wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein uS5 (30S ribosomal protein S5) (P0A7W1)
Organism: Escherichia coli (strain K12)
Function: With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).
Interaction partners:
- Small ribosomal subunit protein uS13
- Elongation factor Tu 1
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL14
- DNA-directed RNA polymerase subunit alpha
- Large ribosomal subunit protein uL30
- GTP pyrophosphokinase
- Small ribosomal subunit protein uS7
Sequence:
MAHIEKQAGELQEKLIAVNRVSKTVKGGRIFSFTALTVVGDGNGRVGFGYGKAREVPAAIQKAMEKARRNMINVALNNGTLQHPVKGVHTGSRVFMQPASEGTGIIAGGAMRAVLEVAGVHNVLAKAYGSTNPINVVRATIDGLENMNSPEMVAAKRGKSVEEILGK
Protein: Adenylosuccinate lyase (ADSL) (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) (P30566)
Organism: Homo sapiens (Human)
Function: Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate.
Interaction partners:
- Bifunctional purine biosynthesis protein ATIC
- Adenylosuccinate synthetase isozyme 1
- Adenylosuccinate synthetase isozyme 2
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Trifunctional purine biosynthetic protein adenosine-3
- Amidophosphoribosyltransferase
- Adenylate kinase 9
- Adenine phosphoribosyltransferase
- Adenylate kinase isoenzyme 6
- Adenosine kinase
Sequence:
MAAGGDHGSPDSYRSPLASRYASPEMCFVFSDRYKFRTWRQLWLWLAEAEQTLGLPITDEQIQEMKSNLENIDFKMAAEEEKRLRHDVMAHVHTFGHCCPKAAGIIHLGATSCYVGDNTDLIILRNALDLLLPKLARVISRLADFAKERASLPTLGFTHFQPAQLTTVGKRCCLWIQDLCMDLQNLKRVRDDLRFRGVKGTTGTQASFLQLFEGDDHKVEQLDKMVTEKAGFKRAFIITGQTYTRKVDIEVLSVLASLGASVHKICTDIRLLANLKEMEEPFEKQQIGSSAMPYKRNPMRSERCCSLARHLMTLVMDPLQTASVQWFERTLDDSANRRICLAEAFLTADTILNTLQNISEGLVVYPKVIERRIRQELPFMATENIIMAMVKAGGSRQDCHEKIRVLSQQAASVVKQEGGDNDLIERIQVDAYFSPIHSQLDHLLDPSSFTGRASQQVQRFLEEEVYPLLKPYESVMKVKAELCL
Protein: Probable fructokinase-6, chloroplastic (EC 2.7.1.4) (Q9C524)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play an important role in maintaining the flux of carbon towards starch formation.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Sorbitol dehydrogenase
- Hexokinase-like 1 protein
- Hexokinase-4
- Hexokinase-3
- Hexokinase-2
- Hexokinase-1
- Probable hexokinase-like 2 protein
- alpha-D-xyloside xylohydrolase
Sequence:
MALQATTTTFCFSGPTFRSTPHSLTSKRPISIKATTSSPSRLSNSRSNLKGRALSSDGSTQESPYVVCFGEMLIDFVPTTSGLSLADAPAFKKAPGGAPANVAVGIARLGGSSAFIGKVGEDEFGYMLANILKDNNVNNDGMRFDPGARTALAFVTLTNEGEREFMFYRNPSADMLLEESELDFDLIKKAKIFHYGSISLITEPCKSAHISAAKAAKEAGVILSYDPNLRLPLWPSADNAREEILSIWETADIIKISEEEIVFLTKGEDPYDDNVVRKLFHPKLKLLLVTEGPEGCRYYTKDFSGRVHGLKVDVVDTTGAGDAFVAGILSQLANDLSLLQDEERLREALMFANACGALTVKVRGAIPALPTKEAVHEALLKAVV
Protein: Family with sequence similarity 126 member A isoform 3 (A0A0S2Z6M9)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MFTSEKGVVEEWLSEFKTLPETSLPNYATNLKDKSSLVSSLYKVIQEPQSELLEPVCHQLFEFYRSGEEQLLQFTLQFLPELIWCYLAVSASRNVHSSGCIEALLLGVYNLEIVDKQGHTKVLSFTIPSLSKPSVYHEPSSIGSMALTESALSQHGLSKVVYSGPHPQREMLTAQNRFEVLTFLLLCYNAALTYMPSVSLQSLCQICSRICVCGYPRQHVRKYKGISSRIPVSSGFMVQMLTGIYFAFYNGEWDLAQKALDDIIYRAQLELYPEPLLVANAIKASLPHGPMKSNKEGTRCIQVEITPTSSRISRNAVTSMSIRGHRWKRHEQPDNNNDATELGILVIPEISVTNVAGERTGNGEKGRTLGEIDAQHIQGVQETATDPRTESKGLPEIRRQKSEIQN
Protein: PWWP domain containing 3A, DNA repair factor (A0A0D9SGJ8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMADAKYVLCRWEKRLWPAKVLARTATSTKNKRRKEYFLAVQILSLEEKIKVKSTEVEILEKSQIEAIASSLASQNEVPAAPLEELAYRRSLRVALDVLSEGSIWSQESSAGTGRADRSLRGKPMEHVSSPCDSNSSSLPRGDVLGSSRPHRRRPCVQQSLSSSFTCEKDPECKVDHKKGLRKSENPRGPLVLPAGGGAQDESGSRIHHKNWTLASKRGGNSAQKASLCLNGSSLSEDDTERDMGSKGGSWAAPSLPSGVREDDPCANAEGHDPGLPLGSLTAPPAPEPSACSEPGECPAKKRPRLDGSQRPPAVQLEPMAAGAAPSPGPGPGPRESVTPRSTARLGPPPSHASADATRCLPCPDSQKLEKECQSSEESMGSNSMRSILEEDEEDEEPPRVLLYHEPRSFEVGMLVWHKHKKYPFWPAVVKSVRQRDKKASVLYIEGHMNPKMKGFTVSLKSLKHFDCKEKQTLLNQAREDFNQDIGWCVSLITDYRVRLGCGSFAGSFLEYYAADISYPVRKSIQQDVLGTKLPQLSKGSPEEPVVGCPLGQRQPCRKMLPDRSRAARDRANQKLVEYIVKAKGAESHLRAILKSRKPSRWLQTFLSSSQYVTCVETYLEDEGQLDLVVKYLQGVYQEVGAKVLQRTNGDRIRFILDVLLPECWEMRVRALDPVRRRSRLLDPCAEMELLRSCQHQGVRTPSLLRAHRCFPASVGHHLCDLCGGRGGLQDG
Protein: Phenazine biosynthesis protein PhzA2 (Q9I2J9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the biosynthesis of the antibiotic phenazine, a nitrogen-containing heterocyclic molecule having important roles in virulence, competition and biological control. PhzA2 (operon phzA2B2C2E2F2G2) has a role in the biosynthesis of the phenazine during both planktonic growth and biofilm development, and in host infection during biofilm development.
Interaction partners:
- Probable pyridoxamine 5'-phosphate oxidase
- Trans-2,3-dihydro-3-hydroxyanthranilate isomerase
- 5-methylphenazine-1-carboxylate 1-monooxygenase
- Phenazine-1-carboxylate N-methyltransferase
- anthranilate synthase
- Phenazine biosynthesis protein PhzD1
- asparagine synthase
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- HTH-type quorum-sensing regulator RhlR
- Transcriptional activator protein LasR
Sequence:
MREYQRLKGFTDNLELRRRNRATVEHYMRMKGAERLQRHSLFVEDGCAGNWTTESGEPLVFRGHESLRRLAEWLERCFPDWEWHNVRIFETEDPNHFWVECDGRGKALVPGYPQGYCENHYIHSFELENGRIKRNREFMNPMQKLRALGIAVPQIKRDGIPT
Protein: Snake venom metalloproteinase HF-1 (BmHF-1) (SVMP) (EC 3.4.24.-) (P86802)
Organism: Bothrops marajoensis (Marajo lancehead)
Function: Snake venom zinc metalloprotease that is weakly hemorrhagic and has Aalpha, Bbeta fibrinogenolytic activities. Cleaves the Aalpha chain of fibrinogen first, followed by the Bbeta chain and shows no effect on the gamma chain. Has caseinolytic activity. Induces dose-dependent edema.
Subcellular location: Secreted {ECO:0000269|PubMed:20607373}.
Interaction partners:
Sequence:
PCWKGWSEDEQNLWPQRYIQLVVVADHGMFMKYNGDLAAIRKRVHELVNNINGFYRSLNIDVSLTDLEIWSDQDFITVVQSSSAKNTLNSFGEWREADLLRRKSHDHAQLLTAIDLDDDTVGLAYTSSMCNPRKSVAWGQDHSEEPINLLDVGVTMAHELGHNLGMNHDEEKKCHCGASLCIMSPSITEGPSLEFSDDSMGYYQSFLVVVNYNPQCILNKPEDQYYYILSPKHRIYSW
Protein: Perilipin-1 (Lipid droplet-associated protein) (P43884)
Organism: Rattus norvegicus (Rat)
Function: Modulator of adipocyte lipid metabolism. Coats lipid storage droplets to protect them from breakdown by hormone-sensitive lipase (HSL). Its absence may result in leanness. Plays a role in unilocular lipid droplet formation by activating CIDEC. Their interaction promotes lipid droplet enlargement and directional net neutral lipid transfer. May modulate lipolysis and triglyceride levels (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:O60240}. Lipid droplet {ECO:0000250|UniProtKB:O60240}. Note=Lipid droplet surface-associated. {ECO:0000250|UniProtKB:O60240}.
Interaction partners:
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Hormone-sensitive lipase
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Perilipin-5
- Perilipin
- Lipid transferase CIDEC
- cGMP-dependent protein kinase 2
- 30 kDa adipocyte complement-related protein
- Caveolin-1
Sequence:
MSMNKGPTLLDGDLPEQENVLQRVLQLPVVSGTCECFQKTYNSTKEAHPLVASVCNAYEKGVQGASNLAAWSMEPVVRRLSTQFTAANELACRGLDHLEEKIPALQYPPEKIASELKGTISTRLRSARNSISVPIASTSDKVLGATLAGCELALGMAKETAEYAANTRVGRLASGGADLALGSIEKVVEYLLPPDKVESAPSSGRQKTQKAPKAKPSLLRRVSTLANTLSRHTMQTTARALKRGHSLAMWIPGVAPLSSLAQWGASAAMQVVSRRQSEVRVPWLHNLAASKDENHEDQTDTEGEETDEEEEEEESEAEENVLREVTALPTPLGFLGGVVHTVQKTLQNTISAVTWAPAAVLGTVGRILHLTPAQAVSSTKGRAMSLSDALKGVTDNVVDTVVHYVPLPRLSLMEPESEFQDIDNPPAEVERKGSGSRPASPESTARPGQPRAACAVRGLSAPSCPDLDDKTETSARPGLLAMPREKPARRVSDSFFRPSVMEPILGRTQYSQLRKKS
Protein: Solute carrier family 22 member 6 (Kidney-specific transport protein) (Novel kidney transcript) (mNKT) (Organic anion transporter 1) (mOAT1) (Renal organic anion transporter 1) (mROAT1) (Q8VC69)
Organism: Mus musculus (Mouse)
Function: Involved in the renal elimination of endogenous and exogenous organic anions. Functions as organic anion exchanger when the uptake of one molecule of organic anion is coupled with an efflux of one molecule of endogenous dicarboxylic acid (glutarate, ketoglutarate, etc). Mediates the transport of prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) and may be involved in their renal excretion (By similarity). May contribute to the transport of organic compounds in testes across the blood-testis-barrier (By similarity). Also mediates the sodium-independent uptake of 2,3-dimercapto-1-propanesulfonic acid (DMPS), cidofovir, adefovir, 9-(2-phosphonylmethoxyethyl) guanine (PMEG), 9-(2-phosphonylmethoxyethyl) diaminopurine (PMEDAP), ochratoxin (OTA), acyclovir (ACV), 3'-azido-3-'deoxythymidine (AZT), cimetidine (CMD), 2,4-dichloro-phenoxyacetate (2,4-D), hippurate (HA), indoleacetate (IA), indoxyl sulfate (IS) and 3-carboxy-4-methyl-5-propyl-2-furanpropionate (CMPF) and edaravone sulfate (By similarity). Mediates the sodium-independent uptake of p-aminohippurate (PAH). PAH uptake is inhibited by benzothiazolylcysteine (BTC), S-chlorotrifluoroethylcysteine (CTFC), cysteine S-conjugates S-dichlorovinylcysteine (DCVC), furosemide, steviol, phorbol 12-myristate 13-acetate (PMA), calcium ionophore A23187, benzylpenicillin, bumetamide, losartan, probenecid, phenol red, urate, glutarate and alpha-ketoglutarate (By similarity). PAH uptake is inhibited by p-chloromercuribenzenesulphonate (PCMBS), diethyl pyrocarbonate (DEPC), indomethacin, sulindac, diclofenac, carprofen, okadaic acid and PKC activators.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:10744714, ECO:0000269|PubMed:14979872, ECO:0000269|PubMed:15944205}; Multi-pass membrane protein {ECO:0000305}. Basal cell membrane {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane protein {ECO:0000305}. Note=Localized to the basolateral side of proximal convoluted tubules corresponding to tubule segments S1 and S2. {ECO:0000269|PubMed:15944205}.
Interaction partners:
- ATP-binding cassette sub-family C member 2
- Solute carrier family 15 member 1
- Multidrug and toxin extrusion protein 1
- Sodium-dependent phosphate transport protein 1
- Solute carrier family 17
- Organic anion transporter 3
- Solute carrier organic anion transporter family member 4C1
Sequence:
MAFNDLLKQVGGVGRFQLIQVTMVVAPLLLMASHNTLQNFTAAIPAHHCRPPANANLSKDGGLEAWLPLDKQGRPESCLRFPFPHNGTEANGTGVTEPCLDGWVYDNSTFPSTIVTEWNLVCSHRAFRQLAQSLFMVGVLLGAMMFGYLADRLGRRKVLILNYLQTAVSGTCAAYAPNYTVYCIFRLLSGMSLASIAINCMTLNMEWMPIHTRAYVGTLIGYVYSLGQFLLAGIAYAVPHWRHLQLAVSVPFFVAFIYSWFFIESARWYSSSGRLDLTLRALQRVARINGKQEEGAKLSIEVLQTSLQKELTLNKGQASAMELLRCPTLRRLFLCLSMLWFATSFAYYGLVMDLQGFGVSMYLIQVIFGAVDLPAKFVCFLVINSMGRRPAQLASLLLAGICILVNGIIPRGHTIIRTSLAVLGKGCLASSFNCIFLYTGELYPTMIRQTGLGMGSTMARVGSIVSPLISMTAEFYPSIPLFIFGAVPVAASAVTALLPETLGQPLPDTVQDLKSRSRGKQKQQQLEQQKQMIPLQVSTQEKNGL
Protein: AMP deaminase (EC 3.5.4.6) (Myoadenylate deaminase) (P50998)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: AMP deaminase plays a critical role in energy metabolism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Adenine phosphoribosyltransferase
- Inosine-5'-monophosphate dehydrogenase
- Adenosine kinase
- Adenylosuccinate synthetase
- Adenylate kinase
- Adenylosuccinate lyase
- IMP-specific 5'-nucleotidase 1
- Inosine triphosphate pyrophosphatase
- Bifunctional purine biosynthesis protein ade10
- Golgi apyrase
Sequence:
MNMEQEDDQVPAVAAETVPLKRYVTNPGANRDEEVAAAPSSQDTPYFDYAYERSLRHQDAKFLAMNGTQNGRDGLPSKSPRRPSVSASTVRNSDDVNHSKAGPGSGKLLNDTLQSKISSIHMPHVQQGDNAVVSSVGGPETDPGNMETTDPLFSDELAEIYLSIHKCMDMRHKYIRVSLQGELDNPIDDDSWIIYPDCKEGEDDTGLFNFADCKIPGIENEMEYHMDHQGIFQVYENDSAYIAGTPSFHIPTIRDYYIDLEFLLSASSDGPSKSFSFRRLQYLEGRWNMYMLLNEYQELADTKKVPHRDFYNVRKVDTHVHHSALANQKHLLRFIKAKLRKCPNEKVIWRDGKFLTLQEVFDSLKLTSYDLSIDTLDMHAHTDTFHRFDKFNLKYNPIGESRLRTIFLKTDNDINGRYLAELTKEVFTDLRTQKYQMAEYRISIYGRNREEWDKLAAWIIDNELFSPNVRWLIQVPRLYDVYKKSGIVETFEEVVRNVFEPLFEVTKDPRTHPKLHVFLQRVIGFDSVDDESKPERRTFRKFPYPKHWDINLNPPYSYWLYYMYANMTSLNSWRKIRGFNTFVLRPHCGEAGDTDHLASAFLLSHGINHGILLRKVPFLQYLWYLDQIPIAMSPLSNNALFLAYDKNPFLTYFKRGLNVSLSTDDPLQFAFTREPLIEEYAVAAQIYKLSAVDMCELARNSVLQSGFERQLKERWLGVDFQDIDRTNVPIIRLAYRALTLTQEIALVNKHVQPSKHPSNHDLEELIHKYDAMTGTSDPLSASPRTNDATISSRLSLHDGHDHGAFFPGLSVISERRRRKDSMASSSQDLKD
Protein: Auxilin (J domain-containing protein) (G5EDJ6)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable clathrin heavy chain 1
- Clathrin light chain
- Protein kinase domain-containing protein
- Dynamin
- Synaptojanin
- Amphiphysin
- Endocytosis protein RME-8
- J domain-containing protein
- Vacuolar protein sorting-associated protein 35
- ENTH domain-containing protein
Sequence:
MVFDEEPPAQKKWTQQATTSAFGLMESLKGQGSSLAKNLKNFGKSLVKEHKSQGATTPPEHRDDDIRLTWLTNRIVLADTLHKSKEGLLKAETAVVREMIDCQPYVVVNVHAEPLKLDGYAKSVHVPLGSAAKGGLPKYPTIQALVPILNEYCLLTNDAAIVIFGNDENVQITAAFCLIASRTISRVSEFMSDSLPNRFDRLPVTYHLFLEQTKHVCKYHARRQQLQSGAILNQIILEPGTLLIDGDLYVAIQQGINQLKVVEFSANSCRNRQGQLVFNMESTETVDDVVIFLGKKSDVKHPILASKFNTQLLHSEDSSIIFTSSEMDVSKMIASAMPVQDLRMIVNFATRRMPTLNTFQFDRYKLLCVRNDRELDGYQRSYGDVDSEDESPILRSARSKSGTKAAETSSSQGNFFDSLQFEDRQEPHHFREQRDSTLLDHHDDVTHHTADLLDGFTIGGTEKLSPANETPILSAPTPASSDYDSMTSSQNRRNPSPATAIDDLLGLGTETSAPAPAPSTHFNNSSSGANLVDFDLGAPIKPTSSASNLSTASPATSSWSNTDLLGGFSPMKPQTTSTPPNTRNPSASNSKPVSQVNSQADFEAFLSNYPEQRQAAPQNTQNVSQKTQQTRPQNTYKPAFGDAATGSAKVSMDAFSDLLNQGGFKPTQRENQKQSIGNMLKVEQSKNLTPEEIQIRDWTQGKERNIRALLGSLHNVLWEGADRWNQPSMGDLLTPDQIKKHYRKACLVVHPDKLTGSPHLSLAKMAFTELNDAYSKYQNDPAAM
Protein: General transcription factor IIi isoform D (X5D2J9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAQVAMSTLPVEDEESSESRMVVTFLMSALESMCKELAKSKAEVACIAVYETDVFVVGTERGRAFVNTRKDFQKDFVKYCVEEEEKAAEMHKMKSTTQANRMSVDAVEIETLRKTVEDYFCFCYGKALGKSTVVPVPYEKMLRDQSAVVVQGLPEGVAFKHPENYDLATLKWILENKAGISFIIKRPFLEPKKHVGGRVMVTDADRSILSPGGSCGPIKVKTEPTEDSGISLEMAAVTVKEESEDPDYYQYNIQGSHHSSEGNEGTEMEVPAEDDDYSPPSKRPKANELPQPPVPEPANAGKRKVREFNFEKWNARITDLRKQVEELFERKYAQAIKAKGPVTIPYPLFQSHVEDLYVEGLPEGIPFRRPSTYGIPRLERILLAKERIRFVIKKHELLNSTREDLQLDKPASGVKEEWYARITKLRKMVDQLFCKKFAEALGSTEAKAVPYQKFEAHPNDLYVEGLPENIPFRSPSWYGIPRLEKIIQVGNRIKFVIKRPELLTHSTTEVTQPRTNTPVKEDWNVRITKLRKQVEEIFNLKFAQALGLTEAVKVPYPVFESNPEFLYVEGLPEGIPFRSPTWFGIPRLERIVRGSNKIKFVVKKPELVISYLPPGMASKINTKALQSPKRPRSPGSNSKVPEIEVTVEGPNNNNPQTSAVRTPTQTNGSNVPFKPRGREFSFEAWNAKITDLKQKVENLFNEKCGEALGLKQAVKVPFALFESFPEDFYVEGLPEGVPFRRPSTFGIPRLEKILRNKAKIKFIIKKPEMFETAIKESTSSKSPPRKINSSPNVNTTASGVEDLNIIQVTIPDDDNERLSKVEKARQLREQVNDLFSRKFGEAIGMGFPVKVPYRKITINPGCVVVDGMPPGVSFKAPSYLEISSMRRILDSAEFIKFTVIRPFPGLVINNQLVDQSESEGPVIQESAEPSQLEVPATEEIKETDGSSQIKQEPDPTW
Protein: Small nuclear ribonucleoprotein E (snRNP-E) (Sm protein E) (Sm-E) (SmE) (Q12330)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-mRNA splicing. Binds and is required for the stability of snRNA U1, U2, U4 and U5 which contain a highly conserved structural motif called the Sm binding site. Involved in cap modification.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11027265}. Nucleus {ECO:0000269|PubMed:11027265}.
Interaction partners:
- Pre-mRNA-splicing factor RSE1
- Small nuclear ribonucleoprotein-associated protein B
- LSM complex subunit LSM6
- Pre-mRNA-splicing factor PRP9
- U2 small nuclear ribonucleoprotein B''
- Pre-mRNA-splicing helicase BRR2
- Small nuclear ribonucleoprotein F
- Nuclear cap-binding protein subunit 2
- Pre-mRNA-processing protein PRP40
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
Sequence:
MSNKVKTKAMVPPINCIFNFLQQQTPVTIWLFEQIGIRIKGKIVGFDEFMNVVIDEAVEIPVNSADGKEDVEKGTPLGKILLKGDNITLITSAD
Protein: Leucine-rich repeat-containing G-protein coupled receptor 6 (Q9HBX8)
Organism: Homo sapiens (Human)
Function: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and acts as a marker of multipotent stem cells in the epidermis. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. In contrast to classical G-protein coupled receptors, does not activate heterotrimeric G-proteins to transduce the signal. May act as a tumor suppressor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22615920}; Multi-pass membrane protein {ECO:0000269|PubMed:22615920}.
Interaction partners:
- R-spondin-1
- R-spondin-4
- R-spondin-2
- R-spondin-3
- Leucine-rich repeat-containing G-protein coupled receptor 4
- Leucine-rich repeat-containing G-protein coupled receptor 5
- E3 ubiquitin-protein ligase ZNRF3
- E3 ubiquitin-protein ligase RNF43
- Prorelaxin H1
- Prorelaxin H2
Sequence:
MPSPPGLRALWLCAALCASRRAGGAPQPGPGPTACPAPCHCQEDGIMLSADCSELGLSAVPGDLDPLTAYLDLSMNNLTELQPGLFHHLRFLEELRLSGNHLSHIPGQAFSGLYSLKILMLQNNQLGGIPAEALWELPSLQSLRLDANLISLVPERSFEGLSSLRHLWLDDNALTEIPVRALNNLPALQAMTLALNRISHIPDYAFQNLTSLVVLHLHNNRIQHLGTHSFEGLHNLETLDLNYNKLQEFPVAIRTLGRLQELGFHNNNIKAIPEKAFMGNPLLQTIHFYDNPIQFVGRSAFQYLPKLHTLSLNGAMDIQEFPDLKGTTSLEILTLTRAGIRLLPSGMCQQLPRLRVLELSHNQIEELPSLHRCQKLEEIGLQHNRIWEIGADTFSQLSSLQALDLSWNAIRSIHPEAFSTLHSLVKLDLTDNQLTTLPLAGLGGLMHLKLKGNLALSQAFSKDSFPKLRILEVPYAYQCCPYGMCASFFKASGQWEAEDLHLDDEESSKRPLGLLARQAENHYDQDLDELQLEMEDSKPHPSVQCSPTPGPFKPCEYLFESWGIRLAVWAIVLLSVLCNGLVLLTVFAGGPVPLPPVKFVVGAIAGANTLTGISCGLLASVDALTFGQFSEYGARWETGLGCRATGFLAVLGSEASVLLLTLAAVQCSVSVSCVRAYGKSPSLGSVRAGVLGCLALAGLAAALPLASVGEYGASPLCLPYAPPEGQPAALGFTVALVMMNSFCFLVVAGAYIKLYCDLPRGDFEAVWDCAMVRHVAWLIFADGLLYCPVAFLSFASMLGLFPVTPEAVKSVLLVVLPLPACLNPLLYLLFNPHFRDDLRRLRPRAGDSGPLAYAAAGELEKSSCDSTQALVAFSDVDLILEASEAGRPPGLETYGFPSVTLISCQQPGAPRLEGSHCVEPEGNHFGNPQPSMDGELLLRAEGSTPAGGGLSGGGGFQPSGLAFASHV
Protein: Rab proteins geranylgeranyltransferase component A 1 (Choroideremia protein) (Rab escort protein 1) (REP-1) (TCD protein) (P24386)
Organism: Homo sapiens (Human)
Function: Substrate-binding subunit of the Rab geranylgeranyltransferase (GGTase) complex. Binds unprenylated Rab proteins and presents the substrate peptide to the catalytic component B composed of RABGGTA and RABGGTB, and remains bound to it after the geranylgeranyl transfer reaction. The component A is thought to be regenerated by transferring its prenylated Rab back to the donor membrane. Besides, a pre-formed complex consisting of CHM and the Rab GGTase dimer (RGGT or component B) can bind to and prenylate Rab proteins; this alternative pathway is proposed to be the predominant pathway for Rab protein geranylgeranylation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:7957092}.
Interaction partners:
- Geranylgeranyl transferase type-2 subunit alpha
- Ras-related protein Rab-1A
- Ras-related protein Rab-7a
- Ras-related protein Rab-27A
- Ras-related protein Rab-3A
- Geranylgeranyl transferase type-2 subunit beta
- Ras-related protein Rab-1B
- Ras-related protein Rab-5A
- Ras-related protein Rab-5C
- Ras-related protein Rab-8A
Sequence:
MADTLPSEFDVIVIGTGLPESIIAAACSRSGRRVLHVDSRSYYGGNWASFSFSGLLSWLKEYQENSDIVSDSPVWQDQILENEEAIALSRKDKTIQHVEVFCYASQDLHEDVEEAGALQKNHALVTSANSTEAADSAFLPTEDESLSTMSCEMLTEQTPSSDPENALEVNGAEVTGEKENHCDDKTCVPSTSAEDMSENVPIAEDTTEQPKKNRITYSQIIKEGRRFNIDLVSKLLYSRGLLIDLLIKSNVSRYAEFKNITRILAFREGRVEQVPCSRADVFNSKQLTMVEKRMLMKFLTFCMEYEKYPDEYKGYEEITFYEYLKTQKLTPNLQYIVMHSIAMTSETASSTIDGLKATKNFLHCLGRYGNTPFLFPLYGQGELPQCFCRMCAVFGGIYCLRHSVQCLVVDKESRKCKAIIDQFGQRIISEHFLVEDSYFPENMCSRVQYRQISRAVLITDRSVLKTDSDQQISILTVPAEEPGTFAVRVIELCSSTMTCMKGTYLVHLTCTSSKTAREDLESVVQKLFVPYTEMEIENEQVEKPRILWALYFNMRDSSDISRSCYNDLPSNVYVCSGPDCGLGNDNAVKQAETLFQEICPNEDFCPPPPNPEDIILDGDSLQPEASESSAIPEANSETFKESTNLGNLEESSE
Protein: Defensin (Q86LE4)
Organism: Rhipicephalus microplus (Cattle tick) (Boophilus microplus)
Function: Antibacterial peptide mostly active against Gram-positive bacteria.
Subcellular location: Secreted {ECO:0000269|PubMed:14642886}.
Interaction partners:
Sequence:
MRGIYICLVFVLVCGLVSGLADVPAESEMAHLRVRRGFGCPFNQGACHRHCRSIRRRGGYCAGLIKQTCTCYRN
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9VHH2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000256|ARBA:ARBA00004419}.
Interaction partners:
- UV radiation resistance-associated gene protein
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Beclin-1-like protein
- Autophagy-related 14
- Autophagy-related 1, isoform B
- phosphatidylinositol 3-kinase
- Autophagy protein 12-like
- Autophagy-related protein 13 homolog
- Autophagy-related protein 101
- Autophagy protein 5
Sequence:
MGNQLVGIAPSQIYAVEHYFSGQFGSEIAFSSNMGSTRFFKVAKAKTDEGQIVVKVFVKHDPTLPLEDHKERLEGIKKTLSLANAVNCLPFQRVELIDKAAYIMREYVKHSLYDRVSTRPFLTVLEKKWITFQILCALNQCHKQKICHGDIKLENILITSWNWILLSDFASFKPTYLPEDNPADYTYFFDTSRRRTCYIAPERFVKTLASDDDGGNGNMSVIHTDSIIRLAPSYAGNTLLPAMDIFSAGCALLELWTEGTAPFELSQLLAYRRGERDLVEKHLAGIENERLRNLLASMIDIHSMNRKSAEDYLDQERGQLFPEYFYSFLQSYLQMFSSTPIMSPDDKIQCLHKDIGHCIKVLTQAQDLTPEEEEKEEKKDPTLCARLPPEHDGLILIITVVTSCIRGLKQSNTKIAALELLQKLSKYTTSETILDRILPYILHLAQKSPAKVQVQAIETLTACLGMVKDIPRSDANVFPEYILPSITDLASETSAVIVRVAFARNIAALAKSAVYFLEETQRNAPNDMPTPRYEAELNALHDIVRQAVLSLLTDSQPVVKQTLMESGICDLCAFFGKEKANDVILSHIMTFLNDEDKNLRGAFYDNIAGVAGYVGWQASDILVPLLQQGFTDREEFVIAKAIRAVTILIELGHIKKPAVTEIVQETACYLCHPNLWVRHEICGMIATTARNLSAIDVQCKIMPAIGAFLKAPLIQVEKPHILLDCVHPPVPRQIFDSVLRFQDIHHFIRALEARSRVRSQTRQGALPQYEEMGQTLRNLFRRLSSEGLTDLIEMQLLAMNPFLISMKHKALQDLDDTASGNGRIVVSRKQVACHEYPLADKASKMPLDNRSSEGPTLASPASDAAITPLGAGGLAGSPASGAVVLGVPTATVSAATSLGEYTMPERNCWLERSSECRKDLESLTAKIKSRYNVLAISQRCSYDKLVTPYPPGWRMTGTLVAHLHEHSESVIKLASLRPHGSLFASGSIDGTVRLWDCSKLNGNQGVNKSRQVYSANTPIYALAACDSGQSLAVGGKDGSMLMMRIDRNSAKMTLQQALNQNDHKDGPVVDMHAYDQATQSVIVYATLYGGIVAWDTRMQHSAWRLQNELRHGVITTICADPTGSWLATGTSGGKHICWDLRFRLPIAEIKHPADSWIRKVACHPTEPSYLISASQSNNEVSVWNIETGQRQTVLWASPVAALSSASPSDPATTCGILSGVVDGSPFILTGSSDQRIRYWDITNPKNSSLKVPAANDNLADVAFNYGARLIDGSQVIEEQIISMASTGDSQQLRSSTEENPRSGPDMPTASHHDAITDLLMCKDKGQIYIASASRNGVIKLWK
Protein: Serine acetyltransferase (SAT) (EC 2.3.1.30) (P0A9D4)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm.
Interaction partners:
- Cysteine synthase A
- Cysteine synthase B
- Cysteine--tRNA ligase
- Glycerol-3-phosphate dehydrogenase [NAD
- L-serine dehydratase 2
- L-serine dehydratase 1
- L-serine dehydratase TdcG
- Phosphoserine phosphatase
- Bifunctional aspartokinase/homoserine dehydrogenase 1
- Bifunctional aspartokinase/homoserine dehydrogenase 2
Sequence:
MSCEELEIVWNNIKAEARTLADCEPMLASFYHATLLKHENLGSALSYMLANKLSSPIMPAIAIREVVEEAYAADPEMIASAACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIFLQNQVSVTFQVDIHPAAKIGRGIMLDHATGIVVGETAVIENDVSILQSVTLGGTGKSGGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKPDSDKPSMDMDQHFNGINHTFEYGDGI
Protein: Small ribosomal subunit protein uS5 C-terminal domain-containing protein (Q38AX6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- 30S Ribosomal protein S17, putative
- Uncharacterized protein
- Uncharacterized protein
- Mitochondrial ribosomal protein S18
- Treble clef zinc finger domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MFRLTAASQKNLNSWYTKGTMRGGVPRIYYAWMRPGSFTRRRFEKMRNPFVDLETGTSLYFRDTRDSAEAIAHAADSKGIKGMDNAIDLYNEYRIVPDLYPEGFQWKHKLNTEYNQWRSNTWLTPDLIPKEHRGRFLCNFQLNIVAYDMRVVKFSPKDHRQWIYCVLYVGSGKGIAGWGRAVAPSTQEAKKEAIREAFSNIIAVDLEQEGPMYPVRVNADGVRVLLYPARRIVANFRVADILCAFGFQHAGCRINLKATNNPKSPTHTVEGVFEAVKALRSVSEIAASRGKVPHSLIYNIYPYLEEIRRRKGMMAMHPPGKDGLLMPDRVVDNRLPDHLKKGYYDDVYWKDFFAGSDEHLNEPRMGLRGDEMRRRLEEAQTSPAPTTAKDTRRRTLEDVLKRLGKTTRDLGSIPIVNPRVDVGLPTHIKRNYQLH