wanglab/gogpt-training-data huggingface dataset:
Protein: Guanine nucleotide-binding protein G(T) subunit gamma-T1 (Transducin gamma chain) (Q61012)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Rhodopsin
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Guanine nucleotide-binding protein G
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Guanine nucleotide-binding protein G
Sequence:
MPVINIEDLTEKDKLKMEVDQLKKEVTLERMMVSKCCEEVRDYIEERSGEDPLVKGIPEDKNPFKELKGGCVIS
Protein: U2 snRNP associated SURP domain containing (E7ET15)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADKTPGGSQKASSKTRSSDVHSSGSSDAHMDASGPSDSDMPSRTRPKSPRKHNYRNESARESLCDSPHQNLSRPLLENKLKAFSIGKMSTAKRTLSKKEQEELKKKEDEKAAAEIYEEFLAAFEGSDGNKVKTFVRGGVVNAAKEEHETDEKRGKIYKPSSRFADQKNPPNQSSNERPPSLLVIETKKPPLKKGEKEKKKSNLELFKEELKQIQEERDERHKTKGRLSRFEPPQSDSDGQRRSMDAPSRRNRSSVLDDYAPGSHDVGDPSTTNLYLGNINPQMNEEMLCQEFGRFGPLASVKIMWPRTDEERARERNCGFVAFMNRRDAERALKNLNGKMIMSFEMKLGWGKAVPIPPHPIYIPPSMMEHTLPPPPSGLPFNAQPRERLKNPNAPMLPPPKNKEDFEKTLSQAIVKVVIPTERNLLALIHRMIEFVVREGPMFEAMIMNREINNPMFRFLFENQTPAHVYYRWKLYSILQANSPTKWRTEDFRMFKNGSFWRPPPLNPYLHGMSEEQETEAFVEEPSKKGALKEEQRDKLEEILRGLTPRKNDIGDAMVFCLNNAEAAEEIVDCITESLSILKTPLPKKIARLYLVSDVLYNSSAKVANASYYRKFFETKLCQIFSDLNATYRTIQGHLQSENFKQRVMTCFRAWEDWAIYPEPFLIKLQNIFLGLVNIIEEKETEDVPDDLDGAPIEEELDGAPLEDVDGIPIDATPIDDLDGVPIKSLDDDLDGVPLDATEDSKKNEPIFKVAPSKWEAVDESELEAQAVTTSKWELFDQHEESEEEENQNQEEESEDEEDTQSSKSEEHHLYSNPIKEEMTESKFSKYSEMSEEKRAKLREIELKVMKFQDELESGKRPKKPGQSFQEQVEHYRDKLLQREKEKELERERERDKKDKEKLESRSKDKKEKDECTPTRKERKRRHSTSPSPSRSSSGRRVKSPSPKSERSERSERSHKESSRSRSSHKDSPRDVSKKAKRSPSGSRTPKRSRRSRSRSPKKSGKKSRSQSRSPHRSHKKSKKNKH
Protein: Holliday junction recognition protein (C9JWC4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLGTLRAMEGEDVEDDQLLQKLRASRRRFQRRMQRLIEKYNQPFEDTPVVQMATLTYETPQGLRIWGGRLIKERNEGEIQCAGNRAGRDVRVTPLPSLASPAVPAPGYCSRISRKSPGDPAKPASSPREWDPLHPSSTDMALVPRNDSLSLQETSSSSFLSSQPFEDDDICNVTISDLYAGMLHSMSRLLSTKPSSIISTKTFIMQNWNSRRRHRYKSRMNKTYCKGARRSQRSSKENFIPCSEPVKGTGALRDCKNVLDVSCRKTGLKLEKAFLEVNRPQIHKLDPSWKERKVTPSKYSSLIYFDSSATYNLDEENRFRTLKWLISPVKIVSRPTIRQGHGENRQREIEIRFDQLHREYCLSPRNQPRRMCLPDSWAMNMYRGGPASPGGLQGLETRRLSLPSSKAKAKSLSEAFENLGKRSLEAGRCLPKSDSSSSLPKTNPTHSATRPQQTSDLHVQGNSSGIFRKSVSPSKTLSVPDKEVPGHGRNRYDEIKEEFDKLHQKYCLKSPGQMTVPLCIGVSTDKASMEVRYQTEGFLGKLNPDPHFQGFQKLPSSPLGCRKSLLGSTA
Protein: Large ribosomal subunit protein mL44 (Q7K141)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
KTYSLLIFKIALKMSFLRSAVGLLARVKLLEGSPTVQTRRHIKRWVSPTLRELAHRQKKLGPQKPERRSGFVEWNQRSELFAFGKRLGESFELSELQRAFTEKSFAEREEDRRRQLGIEESDLQMPHNSDLVEKGQQIARAYVEAFLQHQLPKVPNEGLQAIASYLLSTETLAHVSTHLGTKDLIQSTEYPPSAESQAKSLHAVIGALASSSGIERAFIFVRDFICTQLNQKDLLEVWTPQEPIQLLEKICQERKLGEAEPRLLGDCGKNTVLAAYQVGIYANRQLLGKGFGEDVKTATETAALDALQSIFDTRDNRRPFDFAIQLEPKTVRLG
Protein: Estrogen related receptor beta (A0A2R8Y491)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002527}.
Interaction partners:
Sequence:
MDVSELCIPDPLGYHNQLLNRMSSDDRHLGSSCGSFIKTEPSSPSSGIDALSHHSPSGSSDASGGFGLALGTHANGLDSPPMFAGAGLGGTPCRKSYEDCASGIMEDSAIKCEYMLNAIPKRLCLVCGDIASGYHYGVASCEACKAFFKRTIQGNIEYSCPATNECEITKRRRKSCQACRFMKCLKVGMLKEGVRLDRVRGGRQKYKRRLDSESSPYLSLQISPPAKKPLTKIVSYLLVAEPDKLYAMPPPGMPEGDIKALTTLCDLADRELVVIIGWAKHIPGFSSLSLGDQMSLLQSAWMEILILGIVYRSLPYDDKLVYAEDYIMDEEHSRLAGLLELYRAILQLVRRYKKLKVEKEEFVTLKALALANSDSMYIEDLEAVQKLQDLLHEALQDYELSQRHEEPWRTGKLLLTLPLLRQTAAKAVQHFYSVKLQGKVPMHKLFLEMLEAKV
Protein: ER membrane protein complex subunit 2 (P47133)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the endoplasmic reticulum membrane protein complex (EMC) that enables the energy-independent insertion into endoplasmic reticulum membranes of newly synthesized membrane proteins. Preferentially accommodates proteins with transmembrane domains that are weakly hydrophobic or contain destabilizing features such as charged and aromatic residues. Involved in the cotranslational insertion of multi-pass membrane proteins in which stop-transfer membrane-anchor sequences become ER membrane spanning helices. It is also required for the post-translational insertion of tail-anchored/TA proteins in endoplasmic reticulum membranes. By mediating the proper cotranslational insertion of N-terminal transmembrane domains in an N-exo topology, with translocated N-terminus in the lumen of the ER, controls the topology of multi-pass membrane proteins (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q15006}; Cytoplasmic side {ECO:0000250|UniProtKB:Q15006}.
Interaction partners:
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 5
- ER membrane protein complex subunit 6
- Endoplasmic reticulum membrane protein complex subunit 10
- Protein SOP4
Sequence:
MLKDLVREKLLTIMNTKAYTQFNPEQLLQLENEMKIYMKSGDSALTEGNYFFLMEMLFYVLVYRNQDVDAQVVYNTLRDRLGENSYKMVIMKATLLQINGNDKGAIEYLENLLNDDLEYETDFVTYVSIAKKLIAIKTTSKNLSQESVLKEVVALTDKFPLDAELWWYASEIYFEMGQFEKACYCLEQVLCITPFNYACFGRLSETLYYEALRSKKQTKTELLEKALKNALRSVELSELYLKGWALVNIISRELGRNKQNDLIKLSASKLKEISAKSNNKDKITAELILNKI
Protein: Myosin-11 (Myosin heavy chain 11) (Myosin heavy chain, smooth muscle isoform) (SMMHC) (O08638)
Organism: Mus musculus (Mouse)
Function: Muscle contraction.
Subcellular location: Melanosome {ECO:0000250}. Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Actin, aortic smooth muscle
- Actin, gamma-enteric smooth muscle
- Myosin regulatory light polypeptide 9
- Myosin light polypeptide 6
- Myosin light chain 6B
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin light chain kinase, smooth muscle
- Myosin regulatory light chain 12B
- Actin, cytoplasmic 1
- Myosin, light chain 12A, regulatory, non-sarcomeric
Sequence:
MAQKGQLSDDEKFLFVDKNFMNSPMAQADWVAKKLVWVPSEKQGFEAASIKEEKGDEVVVELVENGKKVTVGKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVVNPYKYLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTQKVIQYLAVVASSHKGKKDSSITGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQARDERTFHIFYYLLAGAKEKMKSDLLLESFNSYTFLSNGFVPIPAAQDDEMFQETLEAMSIMGFNEEEQLAILKVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLVGINVTDFTRAILTPRIKVGRDVVQKAQTKEQADFAIEALAKATYERLFRWILSRVNKALDKTHRQGASFLGILDIAGFEIFEVNSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPSIELIERPNNPPGVLALLDEECWFPKATDKSFVEKLCSEQGNHPKFQKPKQLKDKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLGKLMATLRNTTANFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKITDVIMAFQAMCRGYLARKAFTKRQQQLTAMKVIQRNCAAYLKLRNWQWWRLFTKVKPLLQVTRQEEEMQAKEEEMQKITERQQKAETELKELEQKHTQLAEEKTLLQEQLQAETELYAESEEMRVRLAAKKQELEEILHEMEARLEEEEDRRQQLQAERKKMAQQMLDLEEQLEEEEAARQKLQLEKVTAEAKIKKLEDDILVMDDQNSKLSKERKLLEERVSDLTTNLAEEEEKAKNLTKLKSKHESMISELEVRLKKEEKSRQELEKLKRKLEGDASDFHEQIADLQAQIAELKMQLAKKEEELQAALARLDEEIAQKNNALKKIRELEGHISDLQEDLDSERAARNKAEKQKRDLGEELEALKTELEDTLDSTATQQELRAKREQEVTVLKKALDEETRSHEAQVQEMRQKHTQAVEELTEQLEQFKRAKANLDKSKQTLEKENADLAGELRVLGQAKQEVEHKKKKLEVQLQDLQSKCSDGERARAELSDKVHKLQNEVESVTGMLNEAEGKAIKLAKDVASLGSQLQDTQELLQEETRQKLNVSTKLRQLEDERNSLQDQLDEEMEAKQNLERHVSTLNIQLSDSKKKLQDFASTIEVMEEGKKRLQKEMEGLSQQYEEKAAAYDKLEKTKNRLQQELDDLVVDLDNQRQLVSNLEKKQKKFDQLLAEEKNISSKYADERDRAEAEAREKETKALSLARALEEALEAKEELERTNKMLKAEMEDLVSSKDDVGKNVHELEKSKRALETQMEEMKTQLEESEDDVQATEDAKLRLEVNMQALKGQFERDLQARDEQNEEKRRQLQRQLHEYETELEDERKQRALAAAAKKKLEGDLKDLELQADSAIKGREEAIKQLRKLQAQMKDFQRELDDARASRDEIFATSKENEKKAKSLEADLMQLQEDLAAAERARKQADLEKEELAEELASSLSGRNTLQDEKRRLEARIAQLEEELEEEQGNMEAMSDRVRKATLQAEQLSNELATERSTAQKNESARQQLERQNKELRSKLQEVEGAVKAKLKSTVAALEAKIAQLEEQVEQEAREKQAATKSLKQKDKKLKEVLLQVEDERKMAEQYKEQAEKGNTKVKQLKRQLEEAEEESQCINANRRKLQRELDEATESNEAMGREVNALKSKLRRGNEASFVPSRRAGGRRVIENTDGSEEEMDARDSDFNGTKASE
Protein: Blue light-responsive regulator BluF (Diguanylate phosphodiesterase) (Putative signal transduction protein) (Uncharacterized protein ycgF) (Q2LD83)
Organism: Escherichia coli
Interaction partners:
Sequence:
MLTTLIYRSHIRGDEPVKKIEEMVSIANRRNMRSDVTGILLFNGSHFFQLLEGPEEQVQMIYRAICQDPRHYNIVELLCDYAPARRFGKAGMELFDLRLHERDDVLQAVFDKGTSKFQLTYDDRALQFFRTFVLATEQSTYFEIPAEDSWLFIADGSDKELDSCTLSSNINDHFAFHPIVDPLSRRIIAFEAIVQKNEDSPSAIAVGQRKDEEIYTADLKSKALAFAMAHALKLGDKMISINLLPMTLVNKPDAVSFLLDEIKANALVPEQIIVEFTESEVISRFDEFAEAVKSLKAAGISVAIDHFGAGFAGLLLLSRFQPDRIKISQELITNVHKSGPRQAIIQAIMKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFSKAKLNGIPSVAWPEKK
Protein: GM10337p (Q86NX0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
PFKDKQEDEETENDVDIMGFEDLEDPQPAAVPQHPNPQPPMEPQDQQPAQPVIDLPQPVPEAAAPRRESPERDFEHERAINPFLLPIKRPRATAPLALPHYMHELADGRARVHEYNVASGSGASGSSRNIVNIIPVEVMLKIFAYLDDMSLWMASEVCKQWHDIVGKNTAQSMWKAYIKQRWPLFDSLADNPNWYRLYGALMSSCFCRTCLIEMGGRGQDAQEADPQLGDREPGNVMRNNFLRGEANLLNSYESEGISAIPLDRQNNYWQATILGPPGSPYEGGKFFLFIYFPERYPMTPPTVRFLTKILHPNVSRHGDVGIDIFQQHNWSLALNVAKVLLSVQSLLTDPYTEVCMEPELGYIYEHERERFEQLVRAWTWKYAMYELIAPR
Protein: Proteasome subunit beta type-6 (Multicatalytic endopeptidase complex subunit C5) (Proteasome component C5) (P23724)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Non-catalytic component of the proteasome which degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Proteasome maturation factor UMP1
- 26S proteasome regulatory subunit RPN5
- Proteasome subunit beta type-4
- 26S proteasome subunit RPT4
- Proteasome subunit alpha type-4
- 26S proteasome regulatory subunit RPN10
- Proteasome subunit alpha type-3
- Ubiquitin carboxyl-terminal hydrolase RPN11
- Peroxisomal targeting signal 2 receptor
- 26S proteasome regulatory subunit RPN12
Sequence:
MATIASEYSSEASNTPIEHQFNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDKKLSINSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKNQYEPGTNGKVKKPLKYLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYELKRD
Protein: Rifin (Q8IFK9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKIHYTNILLFPLKLNILVNTHKKPHTTARHIQTNRLLCECELYMSNYDNDPEMKSVMQQFHDRTKQRFQEYDEMLQEKRQICKDTCDKEIQKIILKDKIEKELNEKFSALHTDIQSDAIPTCICEKSVTDKFEKTCLKCSGIFATAVPELGLIGGTVVYDAAVKAATKAAIKKAIEEVGKIFFLADESTMQWTNMINAGNYSDKMSLVSILTSLNNGCQDGEAVAGPLFCTASNALTESGNPYVFTRTISEKAANAADAARKAASGKFAEMTSVGTIFSDPIVISAIVVISIAVILLIIYLILRYRRKIKMNKKLQYIKLLKE
Protein: Aspartic proteinase MKC7 (EC 3.4.23.41) (Yapsin-2) (P53379)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cleaves proteins C-terminally to the most C-terminal basic residue. Can process the alpha-mating factor precursor. Required for cell wall integrity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10446224, ECO:0000269|PubMed:7479877}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:10446224, ECO:0000269|PubMed:7479877}. Note=GPI-anchored plasma membrane protein (GPI-PMP).
Interaction partners:
- Aspartic proteinase 3
- Signaling mucin MSB2
- Kexin
Sequence:
MKLSVLTFVVDALLVCSSIVDAGVTDFPSLPSNEVYVKMNFQKKYGSSFENALDDTKGRTRLMTRDDDYELVELTNQNSFYSVELDIGTPPQKVTVLVDTGSSDLWVTGSDNPYCSTKKKDTTGSSFKQVNKDALASVVESVFTEISYDTTIVTSEATATFDSTASTSQLIDCATYGTFNTSKSSTFNSNNTEFSIAYGDTTFASGTWGHDQLSLNDLNITGLSFAVANETNSTVGVLGIGLPGLESTYSGVSLSSVQKSYTYNNFPMVLKNSGVIKSTAYSLFANDSDSKHGTILFGAVDHGKYAGDLYTIPIINTLQHRGYKDPIQFQVTLQGLGTSKGDKEDNLTTLTTTKIPVLLDSGTTISYMPTELVKMLADQVGATYSSAYGYYIMDCIKEMEEESSIIFDFGGFYLSNWLSDFQLVTDSRSNICILGIAPQSDPTIILGDNFLANTYVVYDLDNMEISMAQANFSDDGEYIEIIESAVPSALKAPGYSSTWSTYESIVSGGNMFSTAANSSISYFASTSHSATSSSSSKGQKTQTSTTALSISKSTSSTSSTGMLSPTSSSSTRKENGGHNLNPPFFARFITAIFHHI
Protein: Vesicle-associated membrane protein 5 (VAMP-5) (Myobrevin) (Q9Z2J5)
Organism: Rattus norvegicus (Rat)
Function: May participate in trafficking events that are associated with myogenesis, such as myoblast fusion and/or GLUT4 trafficking.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Endomembrane system {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Associated with the plasma membrane as well as intracellular perinuclear and peripheral vesicular structures of myotubes. Associated with the trans-Golgi, but not with the cis-Golgi apparatus (By similarity). {ECO:0000250}.
Interaction partners:
- Vesicle-associated membrane protein 8
- Synaptobrevin homolog YKT6
- Syntaxin-8
- Synaptosomal-associated protein 23
- Vesicle-associated membrane protein 7
- Syntaxin-11
Sequence:
MAGKELERCQRQADQVTEIMLNNFDKVLERDGKLSELQQRSDQLLDMSSAFSKTTKTLAQQKRWENIRCRVYLGLAVAGGLLLILVVLLVIFLPSGEDSSKP
Protein: Esculentin-1SIa (F1T149)
Organism: Odorrana ishikawae (Ishikawa's frog) (Rana ishikawae)
Function: Has antimicrobial activity against Gram-negative bacterium E.coli ATCC 8739 (MIC=6.3 ug), against Gram positive bacteria S.aureus ATCC 6538 (MIC=3.1 ug), methicillin-resistant S.aureus ATCC 43300 (MIC=25 ug) and B.subtilis ATCC 6633 (MIC=25 ug). Has no activity against fungus C.albicans ATCC 90028.
Subcellular location: Secreted {ECO:0000305|PubMed:21193000}.
Interaction partners:
Sequence:
MFTLKKPLLLIVLLGIISLSLCEQERAADEDEGSEIKRGIFSKFAGKGIKNLLVKGVKNIGKEVGMDVIRTGIDIAGCKIKGEC
Protein: Uncharacterized protein (Q388A3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MTYKEVALSSQLNGVFHCAAVVTLRTAPADTLHHPVSSSGTHKQVPDGGVKCEELEGDNRRSRSPSITVFTVLNPKAASSSLQVRQLPQQPPEEMRCTLWVGASSGDIEVRSAVQPDRVLRFVPKKSRAVVTSLIQIGSSRVVAGLSDGYIRVFDAVTLCEYQQTRAHTSAVRCLMAVATPIVQGVQPECEFTPAPVFLTASSDRTIAKWDAVSLQCLCRLKGHTCSVSALVSTLNGVFVFSGADDGSLHMWSMVDNTQVVGRPTTVAKSAGKKKRTGKDLLGPSPHRQKSQLPKCSLEEPQVKQTSQASGRGASQARPGKCRTSRSASVGIMKVRSLLRSPSIGSPQRHRVDGGGTGRSRSIAAMQRHGLLPKINWGKDLALPTTAARAPNTATRDSDSDRQFDGSSDDENLLTAEPVIPVDGQGSAVFCRSGRNVGDGVGAPREGRKGRGKLKKKSAQQVQVSRFADVLAKLQGPVSDSAMGCRLAAVHSEPVASGIEGGTLLWPLKCEHAKRITHLAIVWDRFLLSGSSDGEVKVLALPSGRSIRTVHRGYTPVTGMTVDNARCLLWIATADGCFHVHNMLTPDLQQLHAWRDLSTPRPLLVPMTTNRLLCQLYLLAAPGSKKKLFDSRSAGNKIKPKINLESRNINCKRKKTGQVAPTDQGAQSGLVEPEEAVQAPPNATLACIQVDDGDDEALADIGSLRKLDVAHMKARCTIAKMESKEEVFRRVLRRPVTDDGMELRECLLKEQTRVVNALYGTRFHFSLRDSFRRWMAWSTRRVRRYQCMRRVRFLAATNQERLLGCYFRKWRRHRVSQRLVEQDVQIRSLESRSFSTTVERCAKPCGVALGGRACVALASTQRRNLLHRYYRYWLHHVVGLRQALSRSVAFNRLFLSFDSKVCDSAFVFRRLATTNQCAQRQKRALQLLLLRMEAHYRQLQHRCMRRWFSFLQDQRESRQTYNLVETLTSVLVNGEALRMSAYFKWYRFALFETKLHRFDEERATLQREWIVVQNALESKETVANLKQEEVQLEVEIAQLAYERDEIDSQNVSLRADIVHIQMSKSLDCILAGYVDAEDKLKTVPRLLPEPPFHSRRLWTSSGERFSPVNEDDSSAEAALLSQLSAVLRALKATVLRCRRHCSLITTSHDRVLRIPIWDKPVETREWSSGVSHSSVGGDSSALHGTSGASLSDTRYSSERRRSIASSTHTVAYLADEFGRTVGRLRLLIEEVARQAGADLEESTDQTLSAFLKHKNSIGMGSESIRVINAECPSVEWLNFVPSTKRAEILPLLADLVTMYDSFKAHSDTEIETGGKTLSTRGALTSAPLPLRSLCRTQAAMWLVRHSAVILELMAPGTWEKHLNVWFLADSMKDSVALFNQNLDVGLATPKRTKKKESSAELKDTSSILSDISFQPSKAVVKEKRKKIPKTVASGKGTPRKASSVSSPITSQPSVESTPVRLWASPKAAIVQPQRKPAVSCSNLHSPVSRSVCGPLDGEFVVHAAQRSNSVPLRHHSAISSSRSFASAPLTRPYLGFRVAVGRDSSGCTTLSIQEVTQTYTGSNGGADLMGPAFAAGLRVGDQLVRFAGYTVTELAAFNTVVARHVRPSASIPVVFSRDGVVMSATIVVGEKRRE
Protein: Neuropeptide-Like Protein (Q18915)
Organism: Caenorhabditis elegans
Interaction partners:
- Neuropeptide-Like Protein
- Neuropeptide-Like Protein
- Neuropeptide-like protein nlp-8
- FMRFamide-like neuropeptides 13
- Histidine-rich glycoprotein-like
- Neuropeptide-Like Protein
- Neuropeptide-Like Protein
Sequence:
MLHLIVLLVALSSAVTAGRPRRALDGLDGSGFGFDKRALNSLDGAGFGFEKRALNSLDGQGFGFEKRALDGLDGAGFGFDKRALNSLDGAGFGFEKRALDGLDGSGFGFDKRALNSLDGAGFGFEKRALNSLDGAGFGFEKRALDGLDGAGFGFDKRALNSLDGAGFGFEKRALDGLDGAGFGFDKRALNSLDGNGFGFDKRTFKHSSNKLRSVFRNLKGFKQH
Protein: Dehydrogenase/reductase SDR family member 4 (EC 1.1.1.184) (NADPH-dependent carbonyl reductase) (CR) (NADPH-dependent retinol dehydrogenase/reductase) (NRDR) (humNRDR) (Peroxisomal short-chain alcohol dehydrogenase) (PSCD) (SCAD-SRL) (Short chain dehydrogenase/reductase family 25C member 2) (Protein SDR25C2) (Short-chain dehydrogenase/reductase family member 4) (Q9BTZ2)
Organism: Homo sapiens (Human)
Function: NADPH-dependent oxidoreductase which catalyzes the reduction of a variety of compounds bearing carbonyl groups including ketosteroids, alpha-dicarbonyl compounds, aldehydes, aromatic ketones and quinones. Reduces 3-ketosteroids and benzil into 3beta-hydroxysteroids and R-benzoin, respectively, in contrast to the stereoselectivity of non-primate DHRS4s which produce 3alpha-hydroxysteroids and S-benzoin. Diplays low activity toward all-trans-retinal and no activity toward 9-cis-retinal as compared to non-primate mammals. In the reverse reaction, catalyze the NAD-dependent oxidation of 3beta-hydroxysteroids and alcohol, but with much lower efficiency. Involved in the metabolism of 3beta-hydroxysteroids, isatin and xenobiotic carbonyl compounds.
Subcellular location: [Isoform 1]: Peroxisome {ECO:0000269|PubMed:10333503, ECO:0000269|PubMed:17230527}. Note=Isoform 4 is not peroxisomal. {ECO:0000269|PubMed:17230527}.; SUBCELLULAR LOCATION: [Isoform 7]: Nucleus {ECO:0000269|PubMed:22227495}.
Interaction partners:
- Aldehyde dehydrogenase 1A1
- Dehydrogenase/reductase SDR family member 9
- All-trans-retinol 13,14-reductase
- Retinaldehyde dehydrogenase 3
- Aldehyde oxidase
- Cytochrome P450 26A1
- Short-chain dehydrogenase/reductase 3
- Retinal dehydrogenase 2
- Beta,beta-carotene 15,15'-dioxygenase
- Lecithin retinol acyltransferase
Sequence:
MHKAGLLGLCARAWNSVRMASSGMTRRDPLANKVALVTASTDGIGFAIARRLAQDGAHVVVSSRKQQNVDQAVATLQGEGLSVTGTVCHVGKAEDRERLVATAVKLHGGIDILVSNAAVNPFFGSIMDVTEEVWDKTLDINVKAPALMTKAVVPEMEKRGGGSVVIVSSIAAFSPSPGFSPYNVSKTALLGLTKTLAIELAPRNIRVNCLAPGLIKTSFSRMLWMDKEKEESMKETLRIRRLGEPEDCAGIVSFLCSEDASYITGETVVVGGGTPSRL
Protein: Z-DNA binding protein kinase (Q5NE12)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAKMSAENEIEMRICDYLRRHGRSTVQDIFKELKLEKSTVNRHLYSLQASKQVFKTVEDNKRPVWDLVESMNDEQKAKPEQIKPEMTRDAIEEKHVKDLLKSGGLKASHIASKLGQQTQSTNKLLYGLMEKGEVRKCSKSHMWTLKNDQERNGSGSDRKLTSVSGMSQTFDVIEELGDGGYGFVCKVKHKIDDKIYAVKRVEFNSEAEPEVKALARLDHPNIVRYFTCWPDSDNWMSNQETNEKSNTTGSSTDTDDTNERSASDDDVADDEDDDDDDVSDDVTLGMESLTFTESTSAAKASGQCDPTNHRTYLFIQMEFCEGGTLTSWIGERNYRGKQRIALEIHRIFYEISSGVEYIHSNNLIHRDLKPDNILFNDGKVKIGDFGLVAAQKNPSGDPIERSKRKGTPTYMSPEQENLRNYDEKTDIFPLGLMWFEMLWKISSGMERAEIWTNLRNQKLPDQFCERYPAENKFIEKMLSVTPEDRPHVKDIRLNLETFFSLHQNSLSQKTI
Protein: Fanconi anemia group I protein (Protein FACI) (Q9NVI1)
Organism: Homo sapiens (Human)
Function: Plays an essential role in the repair of DNA double-strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting FANCD2 monoubiquitination by FANCL and participating in recruitment to DNA repair sites. Required for maintenance of chromosomal stability. Specifically binds branched DNA: binds both single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA). Participates in S phase and G2 phase checkpoint activation upon DNA damage.
Subcellular location: Nucleus {ECO:0000269|PubMed:17412408, ECO:0000269|PubMed:17460694, ECO:0000269|PubMed:19465922}. Cytoplasm {ECO:0000269|PubMed:18445686}. Note=Observed in spots localized in pairs on the sister chromatids of mitotic chromosome arms and not centromeres, one on each chromatids. These foci coincide with common fragile sites. They are frequently interlinked through BLM-associated ultra-fine DNA bridges.
Interaction partners:
- Fanconi anemia group A protein
- Fanconi anemia group D2 protein
- Fanconi anemia group G protein
- E3 ubiquitin-protein ligase FANCL
- Fanconi anemia group C protein
- Fanconi anemia group B protein
- Fanconi anemia group E protein
- WD repeat-containing protein 48
- Fanconi anemia group M protein
- Fanconi anemia group F protein
Sequence:
MDQKILSLAAEKTADKLQEFLQTLREGDLTNLLQNQAVKGKVAGALLRAIFKGSPCSEEAGTLRRRKIYTCCIQLVESGDLQKEIASEIIGLLMLEAHHFPGPLLVELANEFISAVREGSLVNGKSLELLPIILTALATKKENLAYGKGVLSGEECKKQLINTLCSGRWDQQYVIQLTSMFKDVPLTAEEVEFVVEKALSMFSKMNLQEIPPLVYQLLVLSSKGSRKSVLEGIIAFFSALDKQHNEEQSGDELLDVVTVPSGELRHVEGTIILHIVFAIKLDYELGRELVKHLKVGQQGDSNNNLSPFSIALLLSVTRIQRFQDQVLDLLKTSVVKSFKDLQLLQGSKFLQNLVPHRSYVSTMILEVVKNSVHSWDHVTQGLVELGFILMDSYGPKKVLDGKTIETSPSLSRMPNQHACKLGANILLETFKIHEMIRQEILEQVLNRVVTRASSPISHFLDLLSNIVMYAPLVLQSCSSKVTEAFDYLSFLPLQTVQRLLKAVQPLLKVSMSMRDCLILVLRKAMFANQLDARKSAVAGFLLLLKNFKVLGSLSSSQCSQSLSVSQVHVDVHSHYNSVANETFCLEIMDSLRRCLSQQADVRLMLYEGFYDVLRRNSQLANSVMQTLLSQLKQFYEPKPDLLPPLKLEACILTQGDKISLQEPLDYLLCCIQHCLAWYKNTVIPLQQGEEEEEEEEAFYEDLDDILESITNRMIKSELEDFELDKSADFSQSTSIGIKNNICAFLVMGVCEVLIEYNFSISSFSKNRFEDILSLFMCYKKLSDILNEKAGKAKTKMANKTSDSLLSMKFVSSLLTALFRDSIQSHQESLSVLRSSNEFMRYAVNVALQKVQQLKETGHVSGPDGQNPEKIFQNLCDITRVLLWRYTSIPTSVEESGKKEKGKSISLLCLEGLQKIFSAVQQFYQPKIQQFLRALDVTDKEGEEREDADVSVTQRTAFQIRQFQRSLLNLLSSQEEDFNSKEALLLVTVLTSLSKLLEPSSPQFVQMLSWTSKICKENSREDALFCKSLMNLLFSLHVSYKSPVILLRDLSQDIHGHLGDIDQDVEVEKTNHFAIVNLRTAAPTVCLLVLSQAEKVLEEVDWLITKLKGQVSQETLSEEASSQATLPNQPVEKAIIMQLGTLLTFFHELVQTALPSGSCVDTLLKDLCKMYTTLTALVRYYLQVCQSSGGIPKNMEKLVKLSGSHLTPLCYSFISYVQNKSKSLNYTGEKKEKPAAVATAMARVLRETKPIPNLIFAIEQYEKFLIHLSKKSKVNLMQHMKLSTSRDFKIKGNILDMVLREDGEDENEEGTASEHGGQNKEPAKKKRKK
Protein: ATP synthase subunit 4 (Q59ZE0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU368017}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU368017}.
Interaction partners:
- ATP synthase subunit d
- F1F0 ATP synthase subunit g
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit gamma
- ATP synthase subunit alpha
- ATP synthase subunit 5
- F1F0 ATP synthase subunit h
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit beta
- ATP synthase subunit a
Sequence:
MSMINRIALRSARPAMGMAFRPAPIGLRYLSAPADPKQKANSIIDALPGNNLLSKTGVLATSAAAAIYGISNGLFIIHDETILLVTFASFTALVAKFVAPLYTEWADGEIKKVNDILNQSRTNHIEAVNKRIETVSELKNVVATTEDLFALSKETAQFEADSFELKQKLAVSHEAKSVLDSWVRFEQQQRQLEQEQLAKEVIDKVDKEIANPKFQDKVLAESLNEIEKLFAKN
Protein: Integrin beta (L7RT22)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}.
Interaction partners:
Sequence:
MPRAPAPLYACLLGLCALLPRLAGLNICTSGSATSCEECLLIHPKCAWCSKEDFGSPRSITSRCDLRANLVKNGCGGEIESPASSFHVLRSLPLSSKGSGSAGWDVIQMTPQEIAVNLRPGDKTTFQLQVRQVEDYPVDLYYLMDLSLSMKDDLDNIRSLGTKLAEEMRKLTSNFRLGFGSFVDKDISPFSYTAPRYQTNPCIGYKLFPNCVPSFGFRHLLPLTDRVDSFNEEVRKQRVSRNRDAPEGGFDAVLQAAVCKEKIGWRKDALHLLVFTTDDVPHIALDGKLGGLVQPHDGQCHLNEANEYTASNQMDYPSLALLGEKLAENNINLIFAVTKNHYMLYKNFTALIPGTTVEILDGDSKNIIQLIINAYNSIRSKVELSVWDQPEDLNLFFTATCQDGVSYPGQRKCEGLKIGDTASFEVSLEARSCPSRHTEHVFALRPVGFRDSLEVGVTYNCTCGCSVGLEPNSARCNGSGTYVCGLCECSPGYLGTRCECQDGENQSVYQNLCREAEGKPLCSGRGDCSCNQCSCFESEFGKIYGPFCECDNFSCARNKGVLCSGHGECHCGECKCHAGYIGDNCNCSTDISTCRGRDGQICSERGHCLCGQCQCTEPGAFGEMCEKCPTCPDACSTKRDCVECLLLHSGKPDNQTCHSLCRDEVITWVDTIVKDDQEAVLCFYKTAKDCVMMFTYVELPSGKSNLTVLREPECGNTPNAMTILLAVVGSILLVGLALLAIWKLLVTIHDRREFAKFQSERSRARYEMASNPLYRKPISTHTVDFTFNKFNKSYNGTVD