wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS2z (40S ribosomal protein Sa-1) (Laminin receptor homolog) (p40) (Q08682)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits.
Subcellular location: Cytoplasm.
Interaction partners:
- Small ribosomal subunit protein eS26x
- Small ribosomal subunit protein eS28z/eS28y
- Small ribosomal subunit protein eS12z
- Small ribosomal subunit protein uS4z
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS24z
- Small ribosomal subunit protein eS21z
- Small ribosomal subunit protein eS1z
- Probable elongation factor 1-gamma 2
- Small ribosomal subunit protein eS6y
Sequence:
MATNGSASSAQLSQKEADVRMMCAAEVHLGTKNCNYQMERYVFKRRNDGIYIFNLGKTWEKLQMAARVIVAIENPQDIIVQSARPYGQRAVLKFAQYTGANAIAGRHTPGTFTNQMQTSFSEPRLLILTDPRTDHQPIKEGALGNIPIIAFCDTDSPMRFVDIGIPANNKGKHSIGCLFWLLARMVLQMRGTIAAGQKWDVMVDLFFYREPEETKPEDEDEAGPQAEYGALPAPEYGMVGGDQWTTAQIPDAAWPGEGQAPISAAPAAASWSDSAAAPADGGWEAAAPPSGAPAAGWE
Protein: N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase 2 (EC 2.4.1.149) (Beta-1,3-N-acetylglucosaminyltransferase 1) (BGnT-1) (Beta-1,3-Gn-T1) (Beta3Gn-T1) (Beta-1,3-galactosyltransferase 7) (Beta-1,3-GalTase 7) (Beta3Gal-T7) (Beta3GalT7) (b3Gal-T7) (Beta-3-Gx-T7) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 7) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2) (BGnT-2) (Beta-1,3-Gn-T2) (Beta-1,3-N-acetylglucosaminyltransferase 2) (Beta3Gn-T2) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 7) (Q9NY97)
Organism: Homo sapiens (Human)
Function: Beta-1,3-N-acetylglucosaminyltransferase involved in the synthesis of poly-N-acetyllactosamine. Catalyzes the initiation and elongation of poly-N-acetyllactosamine chains. Shows a marked preference for Gal(beta1-4)Glc(NAc)-based acceptors. Probably constitutes the main polylactosamine synthase.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 4
- Beta-1,4-galactosyltransferase 3
- Galactoside alpha-
- Type 2 lactosamine alpha-2,3-sialyltransferase
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase FUT5
- 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
- Galactoside alpha-
Sequence:
MSVGRRRIKLLGILMMANVFIYFIMEVSKSSSQEKNGKGEVIIPKEKFWKISTPPEAYWNREQEKLNRQYNPILSMLTNQTGEAGRLSNISHLNYCEPDLRVTSVVTGFNNLPDRFKDFLLYLRCRNYSLLIDQPDKCAKKPFLLLAIKSLTPHFARRQAIRESWGQESNAGNQTVVRVFLLGQTPPEDNHPDLSDMLKFESEKHQDILMWNYRDTFFNLSLKEVLFLRWVSTSCPDTEFVFKGDDDVFVNTHHILNYLNSLSKTKAKDLFIGDVIHNAGPHRDKKLKYYIPEVVYSGLYPPYAGGGGFLYSGHLALRLYHITDQVHLYPIDDVYTGMCLQKLGLVPEKHKGFRTFDIEEKNKNNICSYVDLMLVHSRKPQEMIDIWSQLQSAHLKC
Protein: Bidirectional sugar transporter SWEET11 (AtSWEET11) (Protein SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTERS 11) (Q9SMM5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane. Involved in phloem loading by mediating export from parenchyma cells feeding H(+)-coupled import into the sieve element/companion cell complex, thus contributing to the sucrose migration from sites of synthesis in the mesophyll to the phloem. Contributes to seed filling by triggering sucrose efflux involved in the transfer of sugars from seed coat to embryos.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22157085, ECO:0000269|PubMed:24027245, ECO:0000269|PubMed:25794936}; Multi-pass membrane protein {ECO:0000250}. Note=Present in the plasma membrane of the phloem. {ECO:0000269|PubMed:22157085}.
Interaction partners:
- Sucrose transport protein SUC2
- Sucrose transport protein SUC3
- Sucrose transport protein SUC4
- At2g39500/F12L6.16
- Sucrose transport protein SUC5
- Sugar transport protein 1
Sequence:
MSLFNTENTWAFVFGLLGNLISFAVFLSPVPTFYRIWKKKTTEGFQSIPYVVALFSATLWLYYATQKKDVFLLVTINAFGCFIETIYISMFLAYAPKPARMLTVKMLLLMNFGGFCAILLLCQFLVKGATRAKIIGGICVGFSVCVFAAPLSIIRTVIKTRSVEYMPFSLSLTLTISAVIWLLYGLALKDIYVAFPNVLGFALGALQMILYVVYKYCKTSPHLGEKEVEAAKLPEVSLDMLKLGTVSSPEPISVVRQANKCTCGNDRRAEIEDGQTPKHGKQSSSAAAT
Protein: small monomeric GTPase (EC 3.6.5.2) (C0H8F9)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWSSCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKTRKKSNCQLL
Protein: Tyrosine specific protein phosphatases domain-containing protein (Q385Z9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MMGDDDRKLNEQQMQLVKGLLESQRRDSIVDVSDAVNSTFFKEEVDCPTASTGGVFLTSAAGAKSGNLTERLLFHEAASPVECSIGGEQTGTVASPRDRWIRGVLITSSTPLMPKESVFVDERSNSRMLFENTPLAQLKLRVVPVSLPTFVPNSDRNLTAAGGGRNLREILEEYERTFLRSLLVCISSLLRRRVALERAEKSVAGSEGDNNGSDCNTVTSPLREEEFFFDGELPVLSVPIYYFAISMEDNATSRIADVVDVVEDFMHLLIDAATSVVMETTVILQCLVHIANTVGANGSQLSENVSEPNDAAAKEALVALHRLTEVMVKKTREKQEPRGAVKTAAARNDDCTEAAEQISSNVAWPARGDGFQPLVLLLGNDLEPSDFLRATLCVLPGVLVHCLKGVSRSPSIIMAYYIRRCAGRIRTPLQQVVEGERGSLHSDDPTNNAAPSGDESGNGDMHVFSFSSLLQCLQRARPVVNPQVCFLAELRSMWMRITRERLNYGERNS
Protein: Salicylate synthase (Chorismate mutase) (CM) (EC 5.4.99.5) (Isochorismate synthase/isochorismate lyase) (EC 4.2.99.21, EC 5.4.4.2) (Mycobactin synthase protein) (P9WFX1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the incorporation of salicylate into the virulence-conferring salicylate-based siderophore mycobactin. Catalyzes the initial conversion of chorismate to yield the intermediate isochorismate (isochorismate synthase activity), and the subsequent elimination of the enolpyruvyl side chain to give salicylate (isochorismate pyruvate-lyase activity). In the absence of magnesium, MbtI displays a chorismate mutase activity and converts chorismate to prephenate.
Interaction partners:
- Salicyl-AMP ligase / salicyl-S-ArCP synthetase
- Phenyloxazoline synthase MbtB
- Anthranilate synthase component 2
- Anthranilate phosphoribosyltransferase
- Polyketide synthetase MbtC
- Indole-3-glycerol phosphate synthase
- Acetyl hydrolase MbtJ
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
- Chorismate synthase
Sequence:
MSELSVATGAVSTASSSIPMPAGVNPADLAAELAAVVTESVDEDYLLYECDGQWVLAAGVQAMVELDSDELRVIRDGVTRRQQWSGRPGAALGEAVDRLLLETDQAFGWVAFEFGVHRYGLQQRLAPHTPLARVFSPRTRIMVSEKEIRLFDAGIRHREAIDRLLATGVREVPQSRSVDVSDDPSGFRRRVAVAVDEIAAGRYHKVILSRCVEVPFAIDFPLTYRLGRRHNTPVRSFLLQLGGIRALGYSPELVTAVRADGVVITEPLAGTRALGRGPAIDRLARDDLESNSKEIVEHAISVRSSLEEITDIAEPGSAAVIDFMTVRERGSVQHLGSTIRARLDPSSDRMAALEALFPAVTASGIPKAAGVEAIFRLDECPRGLYSGAVVMLSADGGLDAALTLRAAYQVGGRTWLRAGAGIIEESEPEREFEETCEKLSTLTPYLVARQ
Protein: Invertase 2 (EC 3.2.1.26) (Beta-fructofuranosidase 2) (Saccharase) (P00724)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: [Isoform Intracellular]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Secreted]: Secreted.
Interaction partners:
- Hexokinase-1
- Hexokinase-2
- Glucokinase-1
- Alpha-glucosidase MAL12
- Putative glucokinase-2
- N-acetylglucosamine kinase
- Alpha-glucosidase MAL32
- Oligo-1,6-glucosidase IMA1
- Oligo-1,6-glucosidase IMA5
- Oligo-1,6-glucosidase IMA2
Sequence:
MLLQAFLFLLAGFAAKISASMTNETSDRPLVHFTPNKGWMNDPNGLWYDEKDAKWHLYFQYNPNDTVWGTPLFWGHATSDDLTNWEDQPIAIAPKRNDSGAFSGSMVVDYNNTSGFFNDTIDPRQRCVAIWTYNTPESEEQYISYSLDGGYTFTEYQKNPVLAANSTQFRDPKVFWYEPSQKWIMTAAKSQDYKIEIYSSDDLKSWKLESAFANEGFLGYQYECPGLIEVPTEQDPSKSYWVMFISINPGAPAGGSFNQYFVGSFNGTHFEAFDNQSRVVDFGKDYYALQTFFNTDPTYGSALGIAWASNWEYSAFVPTNPWRSSMSLVRKFSLNTEYQANPETELINLKAEPILNISNAGPWSRFATNTTLTKANSYNVDLSNSTGTLEFELVYAVNTTQTISKSVFADLSLWFKGLEDPEEYLRMGFEVSASSFFLDRGNSKVKFVKENPYFTNRMSVNNQPFKSENDLSYYKVYGLLDQNILELYFNDGDVVSTNTYFMTTGNALGSVNMTTGVDNLFYIDKFQVREVK
Protein: Spermine synthase (SPMSY) (EC 2.5.1.22) (Spermidine aminopropyltransferase) (P97355)
Organism: Mus musculus (Mouse)
Function: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM). Required for normal viability, growth and fertility.
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme 1
- S-adenosylmethionine decarboxylase proenzyme 2
- Spermidine synthase
- S-methyl-5'-thioadenosine phosphorylase
- Ornithine decarboxylase
- Peroxisomal N
- Gene model 853
- Spermine oxidase
- Guanidino acid hydrolase, mitochondrial
- Deoxyhypusine synthase
Sequence:
MAAARHSTLDFKLGAKADGEAILKGLQSIFQEQGMTESVHTWQDHGYLATYTNKNGSFANLRIYPHGLVLLDLQSYDSDVQGKQETDSLLNKIEEKMKELSQDSTGRVKRLPPIVRGGAIDRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAIMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRRTCGDVLDNLRGDCYQVLIEDCIPVLKMYAKEGREFDYVINDLTAVPISTSPEEDSTWDFLRLILDLSMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVWKKAKP
Protein: Zinc finger CCCH domain-containing protein 14 (Mammalian suppressor of tau pathology-2) (MSUT-2) (Renal carcinoma antigen NY-REN-37) (Q6PJT7)
Organism: Homo sapiens (Human)
Function: Involved in poly(A) tail length control in neuronal cells. Binds the polyadenosine RNA oligonucleotides.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:17630287, ECO:0000269|PubMed:19303045, ECO:0000269|PubMed:24671764, ECO:0000269|PubMed:27563065, ECO:0000269|PubMed:39461343}. Note=Colocalizes with poly(A) RNA in nuclear speckles. {ECO:0000250|UniProtKB:Q7TMD5}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus speckle {ECO:0000269|PubMed:19303045}.; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus speckle {ECO:0000269|PubMed:19303045}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000269|PubMed:21734151}.
Interaction partners:
- Polyadenylate-binding protein 2
- THO complex subunit 4
- Protein Hook homolog 2
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein subunit 2-like
- NGFI-A-binding protein 2
- RNA-binding protein Musashi homolog 2
- DAZ-associated protein 1
- RNA-binding protein Musashi homolog 1
- Spliceosome RNA helicase DDX39B
Sequence:
MEIGTEISRKIRSAIKGKLQELGAYVDEELPDYIMVMVANKKSQDQMTEDLSLFLGNNTIRFTVWLHGVLDKLRSVTTEPSSLKSSDTNIFDSNVPSNKSNFSRGDERRHEAAVPPLAIPSARPEKRDSRVSTSSQESKTTNVRQTYDDGAATRLMSTVKPLREPAPSEDVIDIKPEPDDLIDEDLNFVQENPLSQKKPTVTLTYGSSRPSIEIYRPPASRNADSGVHLNRLQFQQQQNSIHAAKQLDMQSSWVYETGRLCEPEVLNSLEETYSPFFRNNSEKMSMEDENFRKRKLPVVSSVVKVKKFNHDGEEEEEDDDYGSRTGSISSSVSVPAKPERRPSLPPSKQANKNLILKAISEAQESVTKTTNYSTVPQKQTLPVAPRTRTSQEELLAEVVQGQSRTPRISPPIKEEETKGDSVEKNQGTQQRQLLSRLQIDPVMAETLQMSQDYYDMESMVHADTRSFILKKPKLSEEVVVAPNQESGMKTADSLRVLSGHLMQTRDLVQPDKPASPKFIVTLDGVPSPPGYMSDQEEDMCFEGMKPVNQTAASNKGLRGLLHPQQLHLLSRQLEDPNGSFSNAEMSELSVAQKPEKLLERCKYWPACKNGDECAYHHPISPCKAFPNCKFAEKCLFVHPNCKYDAKCTKPDCPFTHVSRRIPVLSPKPAVAPPAPPSSSQLCRYFPACKKMECPFYHPKHCRFNTQCTRPDCTFYHPTINVPPRHALKWIRPQTSE
Protein: Protein ERP5 (P38819)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in vesicular protein trafficking.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Endoplasmic reticulum vesicle protein 25
- Protein ERP3
- Endosomal protein P24B
- Protein ERP2
Sequence:
MKYNIVHGICLLFAITQAVGAVHFYAKSGETKCFYEHLSRGNLLIGDLDLYVEKDGLFEEDPESSLTITVDETFDNDHRVLNQKNSHTGDVTFTALDTGEHRFCFTPFYSKKSATLRVFIELEIGNVEALDSKKKEDMNSLKGRVGQLTQRLSSIRKEQDAIREKEAEFRNQSESANSKIMTWSVFQLLILLGTCAFQLRYLKNFFVKQKVV
Protein: Vacuolar cation-chloride cotransporter 1 (Vacuolar homolog of CCC family protein 1) (P38329)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the coordinated symport of chloride with potassium ions across the vacuolar membrane. Involved in vacuolar osmoregulation.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:23022132}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MVSRFYQIPGTHRPSSAISSSNESSSLLSARRISQTYFNYQATPECQKVSSKYDPDNPNKDKLGTYDGVFVPTALNVLSILMFLRFGFILGQLGIICTIGLLLLSYTINLLTTLSISAISTNGTVRGGGAYYMISRSLGPEFGGSIGLVFFLGQVFNAGMNAVGIIEPLLYNLGYSAQGEPPAALGELLPRGHWHEFTYATVILFLCFSVAFVGSQTVSRAGNILFLVLAASIFSIPLSALIRSPFTEGGISYTGPSWQTFHDNLLPHLTKGAAGSLLKGKETFNDLFGVFFPATAGIFAGAGMSSELRKPSKSIPKGTLWGLLFTFICYAVVVFSMGCSIPRRSLYDEVQIIQTISSVQWVIFMGEMATSLFSIIVGMLGAAYVLEAIAKDNIIPGLEIFAHSPLYSLIFTWILTQLCLFSDVNKIATFITMTFLMTFVVMNLACFLLGISSAPNFRPSFKYFNRYTTAIGALLSVVAMLIVDGISASVLFLAMILLFLFIHYFSPPKSWGDVSQSLIYHQVRKYLLRLRQDNIKYWRPQILLFVDNPRTSWNLIRFCNHLKKGGLYILGHVAVTADFPKQLNELKTQQKAWMKIRDMAAIKAFVQVGTGPSLIWGIRNVFIGSGLGGMKPNITVVGFFDLESYRKHIPQSRSQNNLQKQVEIKATVPRSTCSDVKINVPLPTDECKNETKVNVQQWVQIVEDLSLMQSNIAIAHGFKNLEIPNKRDSCFPKKTIDLYPIQMCGKVEAKGDQPAAITTNFDTYTLILQLAAILVTVPEWKRTHSLRVILFVEQEYHRTNETQRMKKLLQVLRIDAEVLVVSLDQFRVYNTIVKGDPIVFDYVNSKLADNEWWKDLVEARDTLKPKRRFSTIEPQTIAKQFTQSRKYTSGVQKLGVSFTMNTRMPTNRIDTPCESEDSDLDTDLTSIRDAFSASTNISVGKDLTTKSKTGSDRTNLLVKNLQSDVSTQSLRPVFSSNTLPRTRVVEDGTGEQPTLIPIAEPDLSNGNGTGSGIGNGNKLKKPVLPELSPCCSKDSLVTAMQNLGFNDLPSTAQHLVLNDVMTQMSKSSDLIFSTLPVPALGTHEDHDASLQYVEDLDIWLEGLPPCMLINSQTMTVTTAL
Protein: Dephosphocoenzyme A carrier, isoform D (A0A0B4LIE8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MSRLLEKPNIAMSIKSTGSQLSSTMTTASATLSSDLDDADTSRTQLSPSETSGVVLVPATTVTPMRQKIDQVVISLISGAAAGALAKTVIAPLDRTKINFQIRNDVPFSFRASLRYLQNTYANEGVLALWRGNSATMARIVPYAAIQFTAHEQWRRILHVDKDGTNTKGRRFLAGSLAGITSQSLTYPLDLARARMAVTDRYTGYRTLRQVFTKIWVEEGPRTLFRGYWATVLGVIPYAGTSFFTYETLKREYYVVGNNKPNTLVSLAFGAAAGAAGQTASYPLDIVRRRMQTMRVNTAGGDRYPTILETLVKIYREEGVKNGFYKGLSMNWIKGPIAVGISFSTYDLIKAWLTELANLRRVEK
Protein: Indole-3-acetic acid-amido synthetase GH3.5 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 5) (AtGH3-5) (O81829)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin. Strongly reactive with Glu, Gln, Trp, Asp, Ala, Leu, Phe, Gly, Tyr, Met, Ile and Val. Little or no product formation with His, Ser, Thr, Arg, Lys, or Cys. Also active on pyruvic and butyric acid analogs of IAA, PAA and the synthetic auxin naphthaleneacetic acid (NAA). The two chlorinated synthetic auxin herbicides 2,4-D and 3,6-dichloro-o-anisic acid (dicamba) cannot be used as substrates.
Interaction partners:
- Auxin response factor 8
- Auxin response factor 17
- Auxin transporter protein 1
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin-responsive protein IAA2
- Auxin-responsive protein IAA17
- At1g09520/F14J9_18
Sequence:
MPEAPKKESLEVFDLTLDQKNKQKLQLIEELTSNADQVQRQVLEEILTRNADVEYLRRHDLNGRTDRETFKNIMPVITYEDIEPEINRIANGDKSPILSSKPISEFLTSSGTSGGERKLMPTIEEELDRRSLLYSLLMPVMSQFVPGLENGKGMYFLFIKSESKTPGGLPARPVLTSYYKSSHFKERPYDPYTNYTSPNETILCSDSYQSMYSQMLCGLCQHQEVLRVGAVFASGFIRAIKFLEKHWIELVRDIRTGTLSSLITDPSVREAVAKILKPSPKLADFVEFECKKSSWQGIITRLWPNTKYVDVIVTGTMSQYIPTLDYYSNGLPLVCTMYASSECYFGVNLRPLCKPSEVSYTLIPSMAYFEFLPVHRNNGVTNSINLPKALTEKEQQELVDLVDVKLGQEYELVVTTYAGLCRYRVGDLLRVTGFKNKAPQFSFICRKNVVLSIDSDKTDEVELQNAVKNAVTHLVPFDASLSEYTSYADTSSIPGHYVLFWELCLDGNTPIPPSVFEDCCLAVEESFNTVYRQGRVSDKSIGPLEIKIVEPGTFDKLMDYAISLGASINQYKTPRCVKFAPIIELLNSRVVDSYFSPKCPKWVPGHKQWGSN
Protein: Cell growth-regulated gene 1 protein (P56553)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Involved in the cell growth regulation.
Interaction partners:
Sequence:
MSLTITKDNIFPKGYRGRLTEGVTYDERNNTLLWVDIIQGEVHRVFLDNTNINTNTSSSSHETLKWDSSNESIGAICLTNDPNKLIICSKYGLAYGDFSSSTIEYFFKYPHTTNPDEKLRLRSNDGIIDPWGNLWIGVMNDFPIGAKEGIQPEGKLYRIGFSKESNKLTCDVMIENSLISNGLCFNNQGDEFYWTDSLTFKIWKYDYDKTTNKLTNKSVFIDLKQFYPDVEQPEPDGLVMTNNGEIYTCVFSTGTILHVDNQGKEIERIKIAAKRPTCVTIGSGIKNNEMFVTTGHLKLDDEKATIDAINLDGDLGGFLFKLKVDKDLNGQKKNIWGGKV
Protein: Integral membrane protein 2C (Cerebral protein 14) (Transmembrane protein BRI3) [Cleaved into: CT-BRI3] (Q9NQX7)
Organism: Homo sapiens (Human)
Function: Negative regulator of amyloid-beta peptide production. May inhibit the processing of APP by blocking its access to alpha- and beta-secretase. Binding to the beta-secretase-cleaved APP C-terminal fragment is negligible, suggesting that ITM2C is a poor gamma-secretase cleavage inhibitor. May play a role in TNF-induced cell death and neuronal differentiation (By similarity).
Subcellular location: Lysosome membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:19114711}; Single-pass type II membrane protein {ECO:0000269|PubMed:19114711}.
Interaction partners:
- Beta-secretase 1
- Proprotein convertase subtilisin/kexin type 7
Sequence:
MVKISFQPAVAGIKGDKADKASASAPAPASATEILLTPAREEQPPQHRSKRGGSVGGVCYLSMGMVVLLMGLVFASVYIYRYFFLAQLARDNFFRCGVLYEDSLSSQVRTQMELEEDVKIYLDENYERINVPVPQFGGGDPADIIHDFQRGLTAYHDISLDKCYVIELNTTIVLPPRNFWELLMNVKRGTYLPQTYIIQEEMVVTEHVSDKEALGSFIYHLCNGKDTYRLRRRATRRRINKRGAKNCNAIRHFENTFVVETLICGVV
Protein: EH domain-binding protein 1 (G5ECW3)
Organism: Caenorhabditis elegans
Interaction partners:
- Ras-related protein Rab-10
- Dynamin-type G domain-containing protein
- Rab8
- FYVE-type domain-containing protein
- ADP-ribosylation factor 6
- Calponin-homology
- Calponin-homology
- C2 NT-type domain-containing protein
- Numb-related protein 1
- PH domain-containing protein
Sequence:
MAGILRRLRRSNKKAAKFRFTVTLQELHLYTDEQWKPENLAVSFVHRRRKVSSKERKWEECSDANKCLIMWPEQFSENIDILTTLYRIASDEYEDKEWTIVVEEVTAKGKRKAIAAVPLNVRLFILDLPDHKSELKLKLRPLTPHLKLCSLIILLGSSLISEVNADDVSITSSAAASFVEKVPVTDEVDASANDSRAAAARQQIDTTATKMMEWIKEEKEIAPPIVPAHRKPSGENENPAKVRPQWRVSAEEEKTSQPAAPAPIATNRHSRSSRASTEEKASTTIEFRVDSNSRHVPVTAIATPYYLQSGTMSRGRSNSPRAPSRDAVPQPIDGETLLSWCQRVTNGYSHVKVNDFMKSWNNGLALCAVLHSYRPDLIGDYETLDISNNMSGRISNIQRALDSLTLIGITEVPTVDMFLTPDRKQIEFLLQHLRRIFEGFDEGSTPASASDHRISRTFGINESEEKVVAMITEIRNQKDLEEAVDYRHIPDEVPVTPQLASRNPALNQPTDADDDDAETSNMRFERSNVSITMVTPGVGAIRASNRASPSKRDELRQRARDLIEKSTTPAATPNSRKASDEERRREEVRRMLNEKQHPTAIPSTSSSPYPTFRRIDGSNTDLRRIELDVHKFKKRDPSPTLVRKQYDPNDTPHVPAIGRGRTNGNRNDSSTPSSASTFDRVKRYGSMRSAELKESLQLMAKQYGYMGNDFESSSQDALATPTKKFSSQWEKDVDDVEGTANELVRIDERISDITAQADVIQDKIRETEVGSSEEEMLTASYLELTNERNTLVHRQEYYNIIETIRQVTSEIDQLGKQINEVPDDFPRSDENKTATDKLIEQYSDAMKTKSNLVQKLFATEDEIEEDSDRLKNLTLDRATRFVRGIDQPVSASKRLIQWWRR
Protein: Ankyrin repeat and LEM domain-containing protein 2 (LEM domain-containing protein 4) (Q86XL3)
Organism: Homo sapiens (Human)
Function: Involved in mitotic nuclear envelope reassembly by promoting dephosphorylation of BAF/BANF1 during mitotic exit. Coordinates the control of BAF/BANF1 dephosphorylation by inhibiting VRK1 kinase and promoting dephosphorylation of BAF/BANF1 by protein phosphatase 2A (PP2A), thereby facilitating nuclear envelope assembly. May regulate nuclear localization of VRK1 in non-dividing cells. It is unclear whether it acts as a real PP2A regulatory subunit or whether it is involved in recruitment of the PP2A complex. Involved in brain development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22770216}; Single-pass type III membrane protein {ECO:0000269|PubMed:22770216}.
Interaction partners:
- Serine/threonine-protein kinase VRK1
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein kinase VRK2
- LEM domain-containing protein 2
- Barrier-to-autointegration factor
- Inner nuclear membrane protein Man1
- Emerin
- NAD-dependent protein deacetylase sirtuin-2
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
Sequence:
MLWPRLAAAEWAALAWELLGASVLLIAVRWLVRRLGPRPGGLGRSGTPVPPPSAAAAPASGEMTMDALLARLKLLNPDDLREEIVKAGLKCGPITSTTRFIFEKKLAQALLEQGGRLSSFYHHEAGVTALSQDPQRILKPAEGNPTDQAGFSEDRDFGYSVGLNPPEEEAVTSKTCSVPPSDTDTYRAGATASKEPPLYYGVCPVYEDVPARNERIYVYENKKEALQAVKMIKGSRFKAFSTREDAEKFARGICDYFPSPSKTSLPLSPVKTAPLFSNDRLKDGLCLSESETVNKERANSYKNPRTQDLTAKLRKAVEKGEEDTFSDLIWSNPRYLIGSGDNPTIVQEGCRYNVMHVAAKENQASICQLTLDVLENPDFMRLMYPDDDEAMLQKRIRYVVDLYLNTPDKMGYDTPLHFACKFGNADVVNVLSSHHLIVKNSRNKYDKTPEDVICERSKNKSVELKERIREYLKGHYYVPLLRAEETSSPVIGELWSPDQTAEASHVSRYGGSPRDPVLTLRAFAGPLSPAKAEDFRKLWKTPPREKAGFLHHVKKSDPERGFERVGRELAHELGYPWVEYWEFLGCFVDLSSQEGLQRLEEYLTQQEIGKKAQQETGEREASCRDKATTSGSNSISVRAFLDEDDMSLEEIKNRQNAARNNSPPTVGAFGHTRCSAFPLEQEADLIEAAEPGGPHSSRNGLCHPLNHSRTLAGKRPKAPRGEEAHLPPVSDLTVEFDKLNLQNIGRSVSKTPDESTKTKDQILTSRINAVERDLLEPSPADQLGNGHRRTESEMSARIAKMSLSPSSPRHEDQLEVTREPARRLFLFGEEPSKLDQDVLAALECADVDPHQFPAVHRWKSAVLCYSPSDRQSWPSPAVKGRFKSQLPDLSGPHSYSPGRNSVAGSNPAKPGLGSPGRYSPVHGSQLRRMARLAELAAL
Protein: Chemotaxis protein MotA (Q9HUL1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004429}.
Interaction partners:
- Chemotaxis protein MotB
- MotD
- Flagellar hook-associated protein 1
- Flagellar basal-body rod protein FlgG
- Flagellar M-ring protein
- Basal-body rod modification protein FlgD
- Flagellar basal-body rod protein FlgC
- Flagellar hook protein FlgE
- Flagellar L-ring protein
- MotC
Sequence:
MSKIIGIIVVFASVLGGFLLSGGKIGAIIQPFEVLIIGGAALGAFLQSNPGSTFMVVLKKAPKMFSNRFTQTYYLEVLGMLYEILNKSRREGMMAIEADIEDPAASPIFSKYPGVLKDERMTAYVCDYLRIMSSGNMAPHELEGLFDMELSSLKEDLEHPSHAVTKVADALPGFGIVAAVLGIVITMALLGEGSQAEIGHHVAAALVGTFLGILAAYGFVGPLAGALEHDAKEELNLFEAIKACLVASASGMPPSLAVEFGRKVLLPAHRPTFAELEQAVRGR
Protein: Delta-1-pyrroline-5-carboxylate synthase A (P5CS A) [Includes: Glutamate 5-kinase (GK) (EC 2.7.2.11) (Gamma-glutamyl kinase); Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase)] (P54887)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate synthase B
- Ornithine aminotransferase, mitochondrial
- Delta-1-pyrroline-5-carboxylate dehydrogenase 12A1, mitochondrial
- Pyrroline-5-carboxylate reductase
- Glutamate synthase 1, chloroplastic
- Glutamate dehydrogenase 2
- Probable glutamate dehydrogenase 3
- glutamate dehydrogenase
- Glutamate dehydrogenase 1
- Proline dehydrogenase 1, mitochondrial
Sequence:
MEELDRSRAFARDVKRIVVKVGTAVVTGKGGRLALGRLGALCEQLAELNSDGFEVILVSSGAVGLGRQRLRYRQLVNSSFADLQKPQTELDGKACAGVGQSSLMAYYETMFDQLDVTAAQLLVNDSSFRDKDFRKQLNETVKSMLDLRVIPIFNENDAISTRRAPYQDSSGIFWDNDSLAALLALELKADLLILLSDVEGLYTGPPSDPNSKLIHTFVKEKHQDEITFGDKSRLGRGGMTAKVKAAVNAAYAGIPVIITSGYSAENIDKVLRGLRVGTLFHQDARLWAPITDSNARDMAVAARESSRKLQALSSEDRKKILLDIADALEANVTTIKAENELDVASAQEAGLEESMVARLVMTPGKISSLAASVRKLADMEDPIGRVLKKTEVADGLVLEKTSSPLGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEARRSNAILHKVITDAIPETVGGKLIGLVTSREEIPDLLKLDDVIDLVIPRGSNKLVTQIKNTTKIPVLGHADGICHVYVDKACDTDMAKRIVSDAKLDYPAACNAMETLLVHKDLEQNAVLNELIFALQSNGVTLYGGPRASKILNIPEARSFNHEYCAKACTVEVVEDVYGAIDHIHRHGSAHTDCIVTEDHEVAELFLRQVDSAAVFHNASTRFSDGFRFGLGAEVGVSTGRIHARGPVGVEGLLTTRWIMRGKGQVVDGDNGIVYTHQDIPIQA
Protein: Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Triose-phosphate isomerase) (P04828)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Fructose-bisphosphate aldolase
- Phosphoglycerate kinase
- Fructose-bisphosphate aldolase
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate isomerase
- Dihydroxyacetone kinase
- Transaldolase
- Phosphoglycerate mutase family protein
Sequence:
MPRKFFVGGNFKMNGNAESTTSIIKNLNSANLDKSVEVVVSPPALYLLQAREVANKEIGVAAQNVFDKPNGAFTGEISVQQLREANIDWTILGHSERRVILKETDEFIARKTKAAIEGGLQVIFCIGETLEEREANKTIDVVTRQLNAAAKELSKEQWAKVVIAYEPVWAIGTGKVATTEQAQEVHSAIRKWLKDAISAEAAENTRIIYGGSVSEKNCKDLAKEADIDGFLVGGASLKPAFVDIVNARL