wanglab/gogpt-training-data huggingface dataset:
Protein: Proton-gated ion channel subunit pbo-5 (PBoc defective protein pbo-5) (G5ECT0)
Organism: Caenorhabditis elegans
Function: Forms a proton-gated ion channel with pbo-6 that is activated by acidification of the posterior coelomic space, leading to posterior body wall muscle contraction (pBoc) during the defecation cycle. Probably by regulating the defecation motor program, required for fatty acid uptake by intestinal cells. Does not bind neurotransmitters such as acetylcholine, gamma-aminobutyric acid, glycine, serotonin, glutamate or choline.
Subcellular location: Membrane {ECO:0000269|PubMed:18191228}; Multi-pass membrane protein {ECO:0000269|PubMed:18191228}.
Interaction partners:
- Na
- EF-hand domain-containing protein
- Ligand-Gated ion Channel
- Gamma-aminobutyric acid receptor exp-1
Sequence:
MTRLSILQHLLTFLILSKINATSTTESYFDSSEEAPNVLLNHLNNESEGEELTQINDTQPAFVPGSSKRLTEYLLSRHNLNAPPDGLLYVEYELELVHILGIDELKQTMTVLIYVDEHWVDPSLTWDPALFGGITKTWIPLDKIWVPDIIVFNMVKSNRLAHEDLLSAVRAPARIHYNGTIVASHPAVHTVSCEINIRHFPLDDQRCAIEIASWAYGQEKIRLHAHTDHSLEHYKRNEEWHLLNLNVSEEKYEHEGVEVSEVKFEISLKRRPLFYMVTLTFPSYIMCAISVVGLFARFSTTGEREERFTLGVTAILTMAVLSLVVSEKVPHSSTHVPLLVAYFLFNMVIVSIAAMTTGIVMKVHRLGRYGDEPSDFWMRCFLLKPVFRTSNRRKYRMNPEEPTQVILVSEAKNGEVLTKKSTELNGTVVKEIMLSSRLEALEEYIRKMVNRCETIKWELDEIDAAENIELVRRRSTNGYVRISERLDILFMFLFLSTVTIPVAVLFYLT
Protein: Protein BNI4 (P53858)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Chitin synthase regulator SKT5
- Chitin synthase 3
- Serine/threonine-protein phosphatase PP1-2
- Cell division control protein 10
- Cell division control protein 12
- Chitin synthase 2
- Chitin synthase 1
- Seventh homolog of septin 1
- Cell division control protein 11
- Cell division control protein 3
Sequence:
MSDSISDSKSSELLNSTFYSSTSINTLDHARTFRNSLILKEISDQSLNSSIKPCESVLDRDVESSVLQRSFGESNARDSEVQTVNMTTSPSLSALADILNERSKYADQKTRKAQNIESSIIEEEEEAEEQNNSINYHEDITGSRLSVREEANENLAMTSPNLIDIDGSNSIQVAPLSLPSFEEPDFLSTPRVKPDSQGPRSKVSTRRTILERDNNLPVKREENTIINSETESTTHSAPFLKEDPKPSPPSSKLYNPKVRLNKAEARKYTDSSAQRTTSAGSVLEDTSMHKKKKSIFSFLKKKEPKPVIGNNSVTNEKNKMSSSSTFSMNIQTSLKTPEKLKKKSHSSSSIFNSFLKGKIETSDSPRKEPMRQKKRTPKSKDKKQDTEQIIDAASVLSTESPLLRKNHDDTPVKIDHVTRSIDQRKPTPLNMDLILGGDKQINTPLQEHVREDDDAKNDLQLPTKDNFLSLDYEAPSPAFSKHDTGEVLFPKFLDNHEVDSIVSLERTRSTKSNKRSSMNSQRRSLTDTLSIKAQSEGMFITEASSVVLSTPDLTKSPASSILKNGRFEYSDNFSREHSYEGTTNEDFLDIKDDSGPLKKDDIFLESIEQKFDQLVMASDEEKTEVERDVPKPREEPLKKDSERQSVFADDDNELISDIMEFASFINFGDDDLNLDLDLGDTTASYATETPEPVGNDEVNRSGTFDTRNNKEDSYKERETQSYSAAGATTYGDERQGQLHTFEQDGSEINDNEFENEDFNKHIEQPIEVTPRNNAYLPEFEPNRPVSMSFKGLKAPRMNTSFIDSMTPDSPVKSDLTSLGEVYVNSNNDQGVRFSSQIILYDTYGEFEYDRHPEISTCNQLTPQLAQMIKLELNELKSAMEVHDDSRCYTHFY
Protein: Serine/threonine-protein kinase kin-29 (EC 2.7.11.1) (Q21017)
Organism: Caenorhabditis elegans
Function: Regulates chemoreceptor expression by phosphorylating the hda-4 class II histone deacetylase (HDAC) and inhibiting the gene repression functions of hda-4 and the mef-2 transcription factor, enabling the correct sensing and transduction of food signals. Role in determining body size, the dauer decision and serotonin-mediated egg laying. May modulate the Sma/Mab pathway and regulates development in the later larval stages.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11832225, ECO:0000269|PubMed:15840165}. Nucleus {ECO:0000269|PubMed:11832225, ECO:0000269|PubMed:15840165}. Note=Nuclear in larval stage. Predominantly cytoplasmic in the adult but translocates into the nucleus following heat shock. {ECO:0000269|PubMed:11832225, ECO:0000269|PubMed:15840165}.
Interaction partners:
- Serine/threonine-protein phosphatase 2B catalytic subunit
- Histone deacetylase 4
- MEF2 transcription factor homolog
- Protein phosphatase 2B regulatory subunit cnb-1
- Cell surface receptor daf-4
Sequence:
MAAPRRRMGLEKIGLYDVGRAIGKGNFATVRIARHKIAKTKVAIKSIDVSALDRENLIKLEREVKIVKVIDHPHIVKSYEIMRVDNMLYIVSEYCSSGELYETLIEKGRVAENVARKWFSETASAVAYLHSQGIVHRDLKAENILLGKNSNIKIIDFGFSNFQTGDQLLNTWCGSPPYAAPELLLGNSYDGMKADIWSMGVLLYILVAGGFPFPSDSVNKLKRSVLSGLVKIPYWVSVECADFIRKMLVLNPGKRYTIQNVLQHRWMHIRDDVQKNQAAQLLEAIPSSSIEIRQQSTKLNPTIMMFMQQHGKWSEEQIIDAVLGRDFESPIFATYELLADKVKKGTLEGTGEEFPRRGSRGSILSGKANVDEQPLTPTISAHQLAQLNLSSPDCDSDDSSNSDLCDDSPMSSMGPMNHERQFGTPHGLDIIGNRFENRRHTLCASEQLLSPNMMGQFPPPNLLLNNFSMNPPLGFPPMPEGQAAEFPLPSLHPAFATIPIADLSKMLPVPKSERRASAGETLLPTNFDLTQHLANLPAPPISFPTVEEEGKSYLSKYGGKRNTVHCLGNQLGGGIQNPIPRYQRTPYTKAPPAERRSSWASPSLSAQQQNHLEKLFKQALQTNNDMTRLHKEFKGLSHGCAQSQITNEGSSLACPQISITDEYNRQHNIAPSASSFDPVSIFQKNAQEVVFGQRPATAIGFSSTSFSGMSTPEQTTRSIDDRVRSIVCTLPFTEVIDELKASLNILKIPFSESHEMVYEPQVTEMRRLSLPSGVEIGVAVLPPEHKAHVEFAIINNDSPTSEYLCDQLICRLRMIDPSWSSE
Protein: HELP domain-containing protein (C4ALD8)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MFTVPGFCSLRSQVQTQQPRGANFYELILNENDRLKFRVDELEKIVVAQRNEILLLQSSTVEILRRLQNLEIQDQSRSPTCSGYSSLPRRISGSKSSYTMSPSHAPPRSSHANSKSLYINGMNNNSEEVSPGPPRHRPPTRGSDGMVNVSVGKSARGSPMRKWVSTHDMKDTDRFRRLSTSSEASTSATMNPIVNSVRRLSTTHRQSSPSLLSLCSVISRSPSTSSILRKNNRTCQFSNGSGHLPIFIGGKTVQVPVPTGYENMDPTMDQDPPTMKVTLKHVYSYRGKDVRSNIEMLPTGELVFFSANLVVLMNITGEDRSQRIYHGHTCDVKCITLHPNKILVASGQSSCHSVEKFQKPEHTSPIDSPEDLVRQLEMEHTEAHVRIWDTIKLTTLMVLNGFEKGICHVAFSKTDSGSLLAVVDDSLKHLMSVWNWQKGKREGEVKASNDVVFECKWHPTIRNLIVLYGKGHFSFFNYDPATGVLVKTVATFEGRDKPKTVLSMCFGENDQVVTGDSNGTISIWDPRTCKTTKQAHSVHPGGVYSLTLAKSGKILSGGKDRMVSEWDLQDLVRTRRPIELPDEKGFPRVILQNGSELIIGTSSNTLLFGNIENSTNLTSLIEGDPGNLTFLLTCSSNQLITSSQCGTLRIWNHIDKKVEFSKKFIDSVECVDVDVTNTHIILGFAAGLWIVMNITKQQTIQEKKEGTAPITAVKFAPSGATFAVATKDPHLTIYRIDASKNLLVIARIHHIPAPIVALDFSSDSQYLRGQSIGAHLLFWTKAGEICDGTSVKDVKWGSSRVKIGFETALVAHSSNGQVTAVAQCEDISACGMENGTIRIYKNPVTSVTAGFVELLGHGRIIKSVAFSNKIQLFSCSPTDNSVFEWCLE
Protein: Sarcosine oxidase delta subunit (Q9HTE7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Sarcosine oxidase alpha subunit
- Sarcosine oxidase gamma subunit
- Sarcosine oxidase subunit beta subunit beta)
- DgcA, Dimethylglycine catabolism
- Glycine betaine monooxygenase oxygenase subunit
- Formyltetrahydrofolate deformylase
- 4-vinyl reductase 4VR domain-containing protein
- Serine hydroxymethyltransferase 1
- Glycine betaine monooxygenase reductase subunit
- Membrane dipeptidase
Sequence:
MLNIFCPHCGELRSEEEFHAKGQAHIPRPLDPNACSDEEWGDYMFFRDNPRGLHHELWVHAAGCRKYFNVTRHTVTYEILETYLIGEQPSVVADGEKKPAVQGEPA
Protein: GTPase Era (SGP) (P37214)
Organism: Streptococcus mutans serotype c (strain ATCC 700610 / UA159)
Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (By similarity). Has GTPase activity, binds both GDP and GTP, does not bind UTP, CTP or ATP.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7790064}. Cell membrane {ECO:0000269|PubMed:7790064}; Peripheral membrane protein {ECO:0000269|PubMed:7790064}.
Interaction partners:
- Endoribonuclease YbeY
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein bS6
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS15
- Undecaprenol kinase
Sequence:
MSFKSGFVAILGRPNVGKSTFLNHVMGQKIAIMSDKAQTTRNKIMGIYTTDKEQIVFIDTPGIHKPKTALGDFMVESAYSTLREVDTVLFMVPADEKRGKGDNMIIERLKAAKVPVILVINKIDKVHPNQLLEQIDDFRNQMDFQEIVPISALQGNNVSHLVDLLVDHLEEGFQYFPADQITDHPERFLVSEMIREKVLLLTREEIPHSVAVVIDSMARDEETHKIHIRATIMVERDSQKGIIIGKKGAMLKKIGQMARRDIELMLGDKVYLETWVKVKKNWRDKKLDLADFGYNKKEY
Protein: Phage shock protein A (Q9F4H4)
Organism: Yersinia enterocolitica
Interaction partners:
Sequence:
MGIFSRFADIVNANINTLLDKAEDPQKLVRLMIQEMEDTLVEIRSTSARALAEKKQLLRRIDHCESQQQEWQDKAELALRKDKEDLARAALIEKQKVVALIETLTREVATVDETLTRMKHEITELESKLTETRARQQALTLRHQAAASSRDVRRQLDSGKLDEAMARFEQFERRIDHMEAEAETVGIGKQKSLESQFAELKADDEISNQLAALKAKMNSAQ
Protein: EXOC7 protein (Q96BU6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRPWVAVLSLFPSRGWAGAALGPKVAPGQQPSQQHSLYGAEEEQQQQDGEVVNWGRQGTGRCSGASPCVSGAQRAEHQWVTGEKQGRLGKGAGLTEQWVAGGGAGQGLHQGGVEDEVTQQQCHLVAYALNGPEGQQPPAHVSQQQCLCRHQESDDGLERRVLQPQLEGEKSGPSRRGGRRWASGAWGLASGRASSLPPASSSPLSASSRLDSPSPGSRAPAAGVGLGSSDHKLRIPS
Protein: Protein phosphatase 2, regulatory subunit B'', alpha (Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha isoform X1) (E9QG28)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAATYRIVVSSINCYNSVVIDRRVQHTVHYCNGPCGALKHGLNCTVAHRSTCAELLDTSISRTCSERPINLHESKTIENGNTGPVAFCDDYHQVIPRVKKGSAIQSSASLKDITGEAINLASGKIKEFSFEKIKYSSSHVTFRKGRKVRPDSFSRRSTDLDIIYGQFTGNDENCPPFGLFQKSVLEEHKLSRSASLEQNLNNVATLYLNSLTEENLITRILEKTKADSSASGEDIKACLDILLKCSEDLKKCTDIIKQCIKRKSMGGTSDDSGNPEIIYKNVMARLSNYLKRLPLELEQGQSIRQEHSELAELVNSIHGLQQIPFSPIFGNEQPPRYEDVVQSPPPTKPRNKPSQPEPSEGSRELTGSLKPIQSVPGLSARTPPSTNGFSHGSLPTASSSSSTPFICQHTVSTSRPDTFSSANSFLSISNENLCKDPMEALYIEEEDSDIGRMPDRPVKGDGKHSCNLSESRQYSKRTTGYSEPSGGVSDKLHELSRNGTTFKPQNDSTVNQMYLPKSTDSKLFSRSTSHTSKGGADDIDKLLMDLECLSQNMQKEPPLPPKLKNCALQTSSPQHLIGNSVVKDLPVVGFSGPSVAKPPEPGVESTEEDDGALLLRILESIESFAQELVESGAGRGTQTKEREVMRLLQETLASTKAEVTPLPLPESETAPSPPQTPQCKPASTLSNTPTAIQIPASTLRDTGSTLLIQQTPEVIRIQPEKKPGTPPPTLSPAPSSPTPRPPSPPPAKVVATPPPSSINIPRFYFPKGLPNCAANYDEAIAKIEAAFTEFEEEKADIYEMGKIAKACGCPLYWKSPMFICAGGERTGFVSVHSFIATWRKLLHSCYDDASKFVYLLAKPGCTYLEQEDFIPLLQDIVDTHPGLTFLKDAPEFHSRYITTVIQRIFYTVNRSWTGKINMTELRRSNFLQTLALLEEEDDINQITDYFSYEHFYVIYCKFWELDSDHDLFIDPKDLARYNDHASSSRIIERLFSGAVTRGNSVQREGRMSYAEFVWFLISEEDKKNPTSIEYWFRCMDMDGDGVLSMFELEYLYEEQCERMEGMGIEPLPFQDLLCQMLDLVKPECPSKITLRDLKRCRMAHIFYDTFFNLEKYLDHEQRDPFAVQKDLDSDGPEPSDWDKYASEEYEILVAEETANEQLREGSFDDDYESDELTVSSDIGNKMDKLVISDLSA
Protein: Properdin (Complement factor P) (P27918)
Organism: Homo sapiens (Human)
Function: A positive regulator of the alternate pathway (AP) of complement. It binds to and stabilizes the C3- and C5-convertase enzyme complexes. Inhibits CFI-CFH mediated degradation of Complement C3 beta chain (C3b).
Subcellular location: Secreted {ECO:0000269|PubMed:28264884, ECO:0000269|PubMed:31507604}.
Interaction partners:
- Complement C3
- Complement factor B
- Natural cytotoxicity triggering receptor 1
- Complement C2
- Complement factor H
- Beta-1,3-glucosyltransferase
- Complement factor D
- Ficolin-1
- Mannose-binding protein C
- Plasma protease C1 inhibitor
Sequence:
MITEGAQAPRLLLPPLLLLLTLPATGSDPVLCFTQYEESSGKCKGLLGGGVSVEDCCLNTAFAYQKRSGGLCQPCRSPRWSLWSTWAPCSVTCSEGSQLRYRRCVGWNGQCSGKVAPGTLEWQLQACEDQQCCPEMGGWSGWGPWEPCSVTCSKGTRTRRRACNHPAPKCGGHCPGQAQESEACDTQQVCPTHGAWATWGPWTPCSASCHGGPHEPKETRSRKCSAPEPSQKPPGKPCPGLAYEQRRCTGLPPCPVAGGWGPWGPVSPCPVTCGLGQTMEQRTCNHPVPQHGGPFCAGDATRTHICNTAVPCPVDGEWDSWGEWSPCIRRNMKSISCQEIPGQQSRGRTCRGRKFDGHRCAGQQQDIRHCYSIQHCPLKGSWSEWSTWGLCMPPCGPNPTRARQRLCTPLLPKYPPTVSMVEGQGEKNVTFWGRPLPRCEELQGQKLVVEEKRPCLHVPACKDPEEEEL
Protein: Fanconi anemia group F protein (Protein FACF) (E9Q5Z5)
Organism: Mus musculus (Mouse)
Function: DNA repair protein that may operate in a postreplication repair or a cell cycle checkpoint function. May be implicated in interstrand DNA cross-link repair and in the maintenance of normal chromosome stability.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NPI8}.
Interaction partners:
- Fanconi anemia group M protein homolog
- Fanconi anemia group B protein homolog
- Fanconi anemia, complementation group E
- E3 ubiquitin-protein ligase FANCL
- Fanconi anemia core complex-associated protein 100
- Fanconi anemia group C protein homolog
- Fanconi anemia group G protein homolog
- Fanconi anemia group A protein homolog
- Fanconi anemia group D2 protein homolog
- Fanconi anemia group I protein homolog
Sequence:
MEPLVQQTERFSELLAVSCGSLVSTWDAEKVRRALQWARYLLHVYRRFAGRGRVREALERRLPARGGPLGLRSFAALESGDARLALRLLRNRALAPAAARALPSLLFPGPAADHRDDVPQSRLVLLARRGSALRLLCRLGGDAPRSALLRTHAELLDARLHELGGADSAAARKLLDTLWTRGPREHVLDVTAEALLLREEDPEPAQATDPAGADETQKLLRWLLESPEVLAAFCRHLPAKRLASVAGCHHALSRAYLDLLTTWATRLHYDLQKGAWVPTQMEDMPWEELCLRLQSLCHAQPFLQEEVLVTLRSRKALDGDFEVPGMSIWTDLLVVLECGIVLE
Protein: cDNA FLJ50351, highly similar to Transcription initiation protein SPT3 homolog (B4E1H0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFEDDEIDEVKQERMERAERQTRIMDSAQYAEFCESRQLSFSKKASKFRDWLDCSSMEIKPNVVAMEILAYLAYETVAQLVDLALLVRQDMVTKAGDPFSHAISATFIQYHNSAESTAACGVEAHSDAIQPCHIREAIRRYSHRIGPLSPFTNAYRRNGMAFLAC
Protein: Dual specificity protein phosphatase, putative (Q384M4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MALEKIDWTVPRKLLPKDSLEVTDSANPYAELSEILPGLYLTSEERVCNRARSIEESISLILTLNGGEHVAPYRIYEYLAEDQRYVYKKICSFNVFASLLEEYASTSVPEDPLQRKVFIRSVPAEDCPTYDISRHFPEMCALIELVMMHRRDTEVELARQHTVVVHCLMGVSRSAAVVAAYMMKRGRYSKDESVSIMRKSRPIVSPNPGFQKQLMRWEEGAYYRISDMLSATLAASEVRGGTELNHFIERQLRLLLRERRFIEDRKNFGYVISSVLSITPGVGSAVLMIAAHINQCIVEEVYVDVPSFFSNVSDIVKSIFQHMPNFINDITEEFGDPFDDCFYFEMVKAIGCSGAGKCLSDVAKAFSSLLETVHTTHMINNPRGVPYWADSEDEIARGCPEGMRLSFTFLPFLAPYAVGFVQLRYSGELMNEEGLYLLQVTSSRISPPSEYKISELTCNATADGCAIAVDIFSCMVSQVGHLKDDVELEMLNAVLGGSTLLAVIDKFVYTEEPNEGIALLWMRKVVGGAVGIRLFFDAIDRYLMESYLNVAEIGTIKSIADEKAPWVEIATSIQLVNRVYMEQYGKVVDFLPWILQELSSMIDNGAVVVSSDISCSGE
Protein: Conidiation protein Con-6, putative (AFU_orthologue AFUA_4G03615) (Q5ASU0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MADERINQMRGYKATLNNPRVSNEAKEHAQSVLDNELGGDQPHEDILTAQGARNKSPNRVAGGYKAAMHNDSISKQGKKQAQEKLGEMPQE
Protein: Pleckstrin homology domain-containing protein 1 (AtPH1) (Q9ST43)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds specifically to phosphatidylinositol 3-phosphate (PtdIns3P), but not to other phosphoinositides.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Histone H4
- Lysine-specific demethylase ELF6
- Zinc ion binding / DNA binding protein
- PHD finger family protein / SWIB complex BAF60b domain-containing protein / GYF domain-containing protein
- Ubiquitin-ribosomal protein eL40y fusion protein
- DNA-directed RNA polymerase II subunit 4
- Ubiquitin-ribosomal protein eL40z fusion protein
- Protein RBL
- Protein TRAUCO
- DNA-directed RNA polymerases II, IV and V subunit 11
Sequence:
MESIWRIATGQDPSREDYEGIEFWSNPERSGWLTKQGDYIKTWRRRWFVLKRGKLLWFKDQAAAGIRGSTPRGVISVGDCLTVKGAEDVVNKPFAFELSSGSYTMFFIADNEKEKEEWINSIGRSIVQHSRSVTDSEVLDYDHRR
Protein: CAP-Gly domain-containing linker protein 1 (Cytoplasmic linker protein 170) (CLIP-170) (Restin) (Q9JK25)
Organism: Rattus norvegicus (Rat)
Function: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes microtubule growth and microtubule bundling. Links cytoplasmic vesicles to microtubules and thereby plays an important role in intracellular vesicle trafficking. Plays a role macropinocytosis and endosome trafficking.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P30622}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:26972003}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P30622}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell projection, ruffle {ECO:0000250|UniProtKB:P30622}. Note=Localizes to microtubule plus ends. Localizes preferentially to the ends of tyrosinated microtubules (PubMed:26972003). Accumulates in plasma membrane regions with ruffling and protrusions. Associates with the membranes of intermediate macropinocytic vesicles (By similarity). {ECO:0000250|UniProtKB:P30622, ECO:0000269|PubMed:26972003}.
Interaction partners:
- Dynactin subunit 1
- Ras GTPase-activating-like protein IQGAP1
- Microtubule-associated protein RP/EB family member 1
- CLIP-associating protein 2
- Microtubule-associated protein RP/EB family member 3
- Cell division control protein 42 homolog
- Nuclear migration protein nudC
- CLIP-associating protein 1
- Serine/threonine-protein kinase PLK1
- Cell division cycle protein 20 homolog
Sequence:
MSMLKPSGLKAPTKILKPGSTALKTPAAAAAPLEKTVPSEKASGPPSSETQEEFVDDFRVGERVWVNGNKPGFIQFLGETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLKGIFTRPSKLTRKVQAEDEANGLQTAHARAASPLSTAAATMVSSSPATPSNIPQKPSQPVAKETSATPQISNLTKTASESISNLSEAGSVKKGERELKIGDRVLVGGTKAGVVRFLGETDFAKGEWCGVELDEPLGKNDGAVAGTRYFQCQPKYGLFAPVHKVTKIGFPSTTPAKAKAAAVRRVMATTPASLKRSPSASSLSSMSSVASSVSSKPSRTGLLTETSSRYARKISGTTALQEALKEKQQHIEQLLAERDLERAEVAKATSHVGEIEQELALARDGHDQHVLELEAKMDQLRTMVEAADREKVELLNQLEEEKRKVEDLQFRVEEESITKGDLETQTKLEHARIKELEQSLLFEKTKADKLQRELEDTRVATVSEKSRIMELEKDLALRVQEVAELRRRLESSKPPGDVDMSLSLLQEISALQEKLEVTHTDHQNEVTSLKDHFGTREEMFQKEIKALHAATEKLSKENESLRSKLDHANKENSDVIALWKSKLETAIASHQQAMEELKVSFSKGIGTDSAEFAELKTQIERLRLDYQHEIESLQSKQDSERSAHAKEMESMKAKLMKIIKEKEDSLEAVKARLDTAEDQHLVEMEEMLSKLQEAEIKKEKFASASEEAVSTQTSMQDTVNKLHQKEEQFNMLSSELEKLRENLTDMEAKFKEKDEREDQLVKAKEKLENDIAEIMKMSGDNSSQLTKMNDELRLKERSVEELQLKLTKANENASLLQKSIGEVTLKAEQSQQEAAKKHEEEKKELENKLLELEKKMETSHYQCQDLKAKYEKASSETKIKHEEILQNFQKMLVDTEDKLKAAQEANRDLMQDMEELKSQADKAKAAQTAEDAMQIMEQMTKEKTETLASLEDTKQTNAKLQSELDTLKENNLKTVEELNKSKELLNEENQKMEEFKKEIETLKQAAAQKSQQLSALQEENVKLAEELGRTRDEVTSHQKLEEERSVLNNQLLEMKKSLPSNTLRESEYRKDADEEKASLQKSISLTSALLTEKDAELEKLRNEVTVLRGENASAKSLHSVVQTLESDKVKLELKVKNLELQLKENKRQLSSSSGNTDVQTEEDERAQESQQMIDFLNSVIVDLQRKNQDLKMKVEMMSEAALNGNGEDPNSYDSDDQEKQSKKKPRLFCDICDCFDLHDTEDCPTQAQMSEDPPHSTHHGSRSEERPYCEICEMFGHWATNCNDDETF
Protein: V-akt murine thymoma viral oncogene-like protein 1 isoform 2 (A0A0S2Z3D6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQCQLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDFRSGSPSDNSGAPRTPRRSCSIASLPVSCGSTCTRRSSAHPSSPRSRRRLTPGILMRSSRPR
Protein: Probable protein S-acyltransferase 23 (EC 2.3.1.225) (Probable palmitoyltransferase At2g14255) (Zinc finger DHHC domain-containing protein At2g14255) (Q3EC11)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Palmitoyl acyltransferase.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDSSEIEVVPLDSNSHQSPTESPTITDVFSASAYGDLHQLKHFVEHNGSSVSLPDDNGFYALQWAALNNSLHVAQYIIQHGGDVNSADNIQQTPLHWAAVKGSIDVADLLLQHGARIEAVDVNGFRAVHVASQYGQTAFVNHIIVDYAADYNALDIEGRSPLHWAAYNGFTETVRLLLFRDACQNRQDNTGCTPLHWAVIKENVEACTLLVHAGTKEELILKDNTGSTPLKLASDKGHRQLALFLSKAMRTRKNSFVDKIFCGKLGETSYAPMLFSLIVILMVLFITSIVSASNLPKITAMVGLWACFGLSCGVYALITFYRVSRKDPGYVKRTGEANSQHTANDPLIDINFKNPSWKGNWSQLCPTCKIIRPVRSKHCPTCKRCVEQFDHHCPWISNCVGKKNKRYFLVFVIMGALTSFVGGTTAVQRLWRGIPQVHHGESWIKHIVIEHPDAAVFLFFDLLIFIATMTLTISQSYMIARNITTNELWNAKRFSYLRGPDGRFYNPYNHGLRRNCTDFLVHGYTRDDEVVPSSIL
Protein: Protein FAM217B (Q9NTX9)
Organism: Homo sapiens (Human)
Interaction partners:
- SH2/SH3 adapter protein NCK1
Sequence:
MNAGPSWNKVQHSKNSSGKRQSKSQVPHASSQPRSSLTAVTQPTEEKLKESISPEARRKRNPLGSRCQGASGNKLFLDFQSMKIIKENADEDSASDLSDSERIPIPPSPLTPPDLNLRAEEIDPVYFDLHPGQGHTKPEYYYPNFLPSPFSSWDLRDMALLLNAENKTEAVPRVGGLLGKYIDRLIQLEWLQVQTVQCEKAKGGKARPPTAPGTSGALKSPGRSKLIASALSKPLPHQEGASKSGPSRKKAFHHEEIHPSHYAFETSPRPIDVLGGTRFCSQRQTLEMRTEEKKKKSSKSTKLQRWDLSGSGSSSKVETSGHIRVPKQAAVILDSADSCKASKTQAHAHPRKKGKAESCGHATVSSEKKLKTNGVKQNTYKLK
Protein: 9-cis-epoxycarotenoid dioxygenase NCED9, chloroplastic (AtNCED9) (EC 1.13.11.51) (Q9M9F5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has a 11,12(11',12') 9-cis epoxycarotenoid cleavage activity. Catalyzes the first step of abscisic-acid biosynthesis from carotenoids. Contributes probably to abscisic acid synthesis for the induction of seed dormancy.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:12834401}.
Interaction partners:
- Xanthoxin dehydrogenase
- Zeaxanthin epoxidase, chloroplastic
- Abscisic-aldehyde oxidase
- Abscisic acid 8'-hydroxylase 2
- Phytoene synthase 1, chloroplastic
- Protein ABSCISIC ACID-INSENSITIVE 5
- Abscisic acid 8'-hydroxylase 1
- B3 domain-containing transcription factor ABI3
- Zeta-carotene desaturase, chloroplastic/chromoplastic
- Abscisic acid 8'-hydroxylase 3
Sequence:
MTIITIISGMYIYSLLSQDAHHSQYGQNTNLVLKKPIPKPQTAAFNQESTMASTTLLPSTSTQFLDRTFSTSSSSSRPKLQSLSFSSTLRNKKLVVPCYVSSSVNKKSSVSSSLQSPTFKPPSWKKLCNDVTNLIPKTTNQNPKLNPVQRTAAMVLDAVENAMISHERRRHPHPKTADPAVQIAGNFFPVPEKPVVHNLPVTGTVPECIQGVYVRNGANPLHKPVSGHHLFDGDGMVHAVRFDNGSVSYACRFTETNRLVQERECGRPVFPKAIGELHGHLGIAKLMLFNTRGLFGLVDPTGGLGVANAGLVYFNGHLLAMSEDDLPYHVKVTQTGDLETSGRYDFDGQLKSTMIAHPKIDPETRELFALSYDVVSKPYLKYFRFTSDGEKSPDVEIPLDQPTMIHDFAITENFVVIPDQQVVFRLPEMIRGGSPVVYDEKKKSRFGILNKNAKDASSIQWIEVPDCFCFHLWNSWEEPETDEVVVIGSCMTPPDSIFNEHDETLQSVLSEIRLNLKTGESTRRPVISEQVNLEAGMVNRNLLGRKTRYAYLALTEPWPKVSGFAKVDLSTGEIRKYIYGEGKYGGEPLFLPSGDGEEDGGYIMVFVHDEEKVKSELQLINAVNMKLEATVTLPSRVPYGFHGTFISKEDLSKQALC
Protein: Immunoglobulin heavy variable 1-2 (Ig heavy chain V-I region ND) (Ig heavy chain V-I region V35) (P23083)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin heavy chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MDWTWRILFLVAAATGAHSQVQLVQSGAEVKKPGASVKVSCKASGYTFTGYYMHWVRQAPGQGLEWMGWINPNSGGTNYAQKFQGWVTMTRDTSISTAYMELSRLRSDDTAVYYCAR
Protein: Man(5)GlcNAc(2)-PP-dolichol translocation protein RFT1 (Requiring fifty-three protein 1) (P38206)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in N-linked oligosaccharide assembly. Required for the translocation of Man(5)GlcNAc(2)-PP-dolichol from the cytoplasmic side to the lumenal side of the endoplasmic reticulum membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11807558}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- GDP-Man:Man
- Alpha-1,3/1,6-mannosyltransferase ALG2
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- UDP-N-acetylglucosamine transferase subunit ALG13
Sequence:
MAKKNSQLPSTSEQILERSTTGATFLMMGQLFTKLVTFILNNLLIRFLSPRIFGITAFLEFIQGTVLFFSRDAIRLSTLRISDSGNGIIDDDDEEEYQETHYKSKVLQTAVNFAYIPFWIGFPLSIGLIAWQYRNINAYFITLPFFRWSIFLIWLSIIVELLSEPFFIVNQFMLNYAARSRFESIAVTTGCIVNFIVVYAVQQSRYPMGVVTSDIDKEGIAILAFALGKLAHSITLLACYYWDYLKNFKPKKLFSTRLTKIKTRENNELKKGYPKSTSYFFQNDILQHFKKVYFQLCFKHLLTEGDKLIINSLCTVEEQGIYALLSNYGSLLTRLLFAPIEESLRLFLARLLSSHNPKNLKLSIEVLVNLTRFYIYLSLMIIVFGPANSSFLLQFLIGSKWSTTSVLDTIRVYCFYIPFLSLNGIFEAFFQSVATGDQILKHSYFMMAFSGIFLLNSWLLIEKLKLSIEGLILSNIINMVLRILYCGVFLNKFHRELFTDSSFFFNFKDFKTVIIAGSTICLLDWWFIGYVKNLQQFVVNVLFAMGLLALILVKERQTIQSFINKRAVSNSKDV
Protein: Zfu2p (A0A1D8PKQ8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Glutamyl-tRNA
Sequence:
MSKRRTVKRSRNGCLSCKKLRIKCDESKPTCEYCLHTNRQCIYTIPKLQEYLDTFTSSSDLLEAISNCEELLSSTTSTGSVTTNTTNTTTTTTTTSINNNNNTTIMTEYSSPVEKDHLHRELILTQPTTILGISKFELKLLKFYDYQCISMFSYGHNQEIHNTWKYKVPHLFIQSQLVRNSIFALASMVLQSTITPAFNDSLQIAQIQNNLFNSTLEYFLDVLNQTKSIINGCPETIDFQNVTTAKELTVSSTILFTILAINPNRLLPLISFDKSQSDFISISKGVVMIIAKASPIVFGSDLIGIIYYGTLNGVNPPNLNNPTFPIIKNLINDLNNNNNNIYDYSSSTYELLYESLDILNKGMYATQSFEFPVPFFRWINLISDDFRQLLYDQDEFALRLLFVFSSLCLYAGFSLNDEFNIWKDFIDWYKHDQEGKYNGQFKYLMDGKLYQLIIVEKKRCNKFKEFPELDVN