wanglab/gogpt-training-data huggingface dataset:
Protein: Protein argonaute 1 (LbrAGO1) (G8XR08)
Organism: Leishmania braziliensis
Function: Involved in RNA-mediated gene silencing (RNAi) of mobile elements and repeats including retroposons SLACS (Spliced Leader Associated Conserved Sequence), TATE (Telomere-Associated Transposable Element) and TAS-like sequences (Telomere Associated Sequence), and a family of 74-nucleotide long tandem repeats, CIR74. Predominantly binds to siRNAs derived from SLACS and TATE transposable elements and to a lesser extent to siRNAs from TAS-like and CIR74 elements.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:23217017}.
Interaction partners:
Sequence:
MLALNAGSQYPGRGRGRGRGDGGNRVHKHDGINRYHGGFRGGRGGGGGGFRDGDMRECRERESWAVSAAQANARTLARVPVPVETNCFPIDLSEGRFHNYIVSFEFLENATDMAGDMWKISLQNELLRTIRKNRTAEKRTRTSAEVEDLCVCTGQAILAPAKLSVEDGFSIECTRKEKVSRNNTEERHYRVRIRYDGEVSLKLPEHAQWVNKIIAFGLADTYSEHIGSDYVDMKSTVERGGDLVTMDAISLNALRIVKQSGSTTAMMDVLQLDVSTKASTKTKCSDEMRRLRQQNPQGFRRAVNEALVGISVTTVFGEPTFLKVKAIDFNILASSPTMFKTNPEETFVEYFKRKYDAIIDPTLPMLYCIFADRTKMSRRMPYPADSLLLNKLNEAQLSKLPILCSIYPNERMKRIKAALERVLASPLMITVLQQYGVRIQPQFVKVSGRVLPAPTIYVPSGPNMFNRINTAEYTGQAGFALGLKDLQHPSQPCEFKTLLMDEYFMHGNITHWLQKYNVALPSPRKTSFDSAAQRITEGPGTFAMVKLRTKEAGAYNNFKERFARSSIVSQMAVVDLTRNVPQMITQQVAAKIGQLCFVADVDEAGKSFACRPLLIVGAVVGTAMNTMLEKYKSINVRLYTITFVAFLANGKSWKPYCMHHQVKGEEHVLYEDSDAASSHMSSTTLTVRRQNANEVLNNRFPDFLKEVTAHFKLNGKGSKGTMVLYRGAMTDAEVGFTANMDLVMEQVLPNWDTATVVVHPRSHFRMAWDPTTVFPHETASAYAGLSNVPRGFSTTDCRIILADSDPYTPVDSFYLSAANCTLGHAANTYYLVQKRAASISLMDLQKLTYNMCYMYPNKPDALPLPLPIKCAYEYARKYGSLKSVKELPTRMRPTMHYL
Protein: BZIP protein (AtbZIP48) (Basic leucine-zipper 48) (Q8RU59)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- bZIP transcription factor 49
- Ethylene-responsive transcription factor ERF037
Sequence:
MIPAEINGYFQYLSPEYNVINMPSSPTSSLNYLNDLIINNNNYSSSSNSQDLMISNNSTSDEDHHQSIMVLDERKQRRMLSNRESARRSRMRKQRHLDELWSQVIRLRNENNCLIDKLNRVSETQNCVLKENSKLKEEASDLRQLVCELKSNKNNNNSFPREFEDN
Protein: Acyltransferase PapA3 (EC 2.3.1.278) (EC 2.3.1.279) (Long-chain-acyl-CoA--trehalose acyltransferase) (Mycolipenoyl-CoA--2-(long-chain-fatty acyl)-trehalose mycolipenoyltransferase) (Polyketide synthase-associated protein A3) (P9WIK5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of polyacyltrehalose (PAT), a pentaacylated, trehalose-based glycolipid that could have a role in anchoring the bacterial capsule. Catalyzes the sequential transfer of two palmitoyl groups onto a single glucose residue of trehalose generating the diacylated product 2,3-diacyltrehalose (trehalose dipalmitate). Although palmitoyl-CoA (PCoA) seems to be the physiological acyl donor, PapA3 can also use docosanoyl (22-carbon saturated fatty acid) coenzyme A as acyl donor.
Interaction partners:
- Mycolipanoate synthase
- Acyltrehalose exporter MmpL10
- Phthioceranic/hydroxyphthioceranic acid synthase
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Mycocerosic acid synthase-like polyketide synthase
- Polyketide synthase Pks13
- Mycoketide-CoA synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Sulfolipid-1 exporter MmpL8
- Phenyloxazoline synthase MbtB
Sequence:
MLRVGPLTIGTLDDWAPSTGSTVSWRPSAVAHTKASQAPISDVPVSYMQAQHIRGYCEQKAKGLDYSRLMVVSCQQPGQCDIRAANYVINAHLRRHDTYRSWFQYNGNGQIIRRTIQDPADIEFVPVHHGELTLPQIREIVQNTPDPLQWGCFRFGIVQGCDHFTFFASVDHVHVDAMIVGVTLMEFHLMYAALVGGHAPLELPPAGSYDDFCRRQHTFSSTLTVESPQVRAWTKFAEGTNGSFPDFPLPLGDPSKPSDADIVTVMMLDEEQTAQFESVCTAAGARFIGGVLACCGLAEHELTGTTTYYGLTPRDTRRTPADAMTQGWFTGLIPITVPIAGSAFGDAARAAQTSFDSGVKLAEVPYDRVVELSSTLTMPRPNFPVVNFLDAGAAPLSVLLTAELTGTNIGVYSDGRYSYQLSIYVIRVEQGTAVAVMFPDNPIARESVARYLATLKSVFQRVAESGQQQNVA
Protein: F26K24.14 protein (Q9SF14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MESPIKCCDCGCDCCSSSPGSWIRSVKKRRHDELQTEKRFSIPELDDLDMFSNPRVQIENECELLRETVSNQQQTIQDLYHELEQERIASSTAADETVKMIQTLEREKAKIDLELKQLQRSVDETLNYENQEIEALENMVYQRDQTIQALTFETQAYKHRMMSFGLTEAEADGERSLLSRNPSMIDFSSEYDCPTQDYPPLKCNINENQDPLEADIYVADDENYPPADSPHGRVHLKTLDRRLSQMETNPSFTQLNRGRDVSEKGMVGESPRRQRHFRRISPTGSSSSHLGASKELRPDVFVDSPRSQSYSSKKMEDVSYTENNNAKDDLSEIGDDMSDRVYTIDSVHHSSVAHSGGVAEQKIEDGASDGNVVFPREHTDLGDPDITKLYMRLQALEADRESMKHALLSMRTEKAQMVLLKEIAQHLSKEVVPQRRLPLRKASIAGPLTFTPVFKWITSFVSWKRKARRSKYMYGMSGNNIGLQMLLEKVPRSRKWRCLRSTQV
Protein: Tetratricopeptide repeat (TPR)-like superfamily protein (F4I448)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- U1 small nuclear ribonucleoprotein C
- RNA-binding motif protein 25
- U1 small nuclear ribonucleoprotein 70 kDa
- AT5g17440/K3M16_10
- Arginine-aspartate-rich RNA binding protein-like
- Pre-mRNA-processing protein 40B
- LUC7 related protein
- Nuclear protein-like
- Pre-mRNA-processing protein 40A
- Small nuclear ribonucleoprotein SmD1a
Sequence:
MGDSEAMVSEGYTSAPYGDYNASAATVESTGQETAPIVDASHSVNNDSLVNGTAPVENGSATDNVAVTAPAAEHGDNTGSTLSTEEERLWNIVRANSLEFNAWTALIDETERIAQDNIAKIRKVYDAFLAEFPLCYGYWKKFADHEARVGAMDKVVEVYERAVLGVTYSVDIWLHYCTFAINTYGDPETIRRLFERALVYVGTDFLSSPLWDKYIEYEYMQQDWSRVALIYTRILENPIQNLDRYFSSFKELAETRPLSELRSAEESAAAAVAVAGDASESAASESGEKADEGRSQVDGSTEQSPKLESASSTEPEELKKYVGIREAMYIKSKEFESKIIGYEMAIRRPYFHVRPLNVAELENWHNYLDFIERDGDFNKLSSIWCIICLIGFPLDQATFKWEITETKACASICSNVINAGVFLTFCLSGKEGPSVVKLYERCVVTCANYPEYWIRYVTNMEASGSADLAENALARATQVFVKKQPEIHLFAARLKEQNGDIAGARAAYQLVHSEISPGLLEAVIKHANMEYRLGNLDDAFSLYEQVIAVEKGKEHSTILPLLYAQYSRFSYLVSRDAEKARRIIVEALDHVQPSKPLMEALIHFEAIQPPPREIDYLEPLVEKVIKPDADAQNIASSTEREELSLIYIEFLGIFGDVKSIKKAEDQHVKLFYPHRSTSELKKRSADDFLASDRTKMAKTYNGTPPAQPVSNAYPNAQAQWSGGYAAQPQTWPPAQAAPAQPQQWNPAYGQQAAYGAYGGYPAGYTAPQAPTPVPQAAAYGAYPAQTYPTQSYAPPVAAAAPAAAPVQQPAAAVAPQAYYNTYY
Protein: cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B (EC 3.1.4.17) (CGIPDE1) (CGIP1) (Cyclic GMP-inhibited phosphodiesterase B) (CGI-PDE B) (Q13370)
Organism: Homo sapiens (Human)
Function: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological process. Regulates angiogenesis by inhibiting the cAMP-dependent guanine nucleotide exchange factor RAPGEF3 and downstream phosphatidylinositol 3-kinase gamma-mediated signaling. Controls cardiac contractility by reducing cAMP concentration in cardiocytes (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q61409}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- RAC-alpha serine/threonine-protein kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Adenosine kinase
- RAC-gamma serine/threonine-protein kinase
- cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A
- RAC-beta serine/threonine-protein kinase
- GMP reductase 1
- GTP:AMP phosphotransferase AK3, mitochondrial
- Deoxycytidine kinase
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MRRDERDAKAMRSLQPPDGAGSPPESLRNGYVKSCVSPLRQDPPRGFFFHLCRFCNVELRPPPASPQQPRRCSPFCRARLSLGALAAFVLALLLGAEPESWAAGAAWLRTLLSVCSHSLSPLFSIACAFFFLTCFLTRTKRGPGPGRSCGSWWLLALPACCYLGDFLVWQWWSWPWGDGDAGSAAPHTPPEAAAGRLLLVLSCVGLLLTLAHPLRLRHCVLVLLLASFVWWVSFTSLGSLPSALRPLLSGLVGGAGCLLALGLDHFFQIREAPLHPRLSSAAEEKVPVIRPRRRSSCVSLGETAASYYGSCKIFRRPSLPCISREQMILWDWDLKQWYKPHYQNSGGGNGVDLSVLNEARNMVSDLLTDPSLPPQVISSLRSISSLMGAFSGSCRPKINPLTPFPGFYPCSEIEDPAEKGDRKLNKGLNRNSLPTPQLRRSSGTSGLLPVEQSSRWDRNNGKRPHQEFGISSQGCYLNGPFNSNLLTIPKQRSSSVSLTHHVGLRRAGVLSSLSPVNSSNHGPVSTGSLTNRSPIEFPDTADFLNKPSVILQRSLGNAPNTPDFYQQLRNSDSNLCNSCGHQMLKYVSTSESDGTDCCSGKSGEEENIFSKESFKLMETQQEEETEKKDSRKLFQEGDKWLTEEAQSEQQTNIEQEVSLDLILVEEYDSLIEKMSNWNFPIFELVEKMGEKSGRILSQVMYTLFQDTGLLEIFKIPTQQFMNYFRALENGYRDIPYHNRIHATDVLHAVWYLTTRPVPGLQQIHNGCGTGNETDSDGRINHGRIAYISSKSCSNPDESYGCLSSNIPALELMALYVAAAMHDYDHPGRTNAFLVATNAPQAVLYNDRSVLENHHAASAWNLYLSRPEYNFLLHLDHVEFKRFRFLVIEAILATDLKKHFDFLAEFNAKANDVNSNGIEWSNENDRLLVCQVCIKLADINGPAKVRDLHLKWTEGIVNEFYEQGDEEANLGLPISPFMDRSSPQLAKLQESFITHIVGPLCNSYDAAGLLPGQWLEAEEDNDTESGDDEDGEELDTEDEEMENNLNPKPPRRKSRRRIFCQLMHHLTENHKIWKEIVEEEEKCKADGNKLQVENSSLPQADEIQVIEEADEEE
Protein: Fatty acid synthase subunit alpha (EC 2.3.1.86) [Includes: 3-oxoacyl-[acyl-carrier-protein] reductase (EC 1.1.1.100); 3-oxoacyl-[acyl-carrier-protein] synthase (EC 2.3.1.41)] (Q6FUY8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Candida glabrata strain CBS138 chromosome L complete sequence
- beta-ketoacyl-[acyl-carrier-protein] synthase I
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome K complete sequence
- Candida glabrata strain CBS138 chromosome I complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- [acyl-carrier-protein] S-malonyltransferase
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- Candida glabrata strain CBS138 chromosome J complete sequence
Sequence:
MVMKPEVEQELAHVLLTELLAYQFASPVRWIETQDVLLKDFNTERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLQRQVLCYSKDAREIYYTADPAEIEPKEEPKAEEAAAPAPAAAPAATPAPAPVAAPAPAAAAADVPDEPVKASLLLHTLVAHKLKKSLDQVPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEDTPLEELAETFQDTFSGALGKQSTSLLSRMVSSKMPGGFNMTSVRKYLQSRWGLGQGRQDSALLVALSNEPASRLGAEPDAKTFLDAQVQKYAQISGLDLSAASSSASAGGAGASASGATIDAAALEEITKDHKVLARQQLQVLARYLKMDLNNGERKFLKEKDTVAELQSQLDYITNELGEFFVNGISTSFSRKKARQFDSSWNWARQSLLSLYFEIIHGVLKNVDREVVTEAINIMNRSNETLIKFMEYHVSKTDVSKGENYKLVKELGDQLIENCKQVLDVDPVYKDVSKPTGPKTTIDKNGNIKYSEEPRDKIRKFSQYVQEMALGGPLTKEDQPTIQEDLTRVYKAISSQAAEQDVTEATRAEFEKLYSDLIQFLKTSKEIDAQQTTQLAGIVDDALDKDSTREVASLPNKSTISTAVSSTIPRQTVPFLHLRKKAPSGEWKYDRHLSSLFLDGLERATINGVTFNDKYVLITGAGQGSIGAEVLQGLLQGGAKVVVTTSRFSKKVTDYYQSMYAKFGARGSTLVVVPFNQGSKQDVEALIDYIYDDEKNGGLGWDLDAFIPFAAIPENGIELENIDSKSEFAHRIMMTNILRMMGCIKKQKSAREIETRPAQVILPMSPNHGTFGGDGLYSESKLSLETLFNRWHSESWANQLTVCGAVIGWTRGTGLMTANNIIAEGIEKMGVRTFSQKEMALNLLGLMIPEIVELCQKSPVMADLNGGLQYLTDLKEFTAKLRRELTETSEIRKAVSIETALEHKIVNGNKADEAYAKVEVQPRANIQLNFPTLKNYKDIKKIAKEELEGMLDLERVIVVTGFSEVGPWGSSRTRWEMEAFGEFSLEGSVEMAWMMGMIKYHNGNLKGRPYTGWVDAKTNEPVDDKDIKAKYESKILEHSGIRLIEPELFHGYNPEKKQMIQEVIVEDDLEPFEASKETAEQFKHEHGDKVDIFEIPETGEYSVKILKGATLYIPKALRFDRLVAGQVPTGWNAKTYGISDDIISQVDPITLFVLVSVVEAFITSGISDPYEMYKYVHVSEVGNCSGSGMGGVSALRGMFKDRYKDMPVQNDILQESFINTMSAWVNMLLISSSGPIKTPVGACATSVESVDIGVETILSGKAKICIVGGYDDFQEEGSYEFGNMKATSNTLEEFEHGRTPAEMSRPATTSRNGFMEAQGAGIQVIMNADLALKMGVPIYGIVALTATATDKIGRSVPAPGKGILTTAREHHGAMRFPTPMMDIKYRKRQLVSREKQIKQWVEDELEMTKYEAEGLSDSERNAFFAERSEEIKKEAQRQLKSAQAQWGNEFFKNDPRIAPLRGSLAAFGLTIDDLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVIGVFQKFLTGHPKGAAGAWMLNGAIQILNSGIVPGNRNADNVDKLLEQFDYVLYPSKSIKTDGIKAVSVTSFGFGQKGAQAVVIHPDYLYAAIDEGRYNEYAAKVTEREKAAHKFFHNGMIYNKLFVSKEHAPYDDSLEEKVYLDPLVRVENDKKSGELKFSSKGIQKHDTYLSESAKKTSEMISGSLKEETKNVGVDVELIASINIDNETFIERNFTSEEVKYCSSQPSAQSSFAGTWSAKEAVFKSLGVKSRGAGAPMKEIEILRDVNGKPTVTLHGEAKKLAQKESIKAVSVSISHDDFQSIAVAIANK
Protein: Major sperm protein isoform beta (Beta-MSP) (P27440)
Organism: Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Function: Central component in molecular interactions underlying sperm crawling. Forms an extensive filament system that extends from sperm villipoda, along the leading edge of the pseudopod.
Subcellular location: Cell projection, pseudopodium. Cytoplasm, cytoskeleton.
Interaction partners:
Sequence:
MAQSVPPGDINTQPGSKIVFNAPYDDKHTYHIKITNAGGRRIGWAIKTTNMRRLGVDPPCGVLDPKESVLMAVSCDTFNAATEDLNNDRITIEWTNTPDGAAKQFRREWFQGDGMVRRKNLPIEYNL
Protein: GTP-binding protein Rhes (Ras homolog enriched in striatum) (P63032)
Organism: Mus musculus (Mouse)
Function: GTPase signaling protein that binds to and hydrolyzes GTP. Regulates signaling pathways involving G-proteins-coupled receptor and heterotrimeric proteins such as GNB1, GNB2 and GNB3. May be involved in selected striatal competencies, mainly locomotor activity and motor coordination.
Subcellular location: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Interaction partners:
- Huntingtin
- Beclin-1
- Endosialin
Sequence:
MMKTLSSGNCTLNVPAKNSYRMVVLGASRVGKSSIVSRFLNGRFEDQYTPTIEDFHRKVYNIHGDMYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDSRESFDEVKRLQKQILEVKSCLKNKTKEAAELPMVICGNKNDHSELCRQVPAMEAELLVSGDENCAYFEVSAKKNTNVNEMFYVLFSMAKLPHEMSPALHHKISVQYGDAFHPRPFCMRRTKVAGAYGMVSPFARRPSVNSDLKYIKAKVLREGQARERDKCSIQ
Protein: Nitric oxide synthase 1 adaptor protein (H0VD63)
Organism: Cavia porcellus (Guinea pig)
Interaction partners:
- Nitric oxide synthase 1
- Ras related dexamethasone induced 1
- Chromosome 1 open reading frame 226
- Methionine synthase reductase
- Nitric oxide synthase 3
- Nitric oxide synthase, inducible
- NADPH--cytochrome P450 reductase
- NADPH-dependent diflavin oxidoreductase 1
- RASD family member 2
- NFKB activating protein like
Sequence:
TSNAYEFKAKNIKKKKVSIMVSVDGVKVILKKKKKKKEWTWDESKMLVMQDPIYRIFYVSHDSQDLKIFSYIARDGASNIFRCNVFKSKKKSQAMRIVRTVGQAFEVCHKLSLQHTQQNADGQEDGESERNSNGSGDPGRQPTGAERASTATTEETDIDAVEVPLPGNDVLEFSRGVTDLDAVGKEGGSHSDSKVSPHPQDPMLTASPHMLLPSSISKPPGLGTGTPLSTHHQMQLLQQLLQQQQQQTQVAVAQVHLLKDQLAAEAAARLEAQARVHQLLLQNKDMLQHISLLVKQVQELELKLSGQNAMGSQDSLLEITFRSGALPVLCDPTTPKPQDLHSPPPLGAGLADFAPPVGSPLGRRDCLVKLECFRFLPSEDTPTPAQGEPLLGGLELLKFRESGIASEYESNTDESEERDSWSQEELPRLLNVLPRQELGDSLDDEIAV
Protein: 4-aminobutyrate aminotransferase GabT (EC 2.6.1.19) (5-aminovalerate transaminase) (EC 2.6.1.48) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (Glutamate:succinic semialdehyde transaminase) (L-AIBAT) (P22256)
Organism: Escherichia coli (strain K12)
Function: Pyridoxal phosphate-dependent enzyme that catalyzes transamination between primary amines and alpha-keto acids. Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA) and glutamate. Thereby functions in a GABA degradation pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth. Also catalyzes the conversion of 5-aminovalerate to glutarate semialdehyde, as part of a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate.
Interaction partners:
- Succinate-semialdehyde dehydrogenase [NADP
- Succinate semialdehyde dehydrogenase [NAD
- Gamma-aminobutyraldehyde dehydrogenase
- L-2-hydroxyglutarate dehydrogenase
- Glutamate decarboxylase beta
- Gamma-aminobutyric acid permease
- Glutamate decarboxylase alpha
- Glutarate 2-hydroxylase
- Fatty acid oxidation complex subunit alpha
- Fatty acid oxidation complex subunit alpha
Sequence:
MNSNKELMQRRSQAIPRGVGQIHPIFADRAENCRVWDVEGREYLDFAGGIAVLNTGHLHPKVVAAVEAQLKKLSHTCFQVLAYEPYLELCEIMNQKVPGDFAKKTLLVTTGSEAVENAVKIARAATKRSGTIAFSGAYHGRTHYTLALTGKVNPYSAGMGLMPGHVYRALYPCPLHGISEDDAIASIHRIFKNDAAPEDIAAIVIEPVQGEGGFYASSPAFMQRLRALCDEHGIMLIADEVQSGAGRTGTLFAMEQMGVAPDLTTFAKSIAGGFPLAGVTGRAEVMDAVAPGGLGGTYAGNPIACVAALEVLKVFEQENLLQKANDLGQKLKDGLLAIAEKHPEIGDVRGLGAMIAIELFEDGDHNKPDAKLTAEIVARARDKGLILLSCGPYYNVLRILVPLTIEDAQIRQGLEIISQCFDEAKQ
Protein: Atypical chemokine receptor 3b (Cxcr7b protein) (A4IG54)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Stromal cell-derived factor 1
- Stromal cell-derived factor 1
- Atypical chemokine receptor 3a
- Beta-arrestin-1
- Arrestin, beta 2a.
- Arrb2b protein
- Claudin b
Sequence:
MSVNVNDFNDILDALGELNFSTLDDNVSHVEVCHSTFSQRALLYALSVLYIFLFIIGLAANALVVWVNVRAERTRYETHLYILNLAIADLCVVATLPVSISSLLQLGHWPFGGAMCKITHLIFSVNLFSSIFFLTCMSVDRYLSVKLFGDTPSQRKRRTRQIICVGVWLLALIAALPEIYFLQAEKSDHSDAIVCKAVYPVESMKEWTVGIQMSFFMLGFAIPFPVIAVFYVLLANTIHPSVDQERRISRHLIFTYIVVFLVCWLPYHGALLLDTLAFLNVLPFNCTLENALYAALHLTQCFSLFHCCANPIIYNFINKNYRYDLMKAFIFKYSTKTGLARLIDASHVSETEYSAVENQGPL
Protein: Lutropin-choriogonadotropic hormone receptor (LH/CG-R) (Luteinizing hormone receptor) (LHR) (LSH-R) (P22888)
Organism: Homo sapiens (Human)
Function: Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11847099}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Follitropin subunit beta
- Choriogonadotropin subunit beta 3
- Guanine nucleotide-binding protein G
- Thyrotropin subunit beta
- Lutropin subunit beta
- Pro-opiomelanocortin
- Gastric inhibitory polypeptide
- Pro-glucagon
- Natriuretic peptides A
- Pituitary adenylate cyclase-activating polypeptide
Sequence:
MKQRFSALQLLKLLLLLQPPLPRALREALCPEPCNCVPDGALRCPGPTAGLTRLSLAYLPVKVIPSQAFRGLNEVIKIEISQIDSLERIEANAFDNLLNLSEILIQNTKNLRYIEPGAFINLPRLKYLSICNTGIRKFPDVTKVFSSESNFILEICDNLHITTIPGNAFQGMNNESVTLKLYGNGFEEVQSHAFNGTTLTSLELKENVHLEKMHNGAFRGATGPKTLDISSTKLQALPSYGLESIQRLIATSSYSLKKLPSRETFVNLLEATLTYPSHCCAFRNLPTKEQNFSHSISENFSKQCESTVRKVNNKTLYSSMLAESELSGWDYEYGFCLPKTPRCAPEPDAFNPCEDIMGYDFLRVLIWLINILAIMGNMTVLFVLLTSRYKLTVPRFLMCNLSFADFCMGLYLLLIASVDSQTKGQYYNHAIDWQTGSGCSTAGFFTVFASELSVYTLTVITLERWHTITYAIHLDQKLRLRHAILIMLGGWLFSSLIAMLPLVGVSNYMKVSICFPMDVETTLSQVYILTILILNVVAFFIICACYIKIYFAVRNPELMATNKDTKIAKKMAILIFTDFTCMAPISFFAISAAFKVPLITVTNSKVLLVLFYPINSCANPFLYAIFTKTFQRDFFLLLSKFGCCKRRAELYRRKDFSAYTSNCKNGFTGSNKPSQSTLKLSTLHCQGTALLDKTRYTEC
Protein: Cd55 molecule (Q9Z0M0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MIRTRAPGTRAPPPPPLLLSLSLLLLLLSPTVSGDCGPPPDIPNATPNSGKHTKFAHQSQVTYSCNKGFKQIPDKPNTVVCLENDQWSNYETFCNKTCSAPLRLNYASLKKEYRNMNFFPIGTTVEFECRPGFQKVTSRTGKSTCLEELVWSPVVEFCKKRACPNPRELKNGHINIPTDILFGSEIIFSCDKGYKLVGVTSTFCSITGNAVDWDDVFPVCTTIFCPDPPKINNGRIREESDSYAYRQSVTYSCDQGFILVGNSSVHCTLNGEVGEWSSAPPKCIERHKVPTKTPPEVDIPSTMPHESTLINFPSTRAPLSHKPTTVKVPGTRVKPTSHKPTEVKVPATQHVPVSKTTVRHPTRTSKDRGESNSGGDHFIYGHTCLITMTILHVMLLLTG
Protein: Uncharacterized protein McbA (MqsR-controlled colanic acid and biofilm protein A) (P0AAX6)
Organism: Escherichia coli (strain K12)
Function: Affects biofilm formation and mucoidy.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- Metalloprotease PmbA
- Uncharacterized protein YjfY
- Uncharacterized protein RclB
Sequence:
MKKCLTLLIATVLSGISLTAYAAQPMSNLDSGQLRPAGTVSATGASNLSDLEDKLAEKAREQGAKGYVINSAGGNDQMFGTATIYK
Protein: U1 small nuclear ribonucleoprotein C (U1 snRNP C) (U1-C) (U1C) (Q5TAL4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|HAMAP-Rule:MF_03153, ECO:0000256|PIRNR:PIRNR037969}.
Interaction partners:
Sequence:
MPKFYCDYCDTYLTHDSPSVRKTHCSGRKHKENVKDYYQKWMEEQAQSLIDKTTAAFQQGKIPPTPFSAPPPAGAMIPPPPSLPGPPRPGMMPAPHMGGPPMMPMMGPPPPGMMPVGPAPGMRPPMGGHMPMMPGPPMMRPPARPMMVPTRPGMTRPDR
Protein: Fructose-bisphosphate aldolase class 1 (EC 4.1.2.13) (Fructose-bisphosphate aldolase class I) (FBP aldolase) (P0A991)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible aldol condensation/cleavage reaction between glyceraldehyde 3-phosphate and dihydroxyacetone phosphate (DHAP) to yield fructose-bisphosphate (FBP).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- ATP-dependent 6-phosphofructokinase isozyme 2
- Transketolase 2
- Transaldolase A
- Fructose-bisphosphate aldolase class 2
- Triosephosphate isomerase
- ATP-dependent 6-phosphofructokinase isozyme 1
- Glyceraldehyde-3-phosphate dehydrogenase A
- Fructose-1,6-bisphosphatase class 1
- Transketolase 1
- Transaldolase B
Sequence:
MTDIAQLLGKDADNLLQHRCMTIPSDQLYLPGHDYVDRVMIDNNRPPAVLRNMQTLYNTGRLAGTGYLSILPVDQGVEHSAGASFAANPLYFDPKNIVELAIEAGCNCVASTYGVLASVSRRYAHRIPFLVKLNHNETLSYPNTYDQTLYASVEQAFNMGAVAVGATIYFGSEESRRQIEEISAAFERAHELGMVTVLWAYLRNSAFKKDGVDYHVSADLTGQANHLAATIGADIVKQKMAENNGGYKAINYGYTDDRVYSKLTSENPIDLVRYQLANCYMGRAGLINSGGAAGGETDLSDAVRTAVINKRAGGMGLILGRKAFKKSMADGVKLINAVQDVYLDSKITIA
Protein: Polyamine-modulated factor 1-binding protein 1 (PMF-1-binding protein) (Q8TBY8)
Organism: Homo sapiens (Human)
Function: Required for normal spermatogenesis. It functions as a scaffold protein that attaches the sperm head-tail connecting piece to the nuclear envelope, thus maintaining sperm head and tail integrity. May also be involved in the general organization of cellular cytoskeleton (By similarity).
Subcellular location: Cell projection, cilium, flagellum {ECO:0000269|PubMed:30032984, ECO:0000269|PubMed:30298696}. Note=Localized at the sperm head-tail connecting piece (PubMed:30032984, PubMed:30298696). During spermatogenesis, it is first observed in the cytoplasm of round spermatids, it later appears in the implantation fossa region of the sperm nucleus during sperm head elongation and differentiation, and finally it localizes to the head-tail connecting piece (By similarity). {ECO:0000250|UniProtKB:Q9WVQ0, ECO:0000269|PubMed:30032984, ECO:0000269|PubMed:30298696}.
Interaction partners:
- SUN domain-containing protein 5
- Testis-specific gene 10 protein
Sequence:
MKDEAGERDREVSSLNSKLLSLQLDIKNLHDVCKRQRKTLQDNQLCMEEAMNSSHDKKQAQALAFEESEVEFGSSKQCHLRQLQQLKKKLLVLQQELEFHTEELQTSYYSLRQYQSILEKQTSDLVLLHHHCKLKEDEVILYEEEMGNHNENTGEKLHLAQEQLALAGDKIASLERSLNLYRDKYQSSLSNIELLECQVKMLQGELGGIMGQEPENKGDHSKVRIYTSPCMIQEHQETQKRLSEVWQKVSQQDDLIQELRNKLACSNALVLEREKALIKLQADFASCTATHRYPPSSSEECEDIKKILKHLQEQKDSQCLHVEEYQNLVKDLRVELEAVSEQKRNIMKDMMKLELDLHGLREETSAHIERKDKDITILQCRLQELQLEFTETQKLTLKKDKFLQEKDEMLQELEKKLTQVQNSLLKKEKELEKQQCMATELEMTVKEAKQDKSKEAECKALQAEVQKLKNSLEEAKQQERLAAQQAAQCKEEAALAGCHLEDTQRKLQKGLLLDKQKADTIQELQRELQMLQKESSMAEKEQTSNRKRVEELSLELSEALRKLENSDKEKRQLQKTVAEQDMKMNDMLDRIKHQHREQGSIKCKLEEDLQEATKLLEDKREQLKKSKEHEKLMEGELEALRQEFKKKDKTLKENSRKLEEENENLRAELQCCSTQLESSLNKYNTSQQVIQDLNKEIALQKESLMSLQAQLDKALQKEKHYLQTTITKEAYDALSRKSAACQDDLTQALEKLNHVTSETKSLQQSLTQTQEKKAQLEEEIIAYEERMKKLNTELRKLRGFHQESELEVHAFDKKLEEMSCQVLQWQKQHQNDLKMLAAKEEQLREFQEEMAALKENLLEDDKEPCCLPQWSVPKDTCRLYRGNDQIMTNLEQWAKQQKVANEKLGNQLREQVKYIAKLSGEKDHLHSVMVHLQQENKKLKKEIEEKKMKAENTRLCTKALGPSRTESTQREKVCGTLGWKGLPQDMGQRMDLTKYIGMPHCPGSSYC
Protein: Large ribosomal subunit protein eL28y (60S ribosomal protein L28-2) (Q9M0E2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL32z
- Large ribosomal subunit protein eL21x/eL21w
- Large ribosomal subunit protein eL31x
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL22z
- Large ribosomal subunit protein uL22y
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Large ribosomal subunit protein eL6z
Sequence:
MATVPGQLIWEIVKRNNCFLVKQFGRGNAKVQFSKESNNLVNINSYKHSGLANKKTVTIQAAGKDQGVVLGTTKTKRQNKPKLSVNKSILKKEFSRMSKVVANQVVDNYYRPDLKKAALARLSAISKGLRVAKSGPKRRNRQA
Protein: Probable cell division protein WhiA (P9WF45)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in cell division and chromosome segregation.
Interaction partners:
- Putative gluconeogenesis factor
- Nucleotide-binding protein Rv1421
- Probable protein-export membrane protein SecG
- Transcriptional regulator WhiB2
- UvrABC system protein C
- Phosphoenolpyruvate transferase
- Possible transcriptional regulatory protein
- dITP/XTP pyrophosphatase
- Cell division protein FtsZ
- Uncharacterized HTH-type transcriptional regulator Rv1828
Sequence:
MAMTTDVKDELSRLVVKSVSARRAEVTSLLRFAGGLHIVGGRVVVEAELDLGSIARRLRKEIFELYGYTAVVHVLSASGIRKSTRYVLRVANDGEALARQTGLLDMRGRPVRGLPAQVVGGSIDDAEAAWRGAFLAHGSLTEPGRSSALEVSCPGPEAALALVGAARRLGVGAKAREVRGADRVVVRDGEAIGALLTRMGAQDTRLVWEERRLRREVRATANRLANFDDANLRRSARAAVAAAARVERALEILGDTVPEHLASAGKLRVEHRQASLEELGRLADPPMTKDAVAGRIRRLLSMADRKAKVDGIPDTESVVTPDLLEDA