wanglab/gogpt-training-data huggingface dataset:
Protein: Synaptotagmin-4 (Synaptotagmin IV) (SytIV) (P40749)
Organism: Mus musculus (Mouse)
Function: Synaptotagmin family member which does not bind Ca(2+). Plays a role in dendrite formation by melanocytes (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle membrane {ECO:0000250|UniProtKB:P50232}; Single-pass membrane protein {ECO:0000250|UniProtKB:P50232}.
Interaction partners:
- Otoferlin
- Synaptosomal-associated protein 25
- Vesicle-associated membrane protein 2
- GTP-binding protein Rit2
- Complexin-1
Sequence:
MAPITTSRVEFDEIPTVVGIFSAFGLVFTVSLFAWICCQRRSAKSNKTPPYKFVHVLKGVDIYPENLSSKKKFGGDDKSEVKGKAALPNLSLHLDLEKRDLNGNFPKANPKAGSSSDLENVTPKLFTETEKEANSPESLKSSTSLTSEEKQEKLGTLFLSLEYNFEKKAFVVNIKEAQGLPAMDEQSMTSDPYIKMTILPEKKHRVKTRVLRKTLDPVFDETFTFYGIPYPHIQELSLHFTVLSFDRFSRDDVIGEVLIPLSGIELSDGKMLMTREIIKRNAKKSSGRGELLVSLCYQSTTNTLTVVVLKARHLPKSDVSGLSDPYVKVNLYHAKKRISKKKTHVKKCTPNAVFNELFVFDIPCESLEEISVEFLVLDSERGSRNEVIGRLVLGATAEGSGGGHWKEICDFPRRQIAKWHMLCDG
Protein: Sestrin 1 (Sestrin-1 isoform X3) (Q5RGN4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MRHALASNETMENSSLTMTDLFKICTQCERLSKKDVGVRIPRPVGNGPSRFIPEKEVHRVSTPLLSQILQVSKLDERTQSIFEDAFAVLGRLDNISLVMGFHPQYLESFLRTQHYLLQMDGPLSLHCRHYIGIMAAARHQCTYLVNLHVNDFLQVGGDPKWLNGLEEAPRKLQALGELNKILAHRPWLLTKEHIERLLKAEEHSWSLAELIHAVVLLTHYHSLASFTFGCGITPDIHTDGGHTFRPPSLSGYCVCDIANGNGAQEDMFGNQQVSESSGEVEVLMERMKQLQECRDEEEASQEEMATRFEREKTECMLVVTSEDEECVPSRDVSRHFEDPSYGYKDFSRRGEHVPTLRVQDYSWEDHGFSLVNRLYSDFGQLLDEKFQIAFNLTYNTMATHQGVDTSMLRRAIWNYIHCMFGIRYDDYDYGEINQLLDRSFKVYIKTMVCSPEKITKRMYESFWRQFRHSEKVHVNLLLMEARMQAELLYALRAITRYMT
Protein: UDP-glucuronosyltransferase 1A3 (UGT1A3) (EC 2.4.1.17) (UDP-glucuronosyltransferase 1-3) (UDPGT 1-3) (UGT1*3) (UGT1-03) (UGT1.3) (UDP-glucuronosyltransferase 1-C) (UGT-1C) (UGT1C) (UDP-glucuronosyltransferase 1A isoform 3) (P35503)
Organism: Homo sapiens (Human)
Function: UDP-glucuronosyltransferase (UGT) that catalyzes phase II biotransformation reactions in which lipophilic substrates are conjugated with glucuronic acid to increase the metabolite's water solubility, thereby facilitating excretion into either the urine or bile. Essential for the elimination and detoxification of drugs, xenobiotics and endogenous compounds. Catalyzes the glucuronidation of endogenous estrogen hormones such as estradiol and estrone. Contributes to bile acid (BA) detoxification by catalyzing the glucuronidation of BA substrates, which are natural detergents for dietary lipids absorption. Involved in the glucuronidation of calcidiol, which is the major circulating form of vitamin D3, essential for the regulation of calcium and phosphate homeostasis. Involved in the glucuronidation of the AGTR1 angiotensin receptor antagonists losartan, candesartan and zolarsartan, which can inhibit the effect of angiotensin II.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:17179145}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-glucuronosyltransferase 1A9
- UDP-glucuronosyltransferase 1A6
- UDP-glucuronosyltransferase 1A1
- UDP-glucuronosyltransferase 1A8
- UDP-glucuronosyltransferase 1A4
- UDP-glucuronosyltransferase 1A7
- UDP-glucuronosyltransferase 1A10
- Cytochrome P450 3A4)
- Cytochrome P450 2D6
- UDP-galactose translocator
Sequence:
MATGLQVPLPWLATGLLLLLSVQPWAESGKVLVVPIDGSHWLSMREVLRELHARGHQAVVLTPEVNMHIKEENFFTLTTYAISWTQDEFDRHVLGHTQLYFETEHFLKKFFRSMAMLNNMSLVYHRSCVELLHNEALIRHLNATSFDVVLTDPVNLCAAVLAKYLSIPTVFFLRNIPCDLDFKGTQCPNPSSYIPRLLTTNSDHMTFMQRVKNMLYPLALSYICHAFSAPYASLASELFQREVSVVDILSHASVWLFRGDFVMDYPRPIMPNMVFIGGINCANRKPLSQEFEAYINASGEHGIVVFSLGSMVSEIPEKKAMAIADALGKIPQTVLWRYTGTRPSNLANNTILVKWLPQNDLLGHPMTRAFITHAGSHGVYESICNGVPMVMMPLFGDQMDNAKRMETKGAGVTLNVLEMTSEDLENALKAVINDKSYKENIMRLSSLHKDRPVEPLDLAVFWVEFVMRHKGAPHLRPAAHDLTWYQYHSLDVIGFLLAVVLTVAFITFKCCAYGYRKCLGKKGRVKKAHKSKTH
Protein: Uncoordinated (Uncoordinated, isoform B) (Q9VRF2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Putative sodium-coupled neutral amino acid transporter 11
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup153
Sequence:
MKVRHVPASTTTLSFRAKQRDVGGIGMPCERERKHEAAKREREEQIKQERATAASATQRVRQHNRRISTDGDPARRRMTQSRERLQATGLGRPGPCGPSNITRVTRGSSLPPEVGAHGYRTGRPTRKHVPIPQDQIEEQDDSDARAERLRQQLEELAAMSEQEFEVKFRQWLDQEGIAREMHSHLRVELIHCFNNTALGQLLSKAAGVQMAQSHALLVSPLAMVLHTLVAEFLHSQNCHFTLSVFCSETPHRSNLPDFRSRPEFRFQTEELQKVVAAILGEKEALADSEFGKLAEAHYEEDLAGQTQCLLMALMRTLVEIRRSVPKQEVEQPVPVSLQDTGCQTEPSACVEARPEVDTTGLYQTEEHELILGADGRSVFVGGRVSQSLHSVEQQLNQLIKNLRHLAKSCAPPVEVISSTKFEDLLMKELRERERLLKAGQAFNPGEPVIKIATGDKEEEHEVTSGRNQKDVVHSNLGPIQVPALDVTIPQLPRLHSEQLASLAVIRQSLEKVQKKSRQPQGRMYVSMERMETLMGDVCGCVQLLSNVLNLSMEQEHSVGMHKGFKWGYREGFAHGHFMGLQEGQKLEQLEQKKWQKERPLPEKRESSVQTESTIPTASIATQTSRKSAHNESVITQTEQKQLKDAGNQASCEPPTFQKSYEQWIHEMLHSSSGQVFLERVELSLNKALELQKVRLNELFQVKLRHQAEMLRLSKRQNSWRTLCKRVERDSQSSAEARDLVQQIFRLLEHYEAHHQQLAEKIQQTELAAEQAARIMPMWADGAAVGSASVNWNTAMSTTLISSGICTPPPAQPAADGALNVGKTHVEQHTYPDLGYPYQLLALAPPGGVPVAGTFVPVTHLPAHLLGASEHPVPLVPVARIYSDPMKTSRRLLSPSSVPADNDSAHRAAGETNAFTFQGGPVSGDLHPTENRNQAPATQGQQFPVPLPVPAPRGPSPSVQSVLPSTASPALPPPDETVPQPGPSQSSIPLKPSMHSVATNTITPVPPKATPLKPVNSKVSEGPSFEEALLSAKSRMLQLEQESDLLEQSFLSYLEKTKSKTSPHKSSEDAARARRIRSSCLREREQVHRTMDGFRDWHRRVRKEDAASVAQLEELRNQRLIPDPILDSKGSSPLWLSELEEGHEQDSYPFTNAITEARNKVLDKIMPVRKEEKKEKQNVKKNWLADLPFQIPEASPKQDRHLTNVKPAVTRSSSNGEMNVLLQRAKDALGLRTPNPLLDSSSSSSSMELPSMGAGRSPSTKFQQSMARMQMLFGGAEAVKPTMPAKTGRPVSAPTAASEPGLCAHLVLPKRPHTAPTLHTINENEPAVHHLDVSTSSSSQSTLPGRSSGEAFEDLVMSAVADGARRRNAESSTEVSYSQAFWKRINL
Protein: Inner membrane protein YcdZ (P75916)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Probable phosphatase YcdX
- Chaperone protein YcdY
- Putative sgc region transcriptional regulator
- Anaerobic C4-dicarboxylate transporter DcuC
Sequence:
MNILLSIAITTGILSGIWGWVAVSLGLLSWAGFLGCTAYFACPQGGLKGLAISAATLLSGVVWAMVIIYGSALAPHLEILGYVITGIVAFLMCIQAKQLLLSFVPGTFIGACATFAGQGDWKLVLPSLALGLIFGYAMKNSGLWLAARSAKTAHREQEIKNKA
Protein: Alpha/beta-Hydrolases superfamily protein (At3g01690) (F28J7.1 protein) (F4P13.23 protein) (Q9S7U7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGGVTSSVAAKFAFFPPSPPSYKVVTDELTGLLLLSPFPHRENVEIVKLRTRRGTEIVGMYVRHPMATSTLLYSHGNAADLGQMYELFIELSIHLKVNLMGYDYSGYGQSTGKPSEHNTYADIEAVYKCLEETFGSKQEGVILYGQSVGSGPTLDLASRLPQLRAVVLHSPILSGLRVMYSVKKTYWFDIYKNIDKIPYVDCPVLIIHGTSDEVVDCSHGKQLWELCKDKYEPLWVKGGNHCDLEHYPEYIRHLKKFIATVERLPCPRMSSDQSERVRDAPPRRSMDRRVKPRQSTERREKEKPPKSQSKMSSSSSKLKISFDQLDRSRRSVDCHEKTRKSVDQIERGRKSVDRLDRVRSE
Protein: Annexin A13 (Annexin XIII) (Annexin-13) (Intestine-specific annexin) (ISA) (Q29471)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Binds to membranes enriched in phosphatidylserine or phosphatidylglycerol in a calcium-dependent manner. Half-maximal membrane binding requires about 60 uM calcium. Does not bind to membranes that lack phospholipids with an acidic headgroup.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:P27216}. Cell membrane {ECO:0000250|UniProtKB:P27216}; Lipid-anchor {ECO:0000250|UniProtKB:P27216}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99JG3}. Note=Myristoylation anchors the protein to the membrane, but the protein also displays calcium-dependent, reversible binding to lipid membranes. {ECO:0000250|UniProtKB:P27216}.; SUBCELLULAR LOCATION: [Isoform B]: Cytoplasmic vesicle {ECO:0000269|PubMed:7896870}. Note=Enriched in apical vesicles. {ECO:0000269|PubMed:7896870}.
Interaction partners:
Sequence:
MGNRHAKAKSHHGFDVDHDAKKLNKACKGMGTDEAAIIEILSSRTSDERQQIKQKYKATYGKDLEEVFKSDLSGNFEKTALALLDRPSEYDARQLQKAMKGLGTDEAVLIEILCTRTNKEIMAIKEAYQRLFDRSLESDVKADTSGNLKAILVSLLQANRDEGDDVDKDLAGQDAKDLYDAGDGRWGTDELAFNEVLAKRSHKQLRATFQAYQILIDKDIEEAIEAETSGDLQKAYLTLVRCARDQEGYFADRLYKSMKGTGTDEETLIHIIVTRAEVDLQGIKAKFQEKYQKSLSDMVRSDTSGDFQKLLVALLH
Protein: UNC-13 protein (O96959)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VIGESTTKLTRLRTEKMCPDVDEEDENLSDHVSDLTDLSKLISQKKKTLLRGETEEVVGGHMQVLRQTEITARQRWHWAYNKIIMQLNNGGGPGEVGLRTNGHPGDNPFYSNIDSMPDIRPRRKSIPLVSELVLKTMAATKRNAGLTSAVPRATLNDEDLKMHVYKKALQALIYPISSTTPHNFLLWTATSPTYCYECEGLLWGIARQGVRCTECGVKCHEKCKDLLNADCLQRAAEKSSKHGAEDKANSIITAMKDRMKQREREKPEIFELIRAVFSVEEKSHAGHMKAVKQSVLDGTSKWSAKIAITVICAQGLMAKDKSGTSDPYVTVQVSKVKKRTRTMPQELNPVWNEKFHFECHNSSDRIKVRVWDEDNDLKSKLRQKLTRESDDFLGQTIIEVRTLSGEMDVWYNLEKRTDKSAVSGAIRLHISVEIKGEEKVAPYHVQYTCLHENLFHYLCEENTGMVKLPTQKGDDAWKLYFDEIPEEIVDEFSMRYGIENIYQAMTHFHCLSAKYLCPGVPAVMSTLLANINAYYAHTTASSAVSASDRFAASNFGKEKFVKLLDQLHNSLRIDLSMYRNNFPASSPEKLMDLKSTVDLLTSITFFRMKVQELSSPPRASTVVKDCVKACLRSTYQFLFENCYELYNREFQVDPNEAKRAPDDHEPKLDSVDFWHKLIALIVSVIDEDKNSYGTVLNQFPQELNIGQLSASSMWHLFAVDMKYALEEHEQHRLCKSSAYMNLHFRVKWLYSNYVKEVPPYKGAVPDYPAWFEPFVMQWLNENDDVSLEYLHGAFKRDKKDGFQKSSEHALFSNSVVDVFTQLTQCFDVVGKLECPDPEIWKRYMRRFAKTIVKVLIAYADIVKLEFPEHMKDERIACILMNNIQQLRVQLEKMFESMGGDKLEEDAANILKELQQNLNSALDDLASQFAISLEPRITQSVRELGDMLLSIKGGSGTLAAGNLAAQRNAVAVEADEVLRPLMDLLDGSLTLYAQSCEKTVLKRLLKELWKIVMRILEKTIVLPPMTDKTMMFKHLTDNAKNLASNAKIEDMGRLFKSHMAGKQDVKSALSGVMDISKEVEKNLSPKQCAVLDVALDTIKQYFHAGGNGLKKTFLEKSPELQSLRYALSLYTQMTDTLIKTFISSQVHEVDLENSEESVGEISVQIDLFSHPGTGEHKVNVKVVAANDLKWQIPSGMFRPFVDINLIGPHLQKKKRKFATKSKSNNWSPKYNESFSFTIGNEEQLDFFELHICVEDYCFARDDRLVGVAVIPLKDISEKGSVACWLPLMRRIEMDETGWTILRILS
Protein: Myosin light chain 12A (A0A8I5ZXA1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSSKRAKTKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASMGKNPTDEYLDAMMNEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEAIGTIQEDYLRELLTTMGDRFTDEEVDELYREAPIDKKGNFNYIEFTRILKHRSHALAFLPFAFLVLYLFSATLGHVYLYHQTGNGTFCHCSMRT
Protein: GLH-binding kinase 1 (EC 2.7.11.24) (O44408)
Organism: Caenorhabditis elegans
Function: Mitogen-activated protein kinase which is an essential component of the JNK pathway composed of mlk-1, mek-1 and kgb-1. Phosphorylates the transcription factor fos-1 which prevents fos-1 dimerization and promoter binding and results in activation of target genes including F53A9.2/kreg-1 and lys-3/kreg-2. Phosphorylates jun-1 and activates the AP-1 transcription factor which is a heterodimer of jun-1 and fos-1. Phosphorylates glh-1 in vitro which may play a role in controlling glh-1 protein levels in the germline by targeting it for degradation by the proteasome. Required for oogenesis and probably also for spermatogenesis. Involved in the response to environmental stress such as heavy metals, infection and protein folding stress in an age-dependent manner. In larvae, has a protective role which becomes detrimental in adults. May control susceptibility to infection, heavy metal stress and premature lethality by regulating daf-16 cellular localization. Involved in the transcriptional response to bacterial pore-forming toxins and to fasting. Required for fasting-induced longevity. Involved in axon regeneration after injury downstream of tyrosine receptor svh-2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17699606}. Note=Uniformly cytoplasmic in distal germline but resolves into discrete particles in developing oocytes. {ECO:0000269|PubMed:17699606}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase mek-1
- Tyrosine-protein phosphatase vhp-1
- Transcription factor fos-1
- Dual specificity mitogen-activated protein kinase kinase jkk-1
- MAP kinase kinase mkk-4
- Forkhead box protein O
- mitogen-activated protein kinase kinase
- mitogen-activated protein kinase kinase
- Transcription factor jun-1
- Protein kinase C-like 1
Sequence:
MEVDLPVHNEYDASRFHQVTIRDPIAGADSTFTIPTRYVNLSFLNAGAQGTVVMADDLVTTQRVAIKKMQQPFVMTMSAKRAYREFILLTTIKHPNIIRLLNAFTPDTSLSTFREVYLVMELMTHNLHEVIHRLRLDHKTLSFFVYQSLCAIKHLHNSGVIHRDLKPSNIVVNDRCVLKVLDFGLARKKNVDTSMRMSDYVVTRYYRAPEVILGLPYSEKVDIWSVGCIFAEMINHTVLFPGKDRIDQWTKIYSVLGTPDDHFISQLGQSAAMYVRSLPRHQARAFSEIVPDTNFLPETENPRVHLTPHVARDLLFNMLKINPEERYSVEDALNHPYVKLWFKDDEVNAPASENRYDQEIDFADKTLIEWKELIFNEVQRYQADHDIFTG
Protein: GRAS family protein TF80 (G7J1L1)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:G7L166}.
Interaction partners:
Sequence:
MDSGSPYHWLRELRYDSHGSNPMIPLIECAKCVASGSIKTADIGLEYISQISSPHGNGVQRMVTYFSEALGYKIVKHLPGVYKALNSSKISLSSDDILVQKYFYDLCPFLKFSYLITNQAIIESMEREKVVHIIDLHCSEPAQWINLIQTLKKRPGGPPFLKITGINEKKEALEQMSFHLTTEAGILDFPLQFNPIISKLEDVDFENLPVKTGDAVAISSVLQLHSLLATDDEMVSSSGAASFNMQRAAHLGQRTFAEWLERDMINAYILSPDSALSPLFLGASPKMGIFLNAMRKLQPKLLVITEQESNLNGCNLTERIDRALYFYGSLFDCLESTVTRTSVERQKLESMLLGEQIKNIITCEGVDRKERHEKLEQWIQRLKMAGFVKVPLSYNGRIEATNLLQRYSHKYKFKEENDCLLVCWSDRPLFSVSAWKFR
Protein: Ephrin-4 (Protein male abnormal 26) (O44516)
Organism: Caenorhabditis elegans
Function: Regulates the formation or stabilization of cell-cell contacts at several stages of epithelial morphogenesis. In early embryonic development, involved in ventral closure of the epidermis. During male tail morphogenesis, regulates precursor cell sorting together with mab-20 and allows the formation of distinct sensory rays. Probably acts as a ligand for lad-2 to regulate axon guidance of several neurons including SDQL, SDQR, SMD and PLN neurons during neurogenesis.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Ephrin receptor 1
- Semaphorin-2A
- Plexin-2
- Sema domain-containing protein
- Protein sax-3
- Tyrosine-protein phosphatase Lar-like
Sequence:
MKQFFEFLITTFLLLGLAAADEHIVYWNSTNSLFRNRQPTIEVRMGDVVRFVCPDNEEGRNDGEYLIVYEVTEFAMDDCALESHSREVIRCAPEGTAEKVLRTQQLSGGRREDWKKQKVPPKNVAQLIRQLNPIPNGKEYQPGQTYYYMTTSTGKANGTNHRMYGLCESQNMRLSMKVSASQPHPTRRAPTRRQEDFVTTASAELMGGQEDEDSDNDNAHLLPRDLEGSTNPKFRRPSQLETAGVENQQFMKVVQMAQAGKTGTFENEKEAIAQKSSEKDGWHPVNVQYVADLMNNAYQNADERISYQRDFEIHEENDLAVKSLEYSSSSTSLSTNFAILLAVIYVLY
Protein: Putative calcium P-type ATPase (Q9UUY0)
Organism: Neurospora crassa
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEAAFAKPVDEVLSTFGVDPTTGLSDEQVAQSRAKYGRNAIPEEPPTPIWELILEQFKDQLVLILLGSAAISFVLALFEDEGGWSAFVDPAVIITILVLNAVVGVSQESSAEKAIAALQEYSANEANVVRNGQITRIKAEDLVPGDVVDIAVGARVPADCRLISIESNSFAVDQAILTGESESVGKDFQAVVSDDKAVLQDQVNMLFSGTTVVTGHAKAVVVLTGSNTAIGDIHESITAQISEPTPLKQKLNDFGDQLAKVITVICVLVWLINIPNFADPSHGNWTKGAIYYLKIAVSLGVAAIPEGLAVVITTCLALGTRKMAAKNAVVRSLPSVETLGSCSVICSDKTGTLTTNQMSVNKIVHFNQDGTDLEELDVEGTTFEPKGAIMSQGKKVTDLAQNSATILQLTEVAALCNDARLDYHPSTGTFSNVGEATEGALRVLTEKIGPCAPSDCPPKDRVHYASSWYEKQYQRLATYEFSRDRKSMSVLVERDGQQKLLVKGAPESLIERCTHALLGPDGKKVPLDSNMSELLMKEVVEYGNRGLRVIALASLDNVAGNPLLHTAKSTAEYASLEQNLTLIGLVGMLDPPRPEVAASIKKCKDAGIRVVVITGDNRNTAESICRQIGVFGSNEDLTGKSYTGREFDNLTPSEQLEAAKTASLFSRVEPTHKSKLVDLLQSLGEVVAMTGDGVNDAPALKKADIGVAMGSGTDVSKLAADMVLADDNFATIEVAIEEGRAIYNNTQQFIRYLISSNIGEVVSIFLTAALGMPEALIPVQLLWVNLVTDGLPATALSFNPPDHDIMRRNPRKRDEALIGGWLFFRYLVIGTYVGLATVAGYAWWFMFYSEGPQISFYQLSHFHRCSTEFPEIGCAMFSNDMAKAGSTVSLSILVVIEMFNAMNALSSSESLLTLPVWKNMMLVYAIGLSMALHFALLYTPILQTLFSILPMNWAEWKAVIVISAPVVLLDELLKAVERKYFVQSTPSSTSSDKKKDL
Protein: Phosphatidylcholine transfer protein (PC-TP) (START domain-containing protein 2) (StARD2) (StAR-related lipid transfer protein 2) (P53808)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of phosphatidylcholine between membranes. Binds a single lipid molecule.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10500206}.
Interaction partners:
- Acyl-coenzyme A thioesterase 13
- StAR-related lipid transfer protein 3
- StAR-related lipid transfer protein 4
- StAR-related lipid transfer protein 5
- StAR-related lipid transfer protein 6
Sequence:
MAGAACCFSDEQFREACAELQKPALTGADWQLLVEASGITIYRLLDQPSGLYEYKVFGVLEGCSPALLTDVYMDLDYRKQWDQYVKELYEKESDEQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDRRKIYVVLAQSISAPQFPEKSGVIRVKQYKQSLAIESDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPNFLKDMVKACQNYHKKT
Protein: Caprin-2 (C1q domain-containing protein 1) (Cytoplasmic activation/proliferation-associated protein 2) (RNA granule protein 140) (Q05A80)
Organism: Mus musculus (Mouse)
Function: Promotes phosphorylation of the Wnt coreceptor LRP6, leading to increased activity of the canonical Wnt signaling pathway (By similarity). Facilitates constitutive LRP6 phosphorylation by CDK14/CCNY during G2/M stage of the cell cycle, which may potentiate cells for Wnt signaling (By similarity). May regulate the transport and translation of mRNAs, modulating for instance the expression of proteins involved in synaptic plasticity in neurons. Involved in regulation of growth as erythroblasts shift from a highly proliferative state towards their terminal phase of differentiation (By similarity). May be involved in apoptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6IMN6}. Cell membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IMN6}.
Interaction partners:
Sequence:
MKSAKSQVNQDQQGENQRALSPLQSTLSSAASPSQAYETYIDNGLICLKHKIRNIEKKKLKLEDYKDRLKNGEQLNPDQLEAVEKYEEVLHNLEFAKELQKTFSALSQDLLKAQKKAQRREHMLKLETEKKKLRTMLQIQYVLQNLTQEHVQKDFKGGLNGAMYLPSKELDYLIKFSKLTCPERNESLSVEDQMEQSSLYFWDLLEGSEKTVVGTTYKHVKDLLSKLLHSGYFESVPVLRNSKEKAEEVLMQSEMKKQLLKSESIKESESLTELVQPEIQPQEFLNRRYMTEVKFSRKQENVEQSWEADYARKPSLLKCWNTLPEPDGQEKKKESLESWKSSLKTQEVSKPVVSLVQGKLRPTLQEEQKQQVPITPVSQWKPESPKSKVGSPQEEQNVQETPKPWVVQSQKEQDPKKLPPGSWAVSVQSEQSGSRSWTTPVCREQASVQPGTPVSWENNAENQKHSLVPQSQISLKSWGAASAGLLPNGQVLTRKLNVEPKDVPKPLPQPIDSSSALPKDPVLRKEKLQDLMSQIQGTYNFMQESVLDFDKPSSAIPSSQPPSACPVSTVSAEQNLSNQSDFLQEPSQASSPVTCSSNACLVTTDQASSGSETEFTTSETPEMVVSPCKPKPASALASPNPPLSKSFQLPPASGSSEAISTAPFQAMQTVFNVNAPLPPRKEQEMKEPPYSSGYNQNFTSSSTQTVSQCQLPAVHIDQTTQPPETGAGYHPDGTVQVSNGSLAFYPAPTSMFPRPAQPFISSRGTLRGCSHGGRLLMSSYQSPGGYKGFDSYRGLPSVSSGNYSQLQLQAREYSGTAYSQRDNFQQCYKRSGTSSGLQANSRAGWSDSSQVSSPERDSETFNSGDSGLGDSRSMTPVDVPVTSPAAAILPVHIYPLPQQMRVAFSAARTSNLAPGTLDQPIVFDLLLNNLGETFDLQLGRFNCPVNGTYVFIFHMLKLAVNVPLYVNLMKNEEVLVSAYANDGAPDHETASNHAVLQLLQGDQIWLRLHRGAIYGSSWKYSTFSGYLLYQD
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A (Oligosaccharyl transferase subunit STT3A) (STT3-A) (EC 2.4.99.18) (Integral membrane protein 1) (Protein STAUROSPORIN AND TEMPERATURE SENSITIVE 3-LIKE A) (Q93ZY3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets (By similarity). Controls adaptive responses to salt/osmotic stress. Acts as a key glycosylation determinant for EFR function during plant innate immunity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22923678}; Multi-pass membrane protein {ECO:0000269|PubMed:22923678}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD2
- Probable dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dol-P-Glc:Glc
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
Sequence:
MAALESPLPGTPTAMRNAFGNVLSVLILVLIGVLAFSIRLFSVIKYESVIHEFDPYFNYRVTQFLSKNGIYEFWNWFDDRTWYPLGRVIGGTVYPGLTLTAGTIWWGLNSLNIPLSVETVCVFTAPVFSAFASWATYLLTKEVKGSGAGLAAAALLAMVPSYISRSVAGSYDNEAVAIFALIFTFYLYIKTLNTGSLFYATLNALAYFYMVCSWGGYTFIINLIPMHVLLCIVTGRYSPRLYIAYAPLVVLGTLLAALVPVVGFNAVLTSEHFASFLVFIIIHVVALVYYIKGILSPKMFKVAVTLVVSIGMVVCFIVVAILVALVASSPTGGWSGRSLSLLDPTYASKYIPIIASVSEHQPPTWPSYFMDINVLAFLVPAGIIACFSPLSDASSFVVLYIVMSVYFSGVMVRLMLVLAPAACIMSGIALSQAFDVFTGSIKYQLGASSNSTDDAEDNTSTNNAPKDDVSAGKTDKGEEIVKERSSKKGKKKEREPADKPSVKAKIKKKALVLPLEASIVALLLLIMLGAFYVIHCVWAAAEAYSAPSIVLTSQSRDGLHVFDDFRESYAWLSHNTDVDDKVASWWDYGYQTTAMANRTVIVDNNTWNNTHIATVGTAMSSPEKAAWEIFNSLDVKYVLVVFGGLIGYPSDDINKFLWMVRIGGGVFPHIKEADYLRDGQYRIDSEATPTMLNSLMYKLSYYRFVETDGKGYDRVRRTEIGKKHFKLTHFEEVFTSHHWMVRLYKLKPPRNRIRGKAKKLKSKTSSGLSSKSAKKNPWV
Protein: Undecaprenyl-diphosphatase (EC 3.6.1.27) (Bacitracin resistance protein) (Undecaprenyl pyrophosphate phosphatase) (P60932)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15138271, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15138271, ECO:0000269|PubMed:15919996}.
Interaction partners:
- Putative undecaprenyl-diphosphatase YbjG
- Ditrans,polycis-undecaprenyl-diphosphate synthase
- Phospho-N-acetylmuramoyl-pentapeptide-transferase
- Phosphatidylglycerophosphatase B
- Lipid A 1-diphosphate synthase
- Penicillin-binding protein 1B
- UDP-N-acetylglucosamine--N-acetylmuramyl-
Sequence:
MSDMHSLLIAAILGVVEGLTEFLPVSSTGHMIIVGHLLGFEGDTAKTFEVVIQLGSILAVVVMFWRRLFGLIGIHFGRPLQHEGESKGRLTLIHILLGMIPAVVLGLLFHDTIKSLFNPINVMYALVVGGLLLIAAECLKPKEPRAPGLDDMTYRQAFMIGCFQCLALWPGFSRSGATISGGMLMGVSRYAASEFSFLLAVPMMMGATALDLYKSWGFLTSGDIPMFAVGFITAFVVALIAIKTFLQLIKRISFIPFAIYRFIVAAAVYVVFF
Protein: Probable aspartic protease At2g35615 (EC 3.4.-.-) (Q3EBM5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}. Note=Prediction of a peroxisomal location. {ECO:0000269|PubMed:15333753}.
Interaction partners:
- GTP-binding protein-like protein
- Translation initiation factor eIF2 assembly protein
- Inner centromere protein, ARK-binding region protein
- Egg cell-secreted protein 1.5
- Transcription factor MYB98
Sequence:
MATQILLCFFLFFSVTLSSSGHPKNFSVELIHRDSPLSPIYNPQITVTDRLNAAFLRSVSRSRRFNHQLSQTDLQSGLIGADGEFFMSITIGTPPIKVFAIADTGSDLTWVQCKPCQQCYKENGPIFDKKKSSTYKSEPCDSRNCQALSSTERGCDESNNICKYRYSYGDQSFSKGDVATETVSIDSASGSPVSFPGTVFGCGYNNGGTFDETGSGIIGLGGGHLSLISQLGSSISKKFSYCLSHKSATTNGTSVINLGTNSIPSSLSKDSGVVSTPLVDKEPLTYYYLTLEAISVGKKKIPYTGSSYNPNDDGILSETSGNIIIDSGTTLTLLEAGFFDKFSSAVEESVTGAKRVSDPQGLLSHCFKSGSAEIGLPEITVHFTGADVRLSPINAFVKLSEDMVCLSMVPTTEVAIYGNFAQMDFLVGYDLETRTVSFQHMDCSANL
Protein: 1,4-alpha-glucan branching enzyme (EC 2.4.1.18) (A1Z992)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glycogen phosphorylase
- Glycogen [starch] synthase
- Glycogen debranching enzyme
- Phosphoglucomutase 1
- Alpha-amylase-related protein
- Alpha-amylase B
- ATP synthase subunit beta, mitochondrial
- UTP--glucose-1-phosphate uridylyltransferase
- glycogenin glucosyltransferase
- Glucose-6-phosphate isomerase
Sequence:
MAEAKDIEKLFETDGYLRPFEHEIRRRHGVLEDWLNKINQSEGGLDGFSTAYKHYGLHFQPDNSVIAREWAPGARDVYLTGDFNNWHWESHPFKKLDFGKWELHLPPNEDGSPAIKHLSEIKIIIRNHSGQLLDRLSPWAKYVVQPPKSANQGVNYKQYVWEPPSYERYQRQHPGPPRPKSLRIYECHVGIASQEPRVGSYDEFADRIVPRIKRQGYNCIQVMAIMEHAYYASFGYQVTSFYAASSRYGNPEQLKRMIDVAHSHGLFVLLDVVHSHASKNVQDGLNQFDGTNSCFFHDGARGEHSLWDSRLFNYVEYEVLRFLLSNLRWWHDEYNFDGYRFDGVTSMLYHSRGIGEGFSGDYNEYFGLNVDTDALNYLGLANHLLHTIDSRIITIAEDVSGMPTLCRPVSEGGIGFDYRLGMAIPDKWIELLKEQSDDEWDMGNLVHTLTNRRWMENTVAYAESHDQALVGDKTIAFWLMDKEMYTHMSTLSDSSVIIDRGLALHKMIRLITHALGGEAYLNFMGNEFGHPEWLDFPRVGNNDSYHYARRQWNLVDDDLLKYKYLNEFDRAMNEAEERYGWLHSGPAWVSWKHEGDKIIAFERAGLVFVFNFHPQQSFTGYRVGTNWAGTYQAVLSSDDPLFGGHNRIDANCKHPSNPEGYAGRSNFIEVYTPSRTAVVYARVSD
Protein: Globin-1 (Dimeric hemoglobin) (Globin I) (HbI) (P02213)
Organism: Anadara inaequivalvis (Inequivalve ark) (Scapharca inaequivalvis)
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
PSVYDAAAQLTADVKKDLRDSWKVIGSDKKGNGVALMTTLFADNQETIGYFKRLGDVSQGMANDKLRGHSITLMYALQNFIDQLDNPDDLVCVVEKFAVNHITRKISAAEFGKINGPIKKVLASKNFGDKYANAWAKLVAVVQAAL