVPVPPTVTIFIVPKTLEEGATALLHKWQFIGDNVHEDLFIGLSMRSVIISPKGDKTILVSFIGLFLGGSDKLVQHMEQSFPELGVKPHDCIEMSWIKSTVVFGVFSNDASLSVLLDRKNPFPPKSYHKVKSDYVTEPLPISVLEGICHRFLKNGVNKAEIIMSPYGGRMNEISESEIAFPHRKGNLYKINYIAEWEEAGSMENHLSWIRELYRYMTPYVSKSPRSSYLNFKDIDLGQTKNGTATYSQAKAWGSKYFKNNFKRLMQVKTKVDPNNFFCNEQGIPPFSS
Protein: Extracellular sulfatase Sulf-2 (mSulf-2) (Arylsulfatase) (EC 3.1.6.1) (N-acetylglucosamine-6-sulfatase) (EC 3.1.6.14) [Cleaved into: Extracellular sulfatase Sulf-2 secreted form] (Q8CFG0)
Organism: Mus musculus (Mouse)
Function: Exhibits arylsulfatase activity and highly specific endoglucosamine-6-sulfatase activity. It can remove sulfate from the C-6 position of glucosamine within specific subregions of intact heparin (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8VI60}. Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:Q8VI60}. Cell surface {ECO:0000269|PubMed:12368295}.; SUBCELLULAR LOCATION: [Extracellular sulfatase Sulf-2 secreted form]: Secreted {ECO:0000269|PubMed:12368295}.
Interaction partners:
- Glypican-3
- Heparan sulfate 2-O-sulfotransferase 1
Sequence:
MAPPGLPLWLLSTALLSLLAGSSAFLSHPRLKGRFQRDRRNIRPNIILVLTDDQDVELGSMQVMNKTRRIMEQGGAHFINAFVTTPMCCPSRSSILTGKYVHNHNTYTNNENCSSPSWQAQHESRTFAVYLNSTGYRTAFFGKYLNEYNGSYVPPGWKEWVGLLKNSRFYNYTLCRNGVKEKHGSDYSTDYLTDLITNDSVSFFRTSKKMYPHRPVLMVISHAAPHGPEDSAPQYSRLFPNASQHITPSYNYAPNPDKHWIMRYTGPMKPIHMEFTNMLQRKRLQTLMSVDDSMETIYDMLVETGELDNTYILYTADHGYHIGQFGLVKGKSMPYEFDIRVPFYVRGPNVEAGSLNPHIVLNIDLAPTILDIAGLDIPADMDGKSILKLLDSERPVNRFHLKKKLRVWRDSFLVERGKLLHKREGDKVNAQEENFLPKYQRVKDLCQRAEYQTACEQLGQKWQCVEDASGTLKLHKCKGPMRFGGGGGSRALSNLVPKYDGQSSEACSCDSGGGGDYKLGLAGRRKLFKKKYKTSYARNRSIRSVAIEVDGEIYHVGLDTVPQPRNLSKPHWPGAPEDQDDKDGGSFSGTGGLPDYSAPNPIKVTHRCYILENDTVQCDLDLYKSLQAWKDHKLHIDHEIETLQNKIKNLREVRGHLKKKRPEECDCHRISYHSQHKGRLKHKGSSLHPFRKGLQEKDKVWLLREQKRKKKLRKLLKRLQNNDTCSMPGLTCFTHDNHHWQTAPLWTLGPFCACTSANNNTYWCLRTINETHNFLFCEFATGFIEYFDLSTDPYQLMNAVNTLDRDVLNQLHVQLMELRSCKGYKQCNPRTRNMDLGLRDGGSYEQYRQFQRRKWPEMKRPSSKSLGQLWEGWEG
Protein: E3 ubiquitin-protein ligase TRIM11 (EC 2.3.2.27) (Tripartite motif-containing protein 11) (Q99PQ2)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18628401}. Nucleus {ECO:0000269|PubMed:18628401}. Note=In the nucleus, colocalizes with PAX6. {ECO:0000269|PubMed:18628401}.
Interaction partners:
- Interferon-inducible protein AIM2
- Ubiquitin-conjugating enzyme E2 N
Sequence:
MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSAQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCAAHREPLTTFCGDDLSLLCPICERSEHWTHRVRPLQEAADDLKGRLEKSLEHLRKQMEDAMLFQAQAEETCALWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQKLEEEELEVLPRLREGAARLGQQSTQLAALISELESRCQLPALGLLQDIKDALCRVQDVKLQPPAVVPMELRTVCRVPGLVETLRRFRGDITLDPDTANPELVLSEDRRSVQRGEQRQALPDNPERFDPGPCVLGQERITSGRHYWEVEVGDQTSWALGVCKETANRKEKGELSAGNGFWILVFLGSFYNSNEPAFSPLRDPPKRVGIFLDYEAGHLSFYSATDGSLLFIFPETLFSGTLRPLFSPLSSSPTPMTICRLIGVSGDTLGPQ
Protein: PX domain-containing protein EREL2 (Protein EREX-like 2) (Q8S8D3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as an effector of RABF2A and RABF2B (By similarity). Involved in vacuolar transport of storage proteins. Regulates membrane trafficking to protein storage vacuoles (PSVs) (Probable). Binds specifically to phosphatidylinositol 3-monophosphate (PtdIns3P) (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:27288222}. Endosome membrane {ECO:0000269|PubMed:27288222}; Peripheral membrane protein {ECO:0000305}. Note=The endosomal localization depends on the active state of RABF2B. {ECO:0000269|PubMed:27288222}.
Interaction partners:
- WD40 repeat-containing protein HOS15
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 10
- Transcription and mRNA export factor ENY2
- Ubiquitin C-terminal hydrolase 22
- Transcription initiation factor TFIID subunit 5
- Probable cytosolic iron-sulfur protein assembly protein CIAO1 homolog
- Transcription initiation factor TFIID subunit 12b
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 6b
Sequence:
MQRRSPPKHRHDGASPLPLGMDWSPPPRNWNGRDTIWPHDFRTGWSYCVTIPSWTLLSKSKNSDPIVFYRVQVSVQSPEGVSTMRGILRRFNDFVKLLADLKRAFPRKSFPSAPPKGFLRVKSRDMLEERRCSLEDWMTKLLSDIELARSVVVASFLELEATARSACQVVDQNASDSNDDGNSTSLSSLVHPNSGGSSLLSSDYGSDTAYETSELGSASLGQDDVSETDTGDLTLDEDLTNPTEKLVKFSMSNIDEGLSMSQTIIEQLEDFPKHRVHLGYANDITETNSYNGKASKGVFRANNDLRCRSESETSHSVMHDRKLSLESADGVSLLAGETSTSSILSSIVHSQLDVNHDISVGNLEIPGNGRIVLPLKMHSKLNRILLTMNERLLNSKTDMEDLIARLNQETAVKEYLNRKVDDLEVELETTKQRNKENLEQALMTERQSVTKMQWDMEELRQKTFEMELKLKSKEDGSSDSKTSGNSTISESHELLQEMDATKQQLEDLSRRYVELEAKSKADIKVLVREVKSLRRSHMEMEKELTRSLTEKSDTEKLLQQERIIVENTLEARRRLYSDCEILHDRLKVNNTNLSMDESSNNREDLSEVSNALQDQIEAQLLLGFDETASEDELRKIMADMYED
Protein: 4-hydroxycoumarin synthase 2 (EC 2.3.1.208) (Biphenyl synthase 3) (SaBIS3) (D2DRC5)
Organism: Sorbus aucuparia (European mountain ash) (Rowan)
Function: Type III polyketide synthase involved preferentially in the biosynthesis of 4-hydroxycoumarin from salicoyl-CoA. Can also use benzoyl-CoA and malonyl-CoA to produce 3,5-dihydroxybiphenyl as a major product and benzoyldiacetic acid lactone as a minor side product. Can also use m-hydroxybenzoyl-CoA as substrate, producing m-hydroxybenzoyl diacetic acid lactone as a derailment product. No activity with p-hydroxybenzoyl-CoA, CoA-linked cinnamic acids or acetyl-CoA.
Interaction partners:
Sequence:
MAPVVKNEPQHAKILAIGTANPPNVFHQKDYPDFLFRVTKNEHRTDLREKFDRICEKSRTKKRYLHLTEEMLKANPNIYTYGAPSLNVRQDICNIEVPKLGQEASLKAIKEWGQPISKITHLIFCTASCVDMPGCDFQLIKLLGLDPSVTRTMIYEAGCYAGATVLRMAKDFAENNKGARVLVVCAEITTVFFHGLTDTHLDILVGQALFADGASAVIVGANPEPEIERPLFEIVACRQTILPNSEHGVVANIREMGFNYYLSGDVPKFVGGNVVDFMTKTFEKVDGKNKDWNSLFFSVHPGGPAIVDQVEEKLGLKEGKLRATRHVLSEYGNMGAPTVHFILDEMRNKSIEEGKTTTGEGLEWGVVIGIGPGLTVETAVLRSEFITY
Protein: SNAP receptor (A0A1D8PNI0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Synaptobrevin homolog YKT6
- Protein transport protein SEC22
- Vam7p
- Tethering complex ATP-binding subunit
- SNAP receptor
- Golgi SNAP receptor complex member 1
- V-SNARE protein
- Syntaxin
- Uncharacterized protein
- Probable vacuolar protein sorting-associated protein 16 homolog
Sequence:
MSFNTPFSEDLERTATNDSHRYKDYPEFDSLSTSIEKQLHYINSELLSSIRSDLAKFEKDKTDTSLSESLSGQFRKTTDAFKKVNKFVKSLNASIVTTEREHEDVETINYLKQKEAIQIKLIRDSLANFNNFQKRFELCQTTQLPEDGTNLSETEPGSIQQSQQQVQITYEPINAEELEQQTLLIQEREREIHQIQQDTQEINDIFSNLSSIVNEQQFQIDSIENNIFSYSSNAREASNELRRAERYQKRSSGRLLCCFMILVAIASFIILIGLIF
Protein: WASH complex subunit 5 (WASH complex subunit strumpellin) (A0A8I6AFP0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLDFLAENNLCGQAILRIVSCGNAIIAEVLRLSEFIPAVFLLKDRADQQRYGDIIFDFSYFKGPEFWESKLEARPELQDLDEEFRENNIEIVTRFYLAFQSVHKYIVDLNRYLDDLNEGVYIQQTLETVLLNEDGKQLLCEALYLYGVMLLVIDQKIEGEVRERMLVSYYRYSAARSSADSNLDDICKLLRSTGYSSQPGAKRPPSYPESYFQRVPINPTFISMAIGRLRSDDIYNQVSAYPLPEHRSTALANQAAMLYVILYFEPSILHTHQAKMREIVDKYFPDNWVISIYMGITVNLADAWEPYKAAKTALNNTLDLPNVKEQASRYASVSERVRAQVQQFLKEGYLREEVLLDNIPRLLNCLRDCNVAIRWLMLHTADSACDPNNKRLRQIKDQILADSRYNPKILFQLLLDTAQFEFILKEMFKQMLSEKQSKWEHYKKEGSERMIELADVFSGVKPLTRVEKNENLQAWFREISKQILSLNYDDSTAAGRKTVQLIQALEEVQEFHQLESNLQVCQFLADTRKFLHQMIRTINIKEEVLITMQIVGDLSFAWQLIDSFTSIMQESIRVNPSMVTKLRATFLKLASALDLPLLRINQANSPDLLSVSQYYSGELVSYVRKVLQIIPESMFTSLLKIIKLQTHDIIEVPTRLDKDKLRDYAQLGPRYEVAKLTHAISIFTEGILMMKTTLVGIIKVDPKQLLEDGIRKELVKRVAFALHRGLIFNPRAKPSELMPKLKELGATMDGFHRSFEYIQDYVNIYGLKIWQEEVSRIINYNVEQECNNFLRTKIQDWQSIYQSTHIPIPKFAPVDESITFIGRLCREILRITDPKVTCYIDQLNTWYDMKTRQEVTSSRLFSEIQTTLGTFGLNGLDRLLCFMIVKELQNFLSMFQKIILRERTVQETLKTLMNAVSPLRSIVANSSKVYLAAITKTQKIWSTYLEAIMKVGQMQILRRQIANELNSSCRFDSRHLAAALDNLNKALLADIEAHYRDPSLPYPKEDNTLLYEITAYLEAAGIHNPLNKIYITTKRLPYFPIVNFLFLIAQLPKLQYNKNLGMVCRKPADPVDWPPLVLGLLTLLKQFHSRYTEQFLALIGQFIRSTMEQCTSQKMPEMPADAVGALLFLEDYVRYTKLPRRVMEHITNLRIKQNLICLLSM
Protein: Uncharacterized protein (Q3TM01)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKGATSKSNHCLILSLFILLSYLGTTLADGTDSLSCELTFNYRNLHGQCSVNGKTLLDFGDKKHEENATKMCADLSQNLTEISEEMWKLQSGNDTLNVTTQSQYNQGKFIDGFWAINTDEQHSIYFYPLNMTWRESHSDNSSAMEQWKNKNLEKDMRNVLITYFSHCLNKSSSHFREMPKSTLKVPDTTQRTNATQIHPTVNNFRHNSDNQGLSVTWIVIICIGGLVSFMAFMVFAWCMLKKKKKGAPCCSSSSAVLITSYNHVTLQHIPVASPAKETYF
Protein: ATPase MORC2 (EC 3.6.1.-) (MORC family CW-type zinc finger protein 2) (Zinc finger CW-type coiled-coil domain protein 1) (Q9Y6X9)
Organism: Homo sapiens (Human)
Function: Essential for epigenetic silencing by the HUSH (human silencing hub) complex. Recruited by HUSH to target site in heterochromatin, the ATPase activity and homodimerization are critical for HUSH-mediated silencing. Represses germ cell-related genes and L1 retrotransposons in collaboration with SETDB1 and the HUSH complex, the silencing is dependent of repressive epigenetic modifications, such as H3K9me3 mark. Silencing events often occur within introns of transcriptionally active genes, and lead to the down-regulation of host gene expression. During DNA damage response, regulates chromatin remodeling through ATP hydrolysis. Upon DNA damage, is phosphorylated by PAK1, both colocalize to chromatin and induce H2AX expression. ATPase activity is required and dependent of phosphorylation by PAK1 and presence of DNA. Recruits histone deacetylases, such as HDAC4, to promoter regions, causing local histone H3 deacetylation and transcriptional repression of genes such as CA9. Exhibits a cytosolic function in lipogenesis, adipogenic differentiation, and lipid homeostasis by increasing the activity of ACLY, possibly preventing its dephosphorylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:20225202, ECO:0000269|PubMed:23260667, ECO:0000269|PubMed:28581500}. Cytoplasm, cytosol {ECO:0000269|PubMed:20225202, ECO:0000269|PubMed:24286864}. Chromosome {ECO:0000269|PubMed:23260667, ECO:0000269|PubMed:28581500}. Nucleus matrix {ECO:0000269|PubMed:23260667}. Note=Mainly located in the nucleus (PubMed:20225202). Upon phosphorylation at Ser-739, recruited to damaged chromatin (PubMed:23260667). {ECO:0000269|PubMed:20225202, ECO:0000269|PubMed:23260667}.
Interaction partners:
- MORC family CW-type zinc finger protein 1
- RNA cytidine acetyltransferase
- Protein TASOR
- M-phase phosphoprotein 8
Sequence:
MAFTNYSSLNRAQLTFEYLHTNSTTHEFLFGALAELVDNARDADATRIDIYAERREDLRGGFMLCFLDDGAGMDPSDAASVIQFGKSAKRTPESTQIGQYGNGLKSGSMRIGKDFILFTKKEDTMTCLFLSRTFHEEEGIDEVIVPLPTWNARTREPVTDNVEKFAIETELIYKYSPFRTEEEVMTQFMKIPGDSGTLVIIFNLKLMDNGEPELDIISNPRDIQMAETSPEGTKPERRSFRAYAAVLYIDPRMRIFIHGHKVQTKRLSCCLYKPRMYKYTSSRFKTRAEQEVKKAEHVARIAEEKAREAESKARTLEVRLGGDLTRDSRVMLRQVQNRAITLRREADVKKRIKEAKQRALKEPKELNFVFGVNIEHRDLDGMFIYNCSRLIKMYEKVGPQLEGGMACGGVVGVVDVPYLVLEPTHNKQDFADAKEYRHLLRAMGEHLAQYWKDIAIAQRGIIKFWDEFGYLSANWNQPPSSELRYKRRRAMEIPTTIQCDLCLKWRTLPFQLSSVEKDYPDTWVCSMNPDPEQDRCEASEQKQKVPLGTFRKDMKTQEEKQKQLTEKIRQQQEKLEALQKTTPIRSQADLKKLPLEVTTRPSTEEPVRRPQRPRSPPLPAVIRNAPSRPPSLPTPRPASQPRKAPVISSTPKLPALAAREEASTSRLLQPPEAPRKPANTLVKTASRPAPLVQQLSPSLLPNSKSPREVPSPKVIKTPVVKKTESPIKLSPATPSRKRSVAVSDEEEVEEEAERRKERCKRGRFVVKEEKKDSNELSDSAGEEDSADLKRAQKDKGLHVEVRVNREWYTGRVTAVEVGKHVVRWKVKFDYVPTDTTPRDRWVEKGSEDVRLMKPPSPEHQSLDTQQEGGEEEVGPVAQQAIAVAEPSTSECLRIEPDTTALSTNHETIDLLVQILRNCLRYFLPPSFPISKKQLSAMNSDELISFPLKEYFKQYEVGLQNLCNSYQSRADSRAKASEESLRTSERKLRETEEKLQKLRTNIVALLQKVQEDIDINTDDELDAYIEDLITKGD
Protein: Beta-ureidopropionase (EC 3.5.1.6) (Beta-alanine synthase) (N-carbamoyl-beta-alanine amidohydrolase) (Q964D8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes a late step in pyrimidine degradation. Converts N-carbamoyl-beta-alanine (3-ureidopropanoate) into beta-alanine, ammonia and carbon dioxide. Likewise, converts N-carbamoyl-beta-aminoisobutyrate (3-ureidoisobutyrate) into beta-aminoisobutyrate, ammonia and carbon dioxide (By similarity).
Interaction partners:
- Dihydropyrimidinase
- Putative aldehyde dehydrogenase family 7 member A1 homolog
- 4-aminobutyrate aminotransferase
- Aldehyde dehydrogenase
- Dihydropyrimidine dehydrogenase [NADP
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase family 3 comG
- Pantoate--beta-alanine ligase
- Glutamate decarboxylase A
- Glutamate decarboxylase B
Sequence:
MSKQFESVQATLEKYIPAEELSEVKRILYGYNRGHHVKSLPICQEALDLANKNNFEIVASKVEADPEQLRKPRIVRLGIIQNSIGAETTAPIQDQYLAIEAKIEKMIDAAGAMGVNVLCLQETWHMPFAFCTREKYPWVEFAESASTGQSIKFIQRMARKYNMVIISPMLERDDVHASTIHNTAVVVGNNGNIIGKSRKNHIPRTGDFNESTYYMESTLGHPVFETIYGKIAINICYGRHHNLNWLAYGLNGAEIVFNPSATVGELSEPMWGVEARNAAMTNNYFVGSINRVGTEHFPNEFTSGNGKPAHKDFGHFYGSSYFSSPDNCCTPSLSRVSDGLNISEVDLNLCQQVKDKWNFQMTARYELYAKFLTDYINPNYQPNIIKDPSMK
Protein: Amidophosphoribosyltransferase (ATase) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase) (GPAT) (Q06203)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Adenylosuccinate lyase
- Bifunctional purine biosynthesis protein ATIC
- Multifunctional protein CAD
- Phosphoribosylformylglycinamidine synthase
- Ribose-phosphate pyrophosphokinase 2
- Ribose-phosphate pyrophosphokinase 1
- Glutamine synthetase
- Ribose-phosphate pyrophosphokinase 3
Sequence:
MELEELGIREECGVFGCIASGEWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPTFKSHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEAPTAYSLLIMHRDVIYAVRDPYGNRPLCIGRLIPVSDINDKEKKTSETEGWVVSSESCSFLSIGARYYREVLPGEIVEISRHNVQTLDIISRSEGNPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAIEAPVDADLVSTVPESATPAALAYAGKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLVDDSIVRGNTISPIIKLLKESGAKEVHIRVASPPIKYPCFMGINIPTKEELIANKPEFDHLAEYLGANSVVYLSVEGLVSSVQEGIKFKKQKEKKHDIMIQENGNGLECFEKSGHCTACLTGKYPVELEW
Protein: Protein SPMIP2 (Sperm-associated microtubule inner protein 2) (Q96LM5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASVSYQKPTSTTVGKQMIFTGPDYIKDYLPKIHQHTSYVGEQHLALEKTGDLRYLWRPASNRSLPAKYKHEYVSEIGWRIPQYNFINKSRLGSGFHIKYEELSQASLDSITHRYQNPWQPKPHVLDMQGKQSRASFAWHMSAFEDTDQRNSKWAILVRQCKSSLPRASKPPKLPKLPKKEKKRKH
Protein: Phytanoyl-CoA hydroxylase-interacting protein-like (Q8BGT8)
Organism: Mus musculus (Mouse)
Function: May play a role in the development of the central system.
Interaction partners:
Sequence:
MEVPRLDHALSSPSSPCEEIKNLSLEAIQLCDRDGNKSQDSGIAEMEELPVPHNIKINNITCDSFKISWDMDSKSKDRITHYFIDLNKKENKNSNKFKHKDVPTKLVAKAVPLPMTVRGHWFLSPRTEYTVAVQTASKQVDGDYVVSEWSEIIEFCTADYSKVHLTQLLEKADVIAGRMLKFSVFYRNQHKEYFDYVREHYGNAMQPSIKDNSGSHGSPISGKLEGIFFSCSTEFNTGKPPQDSPYGRYRFEIAAEKLFNPNTNLYFGDFYCMYTAYHYVILVIAPVGSPGDEFCKQRLPQLNSKDNNFLTCTEEDGVLVYHHAQDVILEVIYTDPVALSLGTVAEITGHQLMSLSTANAKKDPSCKTCNISVGR
Protein: Innexin-3 (Protein opu-3) (Q19746)
Organism: Caenorhabditis elegans
Function: Structural component of gap junctions. Plays a role in maintaining gap junction activity to promote phayngeal muscle contraction.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000269|PubMed:33238150}. Note=Partially co-localizes with F-actin at gap junctions between EA and EP endodermal precursor cells in embryos. {ECO:0000269|PubMed:33238150}.
Interaction partners:
- Innexin-2
- Anion exchange protein
Sequence:
MLGVPFIDRWLSETFKPKTFDDAVDRLSYVTTATLLAFFSIMVSCKQYVGSAIQCWMPMEFKGGWEQYAEDYCFIQNTFFIPERSEIPGDVEDRQKAEIGYYQWVPIVLAIQAFMFYLPSWIWSSLYKQCGLDFPSVISEAEALRSQDSETRTKGVNKLVDFIGDILDTRSKNEYGRFYCYRFGKGLGSMTSMLYICIKLMYLANVFVQFIILNKFLGNETFLWGFHTFADLYAGREWQDSGVFPRVTLCDFSVRKLANVHRYTVQCVLMINMFNEKIYLFIWFWFVFVLITTFINTLCTIYRLSFDSSRHNYIRSLLSGPVNNFKDEKAMIASFANNGLKQDGVLLMRFIDDHAGAMVTKEICEELFKKHGENLQHNRDFHHGHSTKSTSPGLEEGHHEHLYTPEKMKLMAPDYPIKHA
Protein: Interleukin 15 receptor subunit alpha (A0A8I6ADB7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MASPQLRGCGVHALPMLLPLLLLLLLLLPLRVTPGITCPTPISIEHADIRVKNYSVNSRERYVCNSGFKRKAGTSTLTECVINKNTNVAHWTTPNLKCIKISPHSSEMTKVAIPTSVLLVAAGIGLVFLTRYIKSRQASQPRRVEVETMETVPMTVRARSKEDEDHTTSETQGDQPTRGV
Protein: Transcriptional regulator CysB (G3XCU6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
Sequence:
MKLQQLRYIWEVAHHDLNVSATAQSLYTSQPGISKQIRLLEDELGVEVFARSGKHLTRVTPAGERIIHTAGEILRKVESIKQIAQEFSNEKKGTLSIATTHTQARYALPNVISGFIKQYPDVSLHMHQGTPMQIAEMAADGTVDFAIATEALELFGDLIMMPCYRWNRCVIVPHGHPLTKLPKLTLEALAEQPIVTYVFGFTGRSKLDEAFSQRGLVPKVVFTAADADVIKTYVRLGLGVGIVAHMAVDPKLDNDLVILDASHLFESSVTKIGFRRGTFLRGFMCDFIEKFAPHLTRELLAKAVQCHNKAELDELFDGIELPVY
Protein: Proteinase inhibitor PSI-1.2 (P83241)
Organism: Capsicum annuum (Capsicum pepper)
Function: Potent inhibitor of trypsin and a weaker inhibitor of chymotrypsin. It does not inhibit elastase and subtilisin DY.
Interaction partners:
Sequence:
KACPRNCDTDIAYMVCPSSGERIIRKVCTNCCAAQKGCKLFRSNGSIKCTGT
Protein: 40S ribosomal protein S5, putative (Q385D9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Large ribosomal subunit protein bL21m
- Elongation initiation factor 2 alpha subunit, putative
- 40S ribosomal protein S27, putative
- Small ribosomal subunit protein mS29
- 40S ribosomal protein S15, putative
- Small ribosomal subunit protein uS4
- 60S ribosomal subunit protein L31, putative
- Ribosomal protein L37
- 50S ribosomal protein L13, putative
- 60S ribosomal protein L35A, putative
Sequence:
MSAKAPKLFNKWSYENLQTTEIALNDYITRTPTYVPHSAGRWQKKRFRKARIPIVERLTNGLMFKGRGNGKKLQAVRLVRHTLEIIHLLTDQNPIQVVIDAVSKGAPREDSTRVGAGGVVRRQAVDVSPMRRVNEAIYLMCKGAREAAFRNLKTLPECLADEIVNASKGSSNSYAIKKKDEVERVAKANR
Protein: Neurotrophic factor BDNF precursor form (proBDNF) (Brain-derived neurotrophic factor) [Cleaved into: Neurotrophic factor BDNF] (P21237)
Organism: Mus musculus (Mouse)
Function: Important signaling molecule that activates signaling cascades downstream of NTRK2. During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P23560}.; SUBCELLULAR LOCATION: [Neurotrophic factor BDNF precursor form]: Secreted {ECO:0000250|UniProtKB:P23560}. Note=A proportion of BDNF is secreted as immature precursor (proBDNF). {ECO:0000250|UniProtKB:P23560}.
Interaction partners:
- High affinity nerve growth factor receptor
- BDNF/NT-3 growth factors receptor
- Tumor necrosis factor receptor superfamily member 16
- NT-3 growth factor receptor
- Sortilin
- Neurotrophin-4
- Glial cell line-derived neurotrophic factor
- Beta-nerve growth factor
- Neurotrophin-3
- Ciliary neurotrophic factor
Sequence:
MTILFLTMVISYFGCMKAAPMKEVNVHGQGNLAYPGVRTHGTLESVNGPRAGSRGLTTTSLADTFEHVIEELLDEDQKVRPNEENHKDADLYTSRVMLSSQVPLEPPLLFLLEEYKNYLDAANMSMRVRRHSDPARRGELSVCDSISEWVTAADKKTAVDMSGGTVTVLEKVPVSKGQLKQYFYETKCNPMGYTKEGCRGIDKRHWNSQCRTTQSYVRALTMDSKKRIGWRFIRIDTSCVCTLTIKRGR
Protein: Catenin delta 1 (A0A669KB62)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
MDDSEVESTASILASVKEQEAQFEKLTRALEEERRHVSAQLERVRVSPQDANPLMANGTLTRRHQDHSHLLYSTIPRMQEPGQIVETYTEEDPEGAMSVVSVETSDDGTTRRTETTVKKVVKTVTTRTVQPVAMGPDGLPVDASSVSNNYIQTLGRDFRKNGNGGPGPYVGQAGTATLPRNFHYPPDGYSRHYEDGYPGGSDNYGSLSRVTRIEERYRPSMEGYRAPSRQDVYGPQPQVRVGGSSVDLHRFHPEPYGLEDDQRSMGYDDLDYGMMSDYGTARRTGTPSDPRRRLRSYEDMIGEEVPSDQYYWAPLAQHERGSLASLDSLRKGGPPPPNWRQPELPEVIAMLGFRLDAVKSNAAAYLQHLCYRNDKVKTDVRKLKGIPVLVGLLDHPKKEVHLGACGALKNISFGRDQDNKIAIKNCDGVPALVRLLRKARDMDLTEVITGTLWNLSSHDSIKMEIVDHALHALTDEVIIPHSGWEREPNEDCKPRHIEWESVLTNTAGCLRNVSSERSEARRKLRECDGLVDALIFIVQAEIGQKDSDSKLVENCVCLLRNLSYQVHREIPQAERYQEAAPNVANNTGPHAASCFGAKKGKGKKPIEDPANDTVDFPKRTSPARGYELLFQPEVVRIYISLLKESKTPAILEASAGAIQNLCAGRWTYGRYIRSALRQEKALSAIADLLTNEHERVVKAASGALRNLAVDARNKELIGKHAIPNLVKNLPGGQQNSSWNFSEDTVISILNTINEVIAENLEAAKKLRETQGIEKLVLINKSGNRSEKEVRAAALVLQTIWGYKELRKPLEKEGWKKSDFQVNLNNASRSQSSHSYDDSTLPLIDRNQKSDNNYSTPNERGDHNRTLDRSGDLGDMEPLKGTTPLMQKI