wanglab/gogpt-training-data huggingface dataset:
Protein: Probable fructokinase-3 (EC 2.7.1.4) (Q9LNE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play an important role in maintaining the flux of carbon towards starch formation.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Sorbitol dehydrogenase
- Hexokinase-3
- Hexokinase-4
- Hexokinase-like 1 protein
- Hexokinase-1
- Hexokinase-2
- Probable hexokinase-like 2 protein
- alpha-D-xyloside xylohydrolase
Sequence:
MASSTGEKGLIVSFGEMLIDFVPTVSGVSLSESPGFLKAPGGAPANVAIAVSRLGGRAAFVGKLGDDDFGHMLAGILRKNGVDDQGINFDEGARTALAFVTLRSDGEREFMFYRNPSADMLLRPDELNLELIRSAKVFHYGSISLITEPCRSAHMKAMEVAKEAGALLSYDPNLREPLWPSPEEARTQIMSIWDKADIIKVSDVELEFLTENKTMDDKTAMSLWHPNLKLLLVTLGEKGCTYFTKKFHGSVETFHVDAVDTTGAGDSFVGALLQQIVDDQSVLEDEARLRKVLRFANACGAITTTKKGAIPALPTDIEALSFLKDQKKRQTNLKFSKWCCTASPC
Protein: WCRKC thioredoxin 1 (F4K3Y1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAFENLKISRHISSSTKNLLKAKKIMAALASNPQMLTRQAHGNKKEQLWRKESLNLEKKCGFCVSVYSNEKLGRSHMEKEWRLKAFWSNIAQPTTLEMEPINNVEELDAVLSHARQLSQPIIIEWMASWCRKCIYLKPKLEKLAAEYNNRAKFYYVDVNKVPQTLVKRGNISVKCLNIILSFFSDVVCAKSEPITSIFVCYAENAYYSGMLTFI
Protein: Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Q9FMP8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a GTPase activator for the Rac-type GTPase by converting it to an inactive GDP-bound state.
Interaction partners:
- Rho GTPase-activating protein 1
- Rho GTPase-activating protein 2
- Rho GTPase-activating protein 5
- Rac-like GTP-binding protein ARAC1
- Rac-like GTP-binding protein ARAC5
- Rho GTPase-activating protein 4
- Rho GTPase-activating protein 3
- Rop guanine nucleotide exchange factor 6
- Rop guanine nucleotide exchange factor 5
Sequence:
MEASLAVIQRPQAGASNTVYKSGPLFISSKGLGWTSWKKRWFILTRTSLVFFKNDPSALPQKGGEVNLTLGGIDLNSSGSVVVREDKKLLTVLFPDGRDGRAFTLKAETLDDLYEWKAALEQALAQAPNAALVIGQNGIFRTEANNTIEASFNSWRDQRPLKSSVVGRPILLALEEIDGSPSFLEKALQFLETYGTKVEGILRQSADVEEVERRVQEYEQGKTEFSPEEDPHVVGDCVKHVLRQLPSSPVPASCCTALLEAYKIDQNEARVNSLRSAIIETFPEPNRRLLLRMLKMMHTITSHSSENRMTSSAVAACMSPLLLRPLLAGECDLEGFDTLGDNSAQLLAAANAANNAQAIVTALLEDYGNMINDEGLGRCSTSTDSHIGDSGPENSSDEEEIVVKHPDLHTLDIEEGETDDDNDVLLSRKPSESSDYAGSDLYDYKGFGVEDSDAESPRDIHCSVESTDFSARVKKHIEEPIKDIEVSSVSPTENCYQSGREAIPSVTPSTPLTALRYTTSAEKPASKTTGSSTVNSKRSSSWGRGNGKKTPAKGSFDSSGNDELLIQRLEHMKDELRQRIAKEAKGNAALQASLERRKQALHERRLALEQDVGRLQEQLQAERDLRSALEVGLSISCGQFSSQAADSKTRAELEEIALAEADVARLKQKVAELHHQLSQQRQHHLSSLPDAQSHHQFLHNHNTQLKSFQQDFDSILAFVNHERNQRTDETSLRADWRNGRGNNRQVPGSPSLNAASLGIPMEEYSPVMDYGRHHHPPATSAALMELTTRLDFFKERRSQLMEQIQNLDLNYGSSSSSLHRSSSPPWN
Protein: H(+)/Cl(-) exchange transporter 3 (Chloride channel protein 3) (ClC-3) (Chloride transporter ClC-3) (P51790)
Organism: Homo sapiens (Human)
Function: Strongly outwardly rectifying, electrogenic H(+)/Cl(-)exchanger which mediates the exchange of chloride ions against protons (By similarity). The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters.
Subcellular location: [Isoform 1]: Early endosome membrane {ECO:0000269|PubMed:12471024}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:12471024}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P51791}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P51792}; Multi-pass membrane protein {ECO:0000255}. Note=Isoform 1 is localized mainly in late endosomes. {ECO:0000269|PubMed:12471024}.; SUBCELLULAR LOCATION: [Isoform 2]: Golgi apparatus membrane {ECO:0000269|PubMed:12471024}; Multi-pass membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000269|PubMed:11967229}; Multi-pass membrane protein {ECO:0000269|PubMed:11967229}. Note=Isoform 2 is mainly enriched in the Golgi (PubMed:12471024). Colocalizes with NHERF1/EBP50 in membrane ruffles (PubMed:11967229). {ECO:0000269|PubMed:11967229, ECO:0000269|PubMed:12471024}.
Interaction partners:
- 72 kDa type IV collagenase
- Neuronal membrane glycoprotein M6-a
- ATP synthase F
- ATP synthase F
- H
- Osteopetrosis-associated transmembrane protein 1
- ATP synthase F
Sequence:
MESEQLFHRGYYRNSYNSITSASSDEELLDGAGVIMDFQTSEDDNLLDGDTAVGTHYTMTNGGSINSSTHLLDLLDEPIPGVGTYDDFHTIDWVREKCKDRERHRRINSKKKESAWEMTKSLYDAWSGWLVVTLTGLASGALAGLIDIAADWMTDLKEGICLSALWYNHEQCCWGSNETTFEERDKCPQWKTWAELIIGQAEGPGSYIMNYIMYIFWALSFAFLAVSLVKVFAPYACGSGIPEIKTILSGFIIRGYLGKWTLMIKTITLVLAVASGLSLGKEGPLVHVACCCGNIFSYLFPKYSTNEAKKREVLSAASAAGVSVAFGAPIGGVLFSLEEVSYYFPLKTLWRSFFAALVAAFVLRSINPFGNSRLVLFYVEYHTPWYLFELFPFILLGVFGGLWGAFFIRANIAWCRRRKSTKFGKYPVLEVIIVAAITAVIAFPNPYTRLNTSELIKELFTDCGPLESSSLCDYRNDMNASKIVDDIPDRPAGIGVYSAIWQLCLALIFKIIMTVFTFGIKVPSGLFIPSMAIGAIAGRIVGIAVEQLAYYHHDWFIFKEWCEVGADCITPGLYAMVGAAACLGGVTRMTVSLVVIVFELTGGLEYIVPLMAAVMTSKWVGDAFGREGIYEAHIRLNGYPFLDAKEEFTHTTLAADVMRPRRNDPPLAVLTQDNMTVDDIENMINETSYNGFPVIMSKESQRLVGFALRRDLTIAIESARKKQEGIVGSSRVCFAQHTPSLPAESPRPLKLRSILDMSPFTVTDHTPMEIVVDIFRKLGLRQCLVTHNGRLLGIITKKDILRHMAQTANQDPASIMFN
Protein: Glyceraldehyde-3-phosphate dehydrogenase A, chloroplastic (EC 1.2.1.13) (NADP-dependent glyceraldehydephosphate dehydrogenase subunit A) (P12858)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
Sequence:
MASATFSVAKPAIKANGKGFSEFSGLRNSSRHLPFSRKSSDDFHSLVTFQTNAVGSSGGHKKSLVVEAKQLKVAINGFGRIGRNFLRCWHGRKDSPLDVIAINDTGGVKQASHLLKYDSTLGIFDADVKPVGTDGISVDGKVIKVVSDRNPANLPWKELGIDLVIEGTGVFVDREGAGRHITAGAKKVLITAPGKGDIPTYVVGVNADAYTHADDIISNASCTTNCLAPFVKVLDQKFGIIKGTMTTTHSYTGDQRLLDASHRDLRRARAAALNIVPTSTGAAKAVALVLPTLKGKLNGIALRVPTPNVSVVDLVVQVSKKTFAEEVNEAFRESAAKELTGILSVCDEPLVSVDFRCTDVSSTVDSSLTMVMGDDLVKVIAWYDNEWGYSQRVVDLADIVANNWK
Protein: Histone H2A type 1 (H2A.1) (Histone H2A/ptl) (P0C0S8)
Organism: Homo sapiens (Human)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2B type 1-C/E/F/G/I
- Histone H2B type 2-E
- Histone H2B type 1-J
- Histone H4
- Histone H2B type 1-K
- Histone H2A type 1-J
- Ubiquitin-ribosomal protein eS31 fusion protein
- Histone H2B type 1-O
- Histone H3.2
- Histone H2B type 2-F
Sequence:
MSGRGKQGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHHKAKGK
Protein: Effector protein NleF (Non-LEE-encoded type III effector F) (Q8XAL7)
Organism: Escherichia coli O157:H7
Function: Effector protein that alters host cell physiology and promotes bacterial survival in host tissues. Inhibits the catalytic activity of human CASP4, CASP8 and CASP9, and thereby inhibits apoptosis of infected host cells.
Subcellular location: Secreted {ECO:0000269|PubMed:18279332}. Host cytoplasm {ECO:0000269|PubMed:18279332}. Note=Injected into host cells via a type III secretion system.
Interaction partners:
- T3SS secreted effector NleH
- Protein-arginine N-acetylglucosaminyltransferase NleB1
- T3SS secreted effector NleA/EspI
- Cysteine S-methyltransferase NleE
- E3 ubiquitin-protein ligase NleG
- T3SS secreted effector EspL
- T3SS secreted effector NleD
Sequence:
MLPTSGSSANLYSWMYVSGRGNPSTPESVSELNHNHFLSPELQDKLDVMVSIYSCARNNNELEEIFQELSAFVSGLMDKRNSVFEVRNENTDEVVGALRAGMTIEDRDSYIRDLFFLHSLKVKIEESRQGKEDSKCKVYNLLCPHHSSELYGDLRAMKCLVEGCSDDFNPFDIIRVPDLTYNKGSLQCG
Protein: Twinfilin-1 (F8VS81)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSHQTGIQDTPQGKLICMVACNACRQFNMQLYLTSIISWFEIGQPAASEDVKEIFARARNGKYRLLKISIENEQLVIGSYSQPSDSWDKDYDSFVLPLLEDKQPCYILFRLDSQNAQGYEWIFIAWSPDHSHVRQKMLYAATRATLKKEFGGGHIKDEVFGTVKEDVSLHGYKKYLLSQSSPAPLTAAEEELRQIKINEVQTDVGVDTKHQTLQGVAFPISREAFQALEKLNNRQLNYVQLEIDIKNEIIILANTTNTELKDLPKRIPKDSARYHFFLYKHSHEGDYLESI
Protein: Annexin A8 (Annexin VIII) (Annexin-8) (Vascular anticoagulant-beta) (VAC-beta) (P13928)
Organism: Homo sapiens (Human)
Function: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.
Interaction partners:
Sequence:
MAWWKSWIEQEGVTVKSSSHFNPDPDAETLYKAMKGIGTNEQAIIDVLTKRSNTQRQQIAKSFKAQFGKDLTETLKSELSGKFERLIVALMYPPYRYEAKELHDAMKGLGTKEGVIIEILASRTKNQLREIMKAYEEDYGSSLEEDIQADTSGYLERILVCLLQGSRDDVSSFVDPGLALQDAQDLYAAGEKIRGTDEMKFITILCTRSATHLLRVFEEYEKIANKSIEDSIKSETHGSLEEAMLTVVKCTQNLHSYFAERLYYAMKGAGTRDGTLIRNIVSRSEIDLNLIKCHFKKMYGKTLSSMIMEDTSGDYKNALLSLVGSDP
Protein: Double homeobox protein 1 (O43812)
Organism: Homo sapiens (Human)
Function: Probable transcription activator. Binds the P5 DNA element sequence 5'-GATCTGAGTCTAATTGAGAATTACTGTAC-3'.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:15709750, ECO:0000269|PubMed:9736770}. Note=Actively transported through the nuclear pore complex (NPC).
Interaction partners:
Sequence:
MALLTALDDTLPEEAQGPGRRMILLSTPSQSDALRACFERNLYPGIATKEELAQGIDIPEPRVQIWFQNERSCQLRQHRRQSRPWPGRRDPQKGRRKRTAITGSQTALLLRAFEKDRFPGIAAREELARETGLPESRIQIWFQNRRARHRGQSGRAPTQASIRCNAAPIG
Protein: Propionate--CoA ligase (EC 6.2.1.17) (Propionyl-CoA synthetase) (P55912)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Catalyzes the synthesis of propionyl-CoA from propionate and CoA. Also converts acetate to acetyl-CoA but with a lower specific activity.
Interaction partners:
- 2-methylcitrate synthase
- 2-methylcitrate dehydratase
- Propionate kinase
- Pyruvate formate lyase II
- Phosphate acetyltransferase
- Fatty acid oxidation complex subunit alpha
- Propionate kinase PduW
- Fatty acid oxidation complex subunit alpha
- Propanal dehydrogenase
- 2-methylisocitrate lyase
Sequence:
MSFSEFYQRSINEPEAFWAEQARRIDWRQPFTQTLDHSRPPFARWFCGGTTNLCHNAVDRWRDKQPEALALIAVSSETDEERTFTFSQLHDEVNIVAAMLLSLGVQRGDRVLVYMPMIAEAQITLLACARIGAIHSVVFGGFASHSVAARIDDARPALIVSADAGARGGKILPYKKLLDDAIAQAQHQPKHVLLVDRGLAKMAWVDGRDLDFATLRQQHLGASVPVAWLESNETSCILYTSGTTGKPKGVQRDVGGYAVALATSMDTIFGGKAGGVFFCASDIGWVVGHSYIVYAPLLAGMATIVYEGLPTYPDCGVWWKIVEKYQVNRMFSAPTAIRVLKKFPTAQIRNHDLSSLEALYLAGEPLDEPTASWVTETLGVPVIDNYWQTESGWPIMALARALDDRPSRLGSPGVPMYGYNVQLLNEVTGEPCGINEKGMLVIEGPLPPGCIQTIWGDDARFVKTYWSLFNRQVYATFDWGIRDAEGYYFILGRTDDVINIAGHRLGTREIEESISSYPNVAEVAVVGIKDALKGQVAVAFVIPKQSDTLADREAARDEENAIMALVDNQIGHFGRPAHVWFVSQLPKTRSGKMLRRTIQAICEGRDPGDLTTIDDPASLQQIRQAIEE
Protein: Nicotinamide phosphoribosyltransferase (NAmPRTase) (Nampt) (EC 2.4.2.12) (Pre-B-cell colony-enhancing factor 1) (Pre-B cell-enhancing factor) (Visfatin) (P43490)
Organism: Homo sapiens (Human)
Function: Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:24130902}. Cytoplasm {ECO:0000250|UniProtKB:Q99KQ4}. Secreted {ECO:0000269|PubMed:21741723}. Note=Under non-inflammatory conditions, visfatin predominantly exhibits a granular pattern within the nucleus. Secreted by endothelial cells upon IL-1beta stimulation. Abundantly secreted in milk, reaching 100-fold higher concentrations compared to maternal serum. {ECO:0000269|PubMed:21741723, ECO:0000269|PubMed:24130902}.
Interaction partners:
- NAD-dependent protein deacetylase sirtuin-1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide riboside kinase 1
- NAD-dependent protein deacetylase sirtuin-3, mitochondrial
- Nicotinamide N-methyltransferase
- NAD-dependent protein deacylase sirtuin-6
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
- NAD-dependent protein lipoamidase sirtuin-4, mitochondrial
- NAD-dependent protein deacetylase sirtuin-2
Sequence:
MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFYGLQYILNKYLKGKVVTKEKIQEAKDVYKEHFQDDVFNEKGWNYILEKYDGHLPIEIKAVPEGFVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGLALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIVSRSTQAPLIIRPDSGNPLDTVLKVLEILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINTLQEIVEGMKQKMWSIENIAFGSGGGLLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVADPNKRSKKGRLSLHRTPAGNFVTLEEGKGDLEEYGQDLLHTVFKNGKVTKSYSFDEIRKNAQLNIELEAAHH
Protein: Syntrophin-1 (Q93646)
Organism: Caenorhabditis elegans
Function: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the dystrophin glycoprotein complex (DGC). May also act by slowing calcium channel activity via a direct or indirect mechanism potentially involving other second messengers. Plays an early role in the formation of the neuromuscular junction and is necessary for muscle maintenance.
Subcellular location: Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Dystrobrevin-1
- Dystrophin-1
- Interactor with SLO-1
- Dystroglycan-type cadherin-like domain-containing protein
- Dystrophin-like protein 1
- Sarcoglycan complex subunit protein
- Beta-sarcoglycan
- Alpha-catulin
- PDZ domain-containing protein
- Dystroglycan 1
Sequence:
MAAVRSGLVDIFVQGQWHRVLATLDPTAITLQTMEQNEAEAEKRTVRVVKYDGNGLGISIKGGRDNNMPIVISKIFKGMAADQAGELFLDDVIISVNGENLLDASHEEAVRALKRAGRVVDLQVQYRREDMMHRENIVENVEWDDDIRERVRTIGLKLAYVARAGIDADAEGRILEMRSPSGRYSLAMRCSSSEEADGWFEALHACTTCLLTQALAQVNIMLGNNPQVRHMGWIAEQVSENGISMWKPKFMTLTNSEILFYEAVPQLKAEWAEPRLVRPLVATRVVQTSSRTAPVIKGLTDVISFRMRTGTQQGVRTHTIRVETHAELARWVRAVVIGGYEACLSTSQVSAPCLWRGESCELIVNLDNGISLLSSTGEVLWQHSFETIRATGDDGGRFLWVDFGPPHGEQELDLLNSAKPVVFILHSFLATKVYRLGLYA
Protein: Uncharacterized protein (Q57X47)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
Sequence:
MCFIFGVEMSNLAKRPMSLRKLPQLLLLIMIGIAFVAVECIGAPVKLPRRVDTVAGQFGVEGETNGYPNTTRLTEPYALCRGRTNDEILVGSSNSFRNYSRKTKETGTYLRYNVGDSVISGSSTINKPRSCVRRGSGNHTIIYFVDDQKDIKYIVGDDVSSFSVPTSGSLNAVAVHEGTLYVTDQNNKSVWKCGLGGAGKPQSCEEKKFTSVTLDAKPEGIAVTSKGIFVTARDSSNKGALLWLDMSGGNRKGNVSGGFVDVFSTESGVLYAATEKELYTVTATDTSLSVTSFAGKNTSQCYFPTNGEDIVLCDNSRLLVIEEYEMYVTSKAKHTMRALTLPPVNLTAIFRGRPAPVGYPNTTIMEQFVASLTEDVNKALGTNDSYVDPDSVRVDPDTWETNFTVFVQQTRFDNTTEEKLRSLTYTQTDKTVDEYYGLTDEYVYIDTVLVPFCDDASLVTIQRALAREAGRALNFSLVYADKPITFGSDVAENVTAVKLLMPHSFKNATTPKQLSAANLTDFAHNLVKDLRASDTRVDITFPDPPFNFSAVVPEREQEVRWFVHGKVMKQLEICERLGSQGDAAVIAAAADATARGKANVTLNTSGVKANDTGVGPNTTNTAGGANTTANVAANGTANVIVNPSTNATPTGTTNASVTNTTERAVPVVAPTQPSNGYAECRSAITNRTETQNMEPPYDRKHRYEVFLPKKYDFNVSWCVDIIDWRDLDEMLNNRTDEVVEKSLSWCGHGCIIAFAVVGSLIAACLVVLAVVLTSKRRRLAAVVAPPRPKFVSTVEDDDEDRVSNIGVPLTDGKGTTAP
Protein: Amino acid transporter (M0R063)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}.
Interaction partners:
Sequence:
MSSHGNSLFLRESGQRLGRVGWLQRLQESLQQRALRTRLRLQTMTLEHVLRFLRRNAFILLTVSAVVIGVSLAFALRPYQLTYRQIKYFSFPGELLMRMLQMLVLPLIVSSLVTGMASLDNKATGRMGMRAAVYYMVTTIIAVFIGILMVTIIHPGKGSKEGLHREGRIETIPTADAFMDLIRNMFPPNLVEACFKQFKTQYSTRVVTRTMVRTENGSEPGASMPPPFSVENGTSFLENVTRALGTLQEMLSFEETVPVPGSANGINALGLVVFSVAFGLVIGGMKHKGRVLRDFFDSLNEAIMRLVGIIICSATLPITFRCLEEGLGVDRRITRFVLPVGATVNMDGTALYEALAAIFIAQVNNYELNLGQITTISITATAASVGAAGIPQAGLVTMVIVLTSVGLPTEDITLIIAVDWFLDRLRTMTNVLGDSIGAAVIEHLSQRELELQEAELTLPSLGKPYKSLMAQEKGASRGRGGNESAM
Protein: IGF-like family receptor 1 (Transmembrane protein 149) (Q3U4N7)
Organism: Mus musculus (Mouse)
Function: Probable cell membrane receptor for the IGF-like family protein IGFL.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21454693}; Single-pass type I membrane protein {ECO:0000269|PubMed:21454693}.
Interaction partners:
- Insulin growth factor-like family member
Sequence:
MGPSWLLWTVAVAVLLLTRAASMEASSFCGHLEYWNSDKRCCSRCLQRFGPPACPDHEFTENCGLNDFGDTVAHPFKKCSPGYCNPNGTELCSQCSSGAAAAPAHVESPGRTHKQCRKKPVPPKDVCPLKPEDAGASSSPGRWSLGQTTKNEVSSRPGFVSASVLPLAVLPLLLVLLLILAVVLLSLFKRKVRSRPGSSSAFGDPSTSLHYWPCPGTLEVLESRNRGKANLLQLSSWELQGLASQPLSLLLDELEVLEELIMLLDPEPGPSGSTAYGTTRHLAARYGLPATWSTFAYSLRPSRSPLRALIEMVVAREPSATLGQFGTYLAQLGRTDALQVLSKLG
Protein: Putative membrane protein IgaA homolog (P45800)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Outer membrane lipoprotein RcsF
- Sensor histidine kinase RcsC
- Phosphotransferase RcsD
- GMP/IMP nucleotidase YrfG
- Transcriptional regulatory protein RcsB
- Transcriptional regulatory protein RcsA
Sequence:
MSTIVIFLAALLACSLLAGWLIKVRSRRRQLPWTNAFADAQTRKLTPEERSAVENYLESLTQVLQVPGPTGASAAPISLALNAESNNVMMLTHAITRYGISTDDPNKWRYYLDSVEVHLPPFWEQYINDENTVELIHTDSLPLVISLNGHTLQEYMQETRSYALQPVPSTQASIRGEESEQIELLNIRKETHEEYALSRPRGLREALLIVASFLMFFFCLITPDVFVPWLAGGALLLLGAGLWGLFAPPAKSSLREIHCLRGTPRRWGLFGENDQEQINNISLGIIDLVYPAHWQPYIAQDLGQQTDIDIYLDRHVVRQGRYLSLHDEVKNFPLQHWLRSTIIAAGSLLVLFMLLFWIPLDMPLKFTLSWMKGAQTIEATSVKQLADAGVRVGDTLRISGTGMCNIRTSGTWSAKTNSPFLPFDCSQIIWNDARSLPLPESELVNKATALTEAVNRQLHPKPEDESRVSASLRSAIQKSGMVLLDDFGDIVLKTADLCSAKDDCVRLKNALVNLGNSKDWDALVKRANAGKLDGVNVLLRPVSAESLDNLVATSTAPFITHETARAAQSLNSPAPGGFLIVSDEGSDFVDQPWPSASLYDYPPQEQWNAFQKLAQMLMHTPFNAEGIVTKIFTDANGTQHIGLHPIPDRSGLWRYLSTTLLLLTMLGSAIYNGVQAWRRYQRHRTRMMEIQAYYESCLNPQLITPSESLIE
Protein: Agouti-signaling protein (Agouti switch protein) (B3DGI7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Melanocyte-stimulating hormone receptor
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Agouti-related peptide 2 2b)
- Agouti-related neuropeptide.
- Dopachrome tautomerase.
- Tyrosinase.
- Sodium/potassium/calcium exchanger 5
- Melanocortin receptor 4
- Pro-opiomelanocortin protein
Sequence:
MSPSLWLCCVLLCLVCCVTVHTHMPMEEQHSSNQSNSNLLANNQTDAPPVLIIGLSKTPKKSKKSEKKPKKKFPNKVKRPPPPPNCVPLWASCKSPNAVCCDQCAFCHCRLLKTVCYCRMGYPKC
Protein: DRBM domain-containing protein (RNA interference promoting factor) (G5EBF5)
Organism: Caenorhabditis elegans
Interaction partners:
- Endoribonuclease dcr-1
- Piwi domain-containing protein
- Dicer-related helicase
- Ribonuclease 3
- Piwi-like protein ergo-1
- Protein argonaute-1
- Argonaute protein hrde-1
- Nuclear RNAi defective-3 protein
- 3'-5' exonuclease eri-1
- Protein argonaute-1
Sequence:
MDLTKLTFESVFGGSDVPMKPSRSEDNKTPRNRTDLEMFLKKTPLMVLEEAAKAVYQKTPTWGTVELPEGFEMTLILNEITVKGQATSKKAARQKAAVEYLRKVVEKGKHEIFFIPGTTKEEALSNIDQISDKAEELKRSTSDAVQDNDNDDSIPTSAEFPPGISPTENWVGKLQEKSQKSKLQAPIYEDSKNERTERFLVICTMCNQKTRGIRSKKKDAKNLAAWLMWKALEDGIESLESYDMVDVIENLEEAEHLLEIQDQASKIKDKHSALIDILSDKKRFSDYSMDFNVLSVSTMGIHQVLLEISFRRLVSPDPDDLEMGAEHTQTEEIMKATAEKEKLRKKNMPDSGPLVFAGHGSSAEEAKQCACKSAIIHFNTYDFTD
Protein: Agroclavine dehydrogenase (EC 1.5.1.46) (Ergot alkaloid biosynthesis protein G) (P0CT21)
Organism: Claviceps purpurea (Ergot fungus) (Sphacelia segetum)
Function: Agroclavine dehydrogenase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid. DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan. The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity). The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde. Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione. The presence of easA is not required to complete this reaction. Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA. Paspalic acid is then further converted to D-lysergic acid. Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit. LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone. LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines. LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C.purpurea. D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams. Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent dioxygenase easH which introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group.
Interaction partners:
Sequence:
MTVLLTGGTGRTAKHIAGIFRQTNVPFLVASRSSSAGTAENHRKFDWLDEETFPNALSVDQGMKPISVVWLCPPPLYDLATPVIKFIDFAVSQNVKKFVLLSASVIQKGGPAMGKIHGHLDSIKDVTYTVLRPTWFMENFSTKGEIQCEAIRRDSTVYSATENGKIPFISVVDIARVAACALTAETLKNSDHILQGPDLLTYDEVAQALTGVLGRKITHTKMTEGELAEKLMEEGVTPEEAYMHAAMDSMIKSGSEERVVSDEVKEWTGVKPRGFINFALSEKAAWRARK
Protein: Sulphydryl oxidase Sox from patent EP565172-A1-Aspergillus niger (EC 1.-.-.-) (A2QUK3)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MAPKSLFYSLFSTISVALASSIPQTDYDVIVVGGGPAGLSVLSSLGRMRRKTVMFDSGEYRNGVTREMHDVLGFDGTPPAQFRGLARQQISKYNSTSVIDIKIDSITPVEDAAANSSYFRAVDANGTQYTSRKVVLGTGLVDVIPDVPGLREAWGKGIWWCPWCDGYEHRDEPLGILGGLPDVVGSVMETHTLYSDIIAFTNGTYTPANEVALAAKYPNWKQQLEAWNVGIDNRSIASIERLQDGDDHRDDTGRQYDIFRVHFTDGSSVVRNTFITNYPTAQRSTLPEELSLVMVDNKIDTTDYTGMRTSLSGVYAVGDCNSDGSTNVPHAMFSGKRAGVYVHVEMSREESNAAISKRDFDRRALEKQTERMVGNEMEDLWKRVLENHHRRS