wanglab/gogpt-training-data huggingface dataset:
Protein: RIM-binding protein, isoform K (Q9VF66)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPYESMHHHQSAAAAVAAGTTPNGMLDALSLQLRDAEMRRTEIERAHQETLAQIRNLSGSARPDAEAVENLQSRARELEKKVALENVRCEELQIELTSALKAKQASRSACSGMGSVSSGGGATIPTSASSSTVTWAPTISHQDQGSEIDIIMAKIEQDNRVLAELEQPRTSASASMSALPPSSMLSTVNSEFRTISKSELEEELNRYKRAVLGGSGGGGGGVGGGGGGVSALSSGYSSLPQSLASTLPNGGASTSLSGTSLGSHSAAAAAAAHSVSAGSGGVVGGGGQGGLSSISALVPNSISGISSSLSSHAIQSMQYGTGQTSVEKLLSGTSGITGIPPLPRGTIQLYNLQSTTMPLLSLNSHNLPPAGSTSYSALGAGGGTSLTHPTMANLGLLDTGTLLGSTGLSGLGVGPSVGGITGATSLYGLSGGGGGAGGLGSSYGPPFLDVASSASYPFTAAALRQASKMKMLDEIDIPLTRYNRSSPCSPIPPNNWGLDEFTDGLSVSMMHNRGGLALGALDLDTRNHGLNGASEPQVDMLDIPGKGRCCVFIARFPYDPPEEAEGELSLCAGDYLLVWTSGEPQGGYLDAELLDGRRGLVPASFVQRLVGDDLLEFHQAVLSTLRDAEDGSMQCDTTSLPSLPPHNPLLTHTHEDLARLSETHTDLEHDQDDISDNVPAPKHLTLERQLNKSVLIGWSPPEPVGYNLIDSYHVYVDGVLKVTVKANERTRALIEGVDSTRPHRISVRSVTQNRQTSRDAACTMIIGRDTAHLGPSAVRASHITCSSAVISWLPANSNHQHVVCVNNVEVRTVKPGMYRHTITGLAPSTQYRVTVRAKHLRAVGQHAANVGQTGGAGRPGQEEAPGAYADFRTLTKGLPDPPQEIQLEAGPQDGTILVTWQPVNRPTSTGPVTGYAVYADGKKVTDINSPTGDHALIDIGKLGVFNPRAVTIRTKSRDSQSADSAPILIPNTVRNAVARRGPNQMGMGPQLPQGPHGMTVQQQMGGMPGQPGQQGQHMMGGQQDHGQYDPNQMQQQQQQQGQPGQPGHQGYQPGQPGAQRGMVPIPGRPQGPQQQQQQPYGPQGPMGGPRFRGPVPGQLNMQGQQMQGQMQGQMQGQMQGQMSGQMPGQMPGQMPGQMPGQMAGQMAGQMPGQMPGQMPGQMSGQMPGQMMGPRGPLNQQQQQQQQMQQGQMMPGQQAGQQQAQPGQPGQPGQMPGAQKKPRYFVAMFDYDPSTMSPNPDGCDEELPFQEGDTIKVFGDKDADGFYWGELRGRRGYVPHNMVSEVEDTTASMTAGGQMPGQMPGQMGQGQGVGVGGTAQVMPGQGAPQQSMRNVSRDRWGDIYANMPVKRMIALYDYDPQELSPNVDAEQVELCFKTGEIILVYGDMDEDGFYMGELDGVRGLVPSNFLADAPDQYNNQMGPGGVAGRGGLSQRGRGQGPGARGPPPPPRDNMMPGMGGRGQPGKNARPASPTLLDNTGHPAPDHQTQGMIGRVGNVGLQQQQQQQQQQQQLQQQQQYGQQQTQMGQQQQQQQQMGQPGMMGQQMGQPMGQQMGQMGQMGQMGQQQMGQQQMGQQQQPPTTQAQTGGLFSGATSLLSGATSAATGGLFGSKQPPKTDPMQPQGGVQPAQQQANAFGAQQPGMGMQQQGGMQSGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQQGMQPGMQQQQQQPQQVPPQAQAPPPGPGAGLLGGLKGIAAAAPGGDVLSKGKDLFGKFGFGFGK
Protein: Transient receptor potential cation channel subfamily V member 6 (TrpV6) (Calcium transport protein 1) (CaT1) (Epithelial calcium channel 2) (ECaC2) (Q91WD2)
Organism: Mus musculus (Mouse)
Function: Calcium selective cation channel that mediates Ca(2+) uptake in various tissues, including the intestine. Important for normal Ca(2+) ion homeostasis in the body, including bone and skin. The channel is activated by low internal calcium level, probably including intracellular calcium store depletion, and the current exhibits an inward rectification. Inactivation includes both a rapid Ca(2+)-dependent and a slower Ca(2+)-calmodulin-dependent mechanism; the latter may be regulated by phosphorylation. In vitro, is slowly inhibited by Mg(2+) in a voltage-independent manner. Heteromeric assembly with TRPV5 seems to modify channel properties. TRPV5-TRPV6 heteromultimeric concatemers exhibit voltage-dependent gating.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12574114, ECO:0000269|PubMed:12601087, ECO:0000269|PubMed:12660155, ECO:0000269|PubMed:12765696, ECO:0000269|PubMed:14736889}; Multi-pass membrane protein {ECO:0000269|PubMed:12660155}.
Interaction partners:
- Calmodulin-1
- Protein S100-G
- Short transient receptor potential channel 1
- Protein S100-A10
- Transient receptor potential cation channel subfamily M member 4
- Transient receptor potential cation channel subfamily M member 8
- Transient receptor potential cation channel subfamily M member 7
- Transient receptor potential cation channel subfamily M member 1
- Calbindin
- Plasma membrane calcium-transporting ATPase 1
Sequence:
MGPLQREDRPALGGANVAPGSSPVGVWHQPQPPKEPAFHPMGWSLPKEKGLILCLWNKFCRWFHRQESWAQSRDEQNLLQQKRIWESPLLLAAKENDVQALSKLLKFEGCEVHQRGAMGETALHIAALYDNLEAAMVLMEAAPELVFEPMTSELYEGQTALHIAVINQNVNLVRALLARGASVSARATGSVFHYRPHNLIYYGEHPLSFAACVGSEEIVRLLIEHGADIRAQDSLGNTVLHILILQPNKTFACQMYNLLLSYDGGDHLKSLELVPNNQGLTPFKLAGVEGNIVMFQHLMQKRKHIQWTYGPLTSTLYDLTEIDSSGDDQSLLELIVTTKKREARQILDQTPVKELVSLKWKRYGRPYFCVLGAIYVLYIICFTMCCVYRPLKPRITNRTNPRDNTLMQQKLLQEAYVTPKDDLRLVGELVSIVGAVIILLVEIPDIFRLGVTRFFGQTILGGPFHVIIITYAFMVLVTMVMRLTNVDGEVVPMSFALVLGWCNVMYFARGFQMLGPFTIMIQKMIFGDLMRFCWLMAVVILGFASAFYIIFQTEDPDELGHFYDYPMALFSTFELFLTIIDGPANYDVDLPFMYSVTYAAFAIIATLLMLNLLIAMMGDTHWRVAHERDELWRAQVVATTVMLERKLPRCLWPRSGICGREYGLGDRWFLRVEDRQDLNRQRIRRYAQAFQQQDGLYSEDLEKDSGEKLETARPFGAYLSFPTPSVSRSTSRSSTNWERLRQGALRKDLRGIINRGLEDGEGWEYQI
Protein: Heparan-alpha-glucosaminide N-acetyltransferase (EC 2.3.1.78) (Transmembrane protein 76) (Q3UDW8)
Organism: Mus musculus (Mouse)
Function: Lysosomal acetyltransferase that acetylates the non-reducing terminal alpha-glucosamine residue of intralysosomal heparin or heparan sulfate, converting it into a substrate for luminal alpha-N-acetyl glucosaminidase.
Subcellular location: Lysosome membrane {ECO:0000269|PubMed:16960811}; Multi-pass membrane protein {ECO:0000269|PubMed:16960811}. Note=Colocalizes with the lysosomal marker LAMP2. The signal peptide is not cleaved upon translocation into the endoplasmic reticulum; the precursor is probably targeted to the lysosomes via the adapter protein complex-mediated pathway that involves tyrosine- and/or dileucine-based conserved amino acid motifs in the last C-terminus 16-amino acid domain (By similarity). {ECO:0000250}.
Interaction partners:
- Alpha-N-acetylglucosaminidase
- Heparan N-sulfatase)
- N-acetylglucosamine-6-sulfatase
Sequence:
MTGGSSSRRRRAEERSSAAGTERNSRREAVGGMGAGPALAALLLAGSVLSATLLAPGRRAEPDLDEKRNVELKMDQALLLIHNELLGTSLTVYWKSDDCYQCTFQPLANVSHGGKPAKPSVAPVSVSTQHGSILQVNSTSEERAACRLEYKFGEFGNYSLLVQHASSGANKIACDIIVNENPVDSNLPVSIAFLVGLALIVAVSLLRLLLSLDDVNNWISKTIASRETDRLINSELGSPSRADPLSADYQPETRRSSANRLRCVDTFRGLALVLMVFVNYGGGKYWYFKHSSWNGLTVADLVFPWFVFIMGTSIFLSMTSILQRGCSKLKLLGKIVWRSFLLICIGVIIVNPNYCLGPLSWDKVRIPGVLQRLGVTYFVVAVLEFFFWKPVPDSCTLESSCFSLRDITSSWPQWLTILTLESIWLALTFFLPVPGCPTGYLGPGGIGDLGKYPHCTGGAAGYIDRLLLGDNHLYQHPSSTVLYHTEVAYDPEGVLGTINSIVMAFLGVQAGKILVYYKDQTKAILTRFAAWCCILGLISIVLTKVSANEGFIPINKNLWSISYVTTLSCFAFFILLILYPVVDVKGLWTGTPFFYPGMNSILVYVGHEVLENYFPFQWKLADEQSHKEHLIQNIVATALWVLIAYVLYKKKLFWKI
Protein: IQ motif and SEC7 domain-containing protein 1 isoform X1 (IQ motif and Sec7 domain ArfGEF 1b) (E7EZE5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDGHFAYIDMENPTENPSKAAEYLKELNKIIETQQELLEKQKNRIEELEQQVCDLCQENACLKDQHQRHLATCRLQQQGNSHPTLGAIKENVIQEKNESEGLRVSNVRRHASLPLDVTDNPGNFIVSHCQRSYPCRKWKSASLGVEGEAPGGESGPSLDNSGGYLRGPVSRSAIISGEHFDGPPLYAHEVRQRPRRPKLQHSQSILRKQAEEEAIKRSRSLSESYELSTDLQDKQVEMLERKYGGRFITRHAARTIQTAFRQYQMNKNFERLRSSMSENRMSRRIVLSNMRMQFSFEGPEKVHSSYFEGKQVSLTDDGSKLGALVQSERGEMVPANMKSPAVQSDFTDAITELEDVFSRQVKSLAESIDDALNCRSLHGDEGQSEATRGHPDLEQEVTYQVKPSHGSEHRKRDEMTASYSDVTLYIDEEELSPPLPLSQSVDRPSSTESDLRLRSLNSSQDYWSLAHKDEKADTDTSCRSTPSLECQEQRLRIDHLPLLTIEPPSDSSVELSDRSDRSSLKRQNAYDRGIASQQGSPKHIPSHALPPRGPAREDEAPRHRPRQLESHLAINGTANRQSKSESDFSDGDNDSINSTSNSNDTINCSSESSSRDSLREQTLSKQTYHKETRNSWDSPAFSNDIIRKRHYRIGLNLFNKKPEKGIQYLIERGFVPDTPVGVAHFLLQRKGLSRQMIGEFLGNRQKQFNRDVLDCVVDEMDFSAMELDEALRKFQAHIRVQGEAQKVERLIEAFSQRYCICNPGVVRQFRNPDTIFILAFAIILLNTDMYSPNVKPERKMKLEDFVKNLRGVDDGEDIPREMLVGIYERIRKRELKTNEDHVSQVQKVEKLIVGKKPIGSLHHGLGCVLSLPHRRLVCYCRLFEVPDPNKPQKLGLHQREIFLFNDLLVVTKIFQKKKNSVTYSFRQSFSLYGMQVLLFENQYYPNGVRLTSALPGADIKVLINFNAPNPQDRKKFTDDLRESIAEVQEMEKYRIESELEKQKGVVRPSISQSSGLKKETGNGNLSRTSLDDSYAMGEGLKRSALSSSLRDLSDAGKRGRRSSAGSLDSNMEGSIISSPHIRRRATSSRDCPSRQQSIPNSSSLLGSLFGTKRGKSPSLPSQSSHPSHPTLISHTPHPSNLHHTARDGVTVTETQAQMHPHHAQFCHMQNPPPYHHHHHYHPPAHIQHPPHQYHPPPGPSSSHSHSHSQHGHGPHPSHSSHPSHSQHAPHHHSQPPAPPPAASSTKPKHSGISTVV
Protein: Protein mushroom body miniature (Q9VPM5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for small ribosomal subunit biogenesis in neuroblasts. Plays a role in mushroom body development.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15375215, ECO:0000269|PubMed:24615015}. Cytoplasm {ECO:0000269|PubMed:15375215, ECO:0000269|PubMed:24615015}. Note=Nuclear from interphase until early prophase and is then redistributed to the cytoplasm during mitosis when the nucleus is disassembled. {ECO:0000269|PubMed:24615015}.
Interaction partners:
Sequence:
MHNSGGQSGWNLSGEERKPFSNYGRNNQQRRSSGGGGRGSHSQNRAANGNWPDAGSEGGQNGNAFNKFRDPQQELDNHQPNKRGGRRNRGGGGGGGGWGGRRGNRGRDSNRRGGRNNSWQPKDQHVSPGQSNMLYFDNVGDFTEDPPLPRSSPAPSSLRQESLPPVTFAADLTPPPPVSVAPPDVAVTPEEPTVPLINIKKEKEMEHKSKIKQFVKAEPKSPKKKKVNSSRSSSTSGEESEPEPGEMVVNTKAVVVPSPKAKAIKTPVASTPKPKAVKPVSSSDSSTSDSDTDDEQSHPPAKSKKMEKNTEEDVVCMGSQERQFTITDEEESTEPEDDKKARKQKNKGKTVDVCGICDKKGHTSFQCQMICRNCSGSYHGLKNCPNPPNLNIAIQSFVEFAMQQMTAFHCEQGFGFPAGTVTAPVSAKPKKDKKASIKKIKKSSQKRMKVEPKDHDEEDDEEDDDEDEDDSSESDDSESSEEPHPAPVSKQKRKRGTKASVSAAASLPPQVFPFPLLGAPGAPFNSMMYSYRAPFNFSK
Protein: Glycerol-1-phosphatase (Q5A7M9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- glycerol kinase
- Bifunctional glycerol-3-phosphate/glycerone-phosphate O-acyltransferase
- Glycerol 2-dehydrogenase
- NADP-dependent oxidoreductase domain-containing protein
- NADP-dependent alcohol dehydrogenase
- Acylglycerol lipase
- Bifunctional glycerol-3-phosphate/glycerone-phosphate O-acyltransferase
- Serine aminopeptidase S33 domain-containing protein
- Glycerol-3-phosphate dehydrogenase [NAD
Sequence:
MTKTQQPAVFYVHAALFDCDGTLVNSTGAISEFWRDFGKTRPHVDPEEIIRTSHGCRTFDVIAKWSPEDAIEEQVTAWEGAIPDTFGHHAKPIPGSVELVKSFDKLSKEATENGKQRWAVVTSGTLPLATKWLKLLSIERPDCFITAEKVTKGKPHPQGYQAARDTLGYHDAHYKVVVFEDAPAGITAGKGAGAMVVGICSTYDPEKVRKSGANIVVKDLSSFRIDSYNKETDEFKVVVDDYFYADEQFLQESA
Protein: Elongation of fatty acids protein (EC 2.3.1.-) (Q6FT73)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase
- Acyl-CoA desaturase
- Elongation of fatty acids protein
- Candida glabrata strain CBS138 chromosome K complete sequence
- Very-long-chain
- beta-ketoacyl-[acyl-carrier-protein] synthase I
- 3-ketodihydrosphingosine reductase TSC10
Sequence:
MDQPVSQVTSAVASGAASAATAASSAAATAASVAVDQLEVLFQGAPSWIKVHTPSIDHPFGLELWPLFSAVFEKIAGYPAEDFRFIYNETFLANGYQAIGIIIFYYIVIFGGQAILRAINASPMHFHFLFQLHNLFLTSISFILMVLLIEQLVPMIYHHGLFWAICSPQAFAPKLVVLYYLNYLTKFVELFDTVFLIFKRKKLLFLHTYHHGATALLCYTQLVGETSVEWVPIVLNLGVHVVMYWYYFLSSCGIRVWWKQWVTRFQIIQFLIDLVFVYFATYTFYANKYFDGILPNKGTCYGTQDAAAYGYLILTSYLVLFISFYINSYKKGSKKKAEKEAEKAAAASATSSAVKTKSSKPSSRKA
Protein: Cell surface receptor daf-4 (EC 2.7.11.30) (Abnormal dauer formation protein 4) (P50488)
Organism: Caenorhabditis elegans
Function: Involved in a TGF-beta pathway. May be a receptor for TGF-beta-like ligand daf-7. Controls the decision of whether or not larvae enter a developmentally arrested state, known as dauer, in response to environmental conditions. Regulates body size and male tail patterning. Involved in regulating entry into quiescence triggered by satiety. Involved in sensitivity to CO2 levels.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21408209}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Protein dbl-1
- Serine/threonine-protein kinase receptor sma-6
- Dauer larva development regulatory growth factor daf-7
- Cell surface receptor daf-1
- Dwarfin sma.
- Smad-related protein daf-14
- TGF-beta family profile domain-containing protein
- Leucine-rich repeats and immunoglobulin-like domains protein sma-10
- Smad protein daf-8
- SMAll.
Sequence:
MNQKGTVRLKALVLICLPLFLIATPVPVAVTEDDRQDRIESEAAEKEWANTLVSKVAQSNGTGTIKVSAPAKPTLRRMDNEEDEVISIECVYYDEMECEKSGDCEITKKTCYSEAHLKAVGCLAVFGLPTQEINSTEPYLKVDKPQYKSLGCMPYQHADSMNCENESSCRQGRSFRGGIGMCCCSTNNCNMPDLIEMVNPSLKKDSDNSALLWASTPSNMDLESLDKFPFYWIIIIALSVILCIALLILAYVGWKFQQNKKEEIKKQQKIKFDMEKTDALEAGNVPLVEPEEEMIEMVETPKELPITDFQLISKGRFGKVFKAQYTPDSGEKRLVAVKKLNEFQKASFLAEKRIFDELNEYPKWYKSIVEFVCAEKIGDEYWIVTEFHERLSLYELLKNNVISITSANRIIMSMIDGLQFLHDDRPYFFGHPKKPIIHRDIKSKNILVKSDMTTCIADFGLARIYSYDIEQSDLLGQVGTKRYMSPEMLEGATEFTPTAFKAMDVYSMGLVMWEVISRTKLHQTDEPPNYQMPFQVIGFDPTIGLMRNYVVSKKERPQWRDEIIKHEYMSLLKKVTEEMWDPEACARITAGCAFARVWNHIMSSPDSSEGYHSGSSMKNRGVDDVEQSEKPEGIEEMQHYHASSPSKRQHPSPNPFFDSCPPPPPIPVILENGGILQPDNAEPEPEELPDLPIVEKIYDIATNMLFSREELDLMNAQRQVEYEAGADTRASTPTPSGTFGTFTT
Protein: Core-binding factor subunit beta (A0A8I6GMB2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPRVVPDQRSKFENEEFFRKLSRECEIKYTGFRDRPHEERQTRFQNACRDGRSEIAFVATGTNLSLQFFPASWQGEQRQTPSREYVDLEREAGKVYLKAPMILNGVCVIWKGWIDLHRLDGMGCLEFDEERAQQEDALAQQAFEEARRRTREFEDRDRSHREEMEARRQQDPSPGSNLGGDDLKLR
Protein: Uncharacterized protein At2g34510 (O64696)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- Helicase and polymerase-containing protein TEBICHI
Sequence:
MMLYSNNSWRSNSILILLLGLSIVAAADSAGKTSPVEDGLVVNGDFETPPSNGFPDDAIIEDTSEIPSWRSDGTVELIKSGQKQGGMILIVPEGRHAVRLGNDAEISQELTVEKGSIYSVTFSAARTCAQLESLNVSVASSDEPIASQTIDLQTVYSVQGWDPYAWAFEAVVDRVRLVFKNPGMEDDPTCGPIIDDIAVKKLFTPDKPKGNAVINGDFEEGPWMFRNTTLGVLLPTNLDEEISSLPGWTVESNRAVRFIDSDHFSVPEGKRALELLSGKEGIISQMVETKANIPYKMSFSLGHAGDKCKEPLAVMAFAGDQAQNFHYMAQANSSFERSELNFTAKAERTRIAFYSIYYNTRTDDMTSLCGPVIDDVKVWFSGSSRIGFSFPLFILLSLVFI
Protein: Pyridine nucleotide-disulfide oxidoreductase domain-containing protein 2 (EC 1.-.-.-) (Q8N2H3)
Organism: Homo sapiens (Human)
Function: Probable oxidoreductase that may play a role as regulator of mitochondrial function.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:31170524}. Note=The import into mitochondria is dependent on TOMM40 and TIMM23. {ECO:0000269|PubMed:31170524}.
Interaction partners:
- Squalene synthase
- WD repeat-containing protein 97
- NADH dehydrogenase complex I, assembly factor 6
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- UDP-glucose 4-epimerase
Sequence:
MAASGRGLCKAVAASPFPAWRRDNTEARGGLKPEYDAVVIGAGHNGLVAAAYLQRLGVNTAVFERRHVIGGAAVTEEIIPGFKFSRASYLLSLLRPQIYTDLELKKHGLRLHLRNPYSFTPMLEEGAGSKVPRCLLLGTDMAENQKQIAQFSQKDAQVFPKYEEFMHRLALAIDPLLDAAPVDMAAFQHGSLLQRMRSLSTLKPLLKAGRILGAQLPRYYEVLTAPITKVLDQWFESEPLKATLATDAVIGAMTSPHTPGSGYVLLHHVMGGLEGMQGAWGYVQGGMGALSDAIASSATTHGASIFTEKTVAKVQVNSEGCVQGVVLEDGTEVRSKMVLSNTSPQITFLKLTPQEWLPEEFLERISQLDTRSPVTKINVAVDRLPSFLAAPNAPRGQPLPHHQCSIHLNCEDTLLLHQAFEDAMDGLPSHRPVIELCIPSSLDPTLAPPGCHVVSLFTQYMPYTLAGGKAWDEQERDAYADRVFDCIEVYAPGFKDSVVGRDILTPPDLERIFGLPGGNIFHCAMSLDQLYFARPVPLHSGYRCPLQGLYLCGSGAHPGGGVMGAAGRNAAHVAFRDLKSM
Protein: Uncharacterized protein CT_671 (O84678)
Organism: Chlamydia trachomatis serovar D (strain ATCC VR-885 / DSM 19411 / UW-3/Cx)
Interaction partners:
- Type III secretion T3S chaperone
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein CT_665
- Flagellar Motor Switch Domain/YscQ family
- Uncharacterized protein CT_666
- Type 3 secretion system ATPase
- S/T Protein Kinase
Sequence:
MELNKTSESLFSAKIDHNHPRTEAHEPRDQREVRVFSLEGRSSTRQEKADRMPGRTSSRQESSKGSEEGAVHESTAGVSSKEEEESKGDGFFTGGNPTSGMALVETPMAVVSEAMVETSTMTVSQVDLQWVEQLVTSTVESLLVADIDGKQLVEIVLDNSNTVPAAFCGANLTLVQTGEEISVSFSNFVDQAQLTEATQLVQQNPKQLVSLVESLKARQLNLTELVVGNVAVSLPTIEKIETPLHMIAATIRHHDQEGDQEGEGRQDQHQGQHQEKKVEEAHI
Protein: 11-beta-hydroxysteroid dehydrogenase 1 (11-DH) (11-beta-HSD1) (EC 1.1.1.146) (7-oxosteroid reductase) (EC 1.1.1.201) (Corticosteroid 11-beta-dehydrogenase isozyme 1) (Short chain dehydrogenase/reductase family 26C member 1) (P28845)
Organism: Homo sapiens (Human)
Function: Controls the reversible conversion of biologically active glucocorticoids such as cortisone to cortisol, and 11-dehydrocorticosterone to corticosterone in the presence of NADP(H). Participates in the corticosteroid receptor-mediated anti-inflammatory response, as well as metabolic and homeostatic processes. Plays a role in the secretion of aqueous humor in the eye, maintaining a normotensive, intraocular environment. Bidirectional in vitro, predominantly functions as a reductase in vivo, thereby increasing the concentration of active glucocorticoids. It has broad substrate specificity, besides glucocorticoids, it accepts other steroid and sterol substrates. Interconverts 7-oxo- and 7-hydroxy-neurosteroids such as 7-oxopregnenolone and 7beta-hydroxypregnenolone, 7-oxodehydroepiandrosterone (3beta-hydroxy-5-androstene-7,17-dione) and 7beta-hydroxydehydroepiandrosterone (3beta,7beta-dihydroxyandrost-5-en-17-one), among others. Catalyzes the stereo-specific conversion of the major dietary oxysterol, 7-ketocholesterol (7-oxocholesterol), into the more polar 7-beta-hydroxycholesterol metabolite. 7-oxocholesterol is one of the most important oxysterols, it participates in several events such as induction of apoptosis, accumulation in atherosclerotic lesions, lipid peroxidation, and induction of foam cell formation. Mediates the 7-oxo reduction of 7-oxolithocholate mainly to chenodeoxycholate, and to a lesser extent to ursodeoxycholate, both in its free form and when conjugated to glycine or taurine, providing a link between glucocorticoid activation and bile acid metabolism. Catalyzes the synthesis of 7-beta-25-dihydroxycholesterol from 7-oxo-25-hydroxycholesterol in vitro, which acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10497248, ECO:0000269|PubMed:15280030}; Single-pass type II membrane protein {ECO:0000269|PubMed:10497248}.
Interaction partners:
- Aldo-keto reductase family 1 member D1
- Cytochrome P450 11B1, mitochondrial
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 11-beta-hydroxysteroid dehydrogenase type 2
- Cytochrome P450 11B2, mitochondrial
- Steroid 21-hydroxylase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Aldo-keto reductase family 1 member C4
- Cytochrome P450 3A4)
- Cytochrome P450 2E1
Sequence:
MAFMKKYLLPILGLFMAYYYYSANEEFRPEMLQGKKVIVTGASKGIGREMAYHLAKMGAHVVVTARSKETLQKVVSHCLELGAASAHYIAGTMEDMTFAEQFVAQAGKLMGGLDMLILNHITNTSLNLFHDDIHHVRKSMEVNFLSYVVLTVAALPMLKQSNGSIVVVSSLAGKVAYPMVAAYSASKFALDGFFSSIRKEYSVSRVNVSITLCVLGLIDTETAMKAVSGIVHMQAAPKEECALEIIKGGALRQEEVYYDSSLWTTLLIRNPCRKILEFLYSTSYNMDRFINK
Protein: Plexin-A1 (Semaphorin receptor NOV) (Q9UIW2)
Organism: Homo sapiens (Human)
Function: Coreceptor for SEMA3A, SEMA3C, SEMA3F and SEMA6D. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the affinity of the complex for specific semaphorins, and its cytoplasmic domain is required for the activation of down-stream signaling events in the cytoplasm (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P70206}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Neuropilin-1
- Semaphorin-3A
- Semaphorin-6D
- Neuropilin-2
- Semaphorin-3F
- Rho-related GTP-binding protein Rho6
- Rho-related GTP-binding protein RhoD
- Semaphorin-3C
- Tyrosine-protein kinase Fes/Fps
- Plexin-A4
Sequence:
MPLPPRSLQVLLLLLLLLLLLPGMWAEAGLPRAGGGSQPPFRTFSASDWGLTHLVVHEQTGEVYVGAVNRIYKLSGNLTLLRAHVTGPVEDNEKCYPPPSVQSCPHGLGSTDNVNKLLLLDYAANRLLACGSASQGICQFLRLDDLFKLGEPHHRKEHYLSSVQEAGSMAGVLIAGPPGQGQAKLFVGTPIDGKSEYFPTLSSRRLMANEEDADMFGFVYQDEFVSSQLKIPSDTLSKFPAFDIYYVYSFRSEQFVYYLTLQLDTQLTSPDAAGEHFFTSKIVRLCVDDPKFYSYVEFPIGCEQAGVEYRLVQDAYLSRPGRALAHQLGLAEDEDVLFTVFAQGQKNRVKPPKESALCLFTLRAIKEKIKERIQSCYRGEGKLSLPWLLNKELGCINSPLQIDDDFCGQDFNQPLGGTVTIEGTPLFVDKDDGLTAVAAYDYRGRTVVFAGTRSGRIRKILVDLSNPGGRPALAYESVVAQEGSPILRDLVLSPNHQYLYAMTEKQVTRVPVESCVQYTSCELCLGSRDPHCGWCVLHSICSRRDACERADEPQRFAADLLQCVQLTVQPRNVSVTMSQVPLVLQAWNVPDLSAGVNCSFEDFTESESVLEDGRIHCRSPSAREVAPITRGQGDQRVVKLYLKSKETGKKFASVDFVFYNCSVHQSCLSCVNGSFPCHWCKYRHVCTHNVADCAFLEGRVNVSEDCPQILPSTQIYVPVGVVKPITLAARNLPQPQSGQRGYECLFHIPGSPARVTALRFNSSSLQCQNSSYSYEGNDVSDLPVNLSVVWNGNFVIDNPQNIQAHLYKCPALRESCGLCLKADPRFECGWCVAERRCSLRHHCAADTPASWMHARHGSSRCTDPKILKLSPETGPRQGGTRLTITGENLGLRFEDVRLGVRVGKVLCSPVESEYISAEQIVCEIGDASSVRAHDALVEVCVRDCSPHYRALSPKRFTFVTPTFYRVSPSRGPLSGGTWIGIEGSHLNAGSDVAVSVGGRPCSFSWRNSREIRCLTPPGQSPGSAPIIININRAQLTNPEVKYNYTEDPTILRIDPEWSINSGGTLLTVTGTNLATVREPRIRAKYGGIERENGCLVYNDTTMVCRAPSVANPVRSPPELGERPDELGFVMDNVRSLLVLNSTSFLYYPDPVLEPLSPTGLLELKPSSPLILKGRNLLPPAPGNSRLNYTVLIGSTPCTLTVSETQLLCEAPNLTGQHKVTVRAGGFEFSPGTLQVYSDSLLTLPAIVGIGGGGGLLLLVIVAVLIAYKRKSRDADRTLKRLQLQMDNLESRVALECKEAFAELQTDIHELTNDLDGAGIPFLDYRTYAMRVLFPGIEDHPVLKEMEVQANVEKSLTLFGQLLTKKHFLLTFIRTLEAQRSFSMRDRGNVASLIMTALQGEMEYATGVLKQLLSDLIEKNLESKNHPKLLLRRTESVAEKMLTNWFTFLLYKFLKECAGEPLFMLYCAIKQQMEKGPIDAITGEARYSLSEDKLIRQQIDYKTLTLNCVNPENENAPEVPVKGLDCDTVTQAKEKLLDAAYKGVPYSQRPKAADMDLEWRQGRMARIILQDEDVTTKIDNDWKRLNTLAHYQVTDGSSVALVPKQTSAYNISNSSTFTKSLSRYESMLRTASSPDSLRSRTPMITPDLESGTKLWHLVKNHDHLDQREGDRGSKMVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDEQADKHQIHDADVRHTWKSNCLPLRFWVNVIKNPQFVFDIHKNSITDACLSVVAQTFMDSCSTSEHKLGKDSPSNKLLYAKDIPNYKSWVERYYADIAKMPAISDQDMSAYLAEQSRLHLSQFNSMSALHEIYSYITKYKDEILAALEKDEQARRQRLRSKLEQVVDTMALSS
Protein: tRNA (32-2'-O)-methyltransferase regulator THADA (Thyroid adenoma-associated protein homolog) (Q9VWB9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a key role in energy homeostasis by regulating the balance between energy storage and heat production. Functions by negatively regulating Ca(2+) signaling pathways that are involved in heat production and maintaining correct lipid storage in the fat body. Regulates Ca(2+) signaling pathways by reducing the activity of the calcium-transporting ATPase SERCA possibly by promoting uncoupling of SERCA ATP hydrolysis from calcium pumping. May also function in the nervous system to control feeding behavior.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:28399403}.
Interaction partners:
- tRNA
- tRNA
- tRNA
Sequence:
MNDLNLRVAALKVCAHPKRFAELRDALVPLPNTWIAAPHDFVLQFAAAKSSAEQVQVVKDVFYGEQAQDHEDVAHFLADLLLASPLKHAVRNQLTKLFSDNALAKQNASPHRRHSKEHLLEALQQSLGEMANSLAVITPPVSHERTNDVFVSANACLQNFPFGREALGKQVHRFAPLLTTALERYWADICDPTLELSPTRRNELYLYVQNALRFLVSLLAEWSDKLRLFEDQRFPGTSNAVAQKVARYYDTPWDVRSIAALLIGHLARFSGTFKAYVEDCSRPKAEQDVPIQMAALLVLRPVDYTENATLALAILKRIVAVSELKSTVTNLLVFLSKHLFIYSKSLGEMHAHLPDDQKLLYQRILAQLQVFALQNISSDTDSVRHMSSALLHQVLQHAQAAGQEELFQVVYRQFEDRAAYLNASCMALEQLVAVAGVSKSIENCPSLFGVIFPRHLGCEDCVDALFKAMMVSAHKTEPFAEWQSRWFGLLLAAIRVPEKRRQVIEELIAQAVQLEPTRLAQVLLPDDRLPLSCKLAAILGVRQLSARRQNLLRGMKEEVEQALIGLDDHTRLLALRFLVETPRPSELLNADQMGAIELYVRHNANNPSAHLRQLGYGLLQKALKRVHFGLVEYRKSRTPASQEVLQFLIRLIRTLAQNLFPTANYGRRWLSLRLLRDCLELSEMVGITFSELGIELPTEALMACLGDSYEHNKVLAAQLLERFQSHSLFKPDEMIELLLSLRPSDSATGAFQLQVYCKASRVQSEMPTPTHGGTIHEPLTFRALQWCLQHLREGLRLAQLDLGEAAKLNPLYGLLFASRHLLQQLKLKELAKEPQWRQYIDELVTMCLAVSSVVLPVVSSASPEGHLPETCDQETDQPLTNVLDRQLSREELLQVRTTPQMILLCAWRSSKEVCLILGELVQRAPLEEEEDEEQQQQQGDFLLSRAQLEAIGEHFLQLLAETKHRGAFEQAYVGFTMLCRRFWHSESVRLNQLPGQWVDEAMAMVSGQEEWAGKGARLCATRRSAGMPFMLQALVGTELKLGTHATLYRCMNRLLEVCERRTGGAAGITARSHALNIMRALFRSSELAELVTEFMARGIQCALDGLLLAEEWAERNSATLLLAALIVRVFGVERARLETGELHVRNRMTGRIFFTRYPQLFDYFHAALQRESEQMDAGGGGSENASGKRRQAVQLEAMLLMLSRLYPSSLEGAESTLNLSEFVPFLIRICHSHDLMTREMAALVVANFVTQEQALAEIRRIVVELKALQLRLKNTEAANTKLNTNVLHGQLLLLLHLHRLVRWTRPSLTRMQLHTLAELAAPLLQHDACAFSALVAVMVAAMEDAVEPGLLDFQLLEQIGVVYLLNHKEVQSRCQQLGISNRFYQIFGLHLHRLRGISQGIVLHIVEDLAETIWALDELKVELWLYILLQRSLSEQNSLVSEQDIEHFEFSRDIRRYFETLSREQREEVGQELYESPAVRSSVLHMMHMIKSSKNSCWSLQLAGRLAALQTLLRDPGLELNQLVQRCSEEHSTHQEAGLLLGLRRLIGESKMLERKHWLPMLNYAQRLVHPGQPVYLRHQAAELCDSLARNHLRDQLVAGTTDVDIGLVGRFSGLVLLLLHDDAEWVRHRAVQLVCGAGLRTRSGAGQEQEQSAMAPLILPSALIPPFLDTMIGKLTFDDFNMVQRLVDIIAEPFTTADAMELFDKQENNHYCERNHVLTELWDARGRADPRARTPTIPTGYQIFK