wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription initiation factor TFIID subunit 1 (TBP-associated transcription factor 1) (G5EGM3)
Organism: Caenorhabditis elegans
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs), including taf-1 (By similarity). May regulate RNA polymerase II activity and thereby may control transcription initiation by RNA polymerase II. Required for early embryonic development. Essential for embryonic transcription of several genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:14726532}.
Interaction partners:
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 10
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 13
- PHD-type domain-containing protein
- Transcription initiation factor TFIID subunit 8
Sequence:
MNNTHHHTNGYRTEKPKNEEDLEDPYANLSDFYKNHPAARNEACSSASNGGSKSVKMEPKVEKNEEFEEYIGDPVRLEDMEPFARPSLRDDAPLSSILHPDLDGIDPRIFFKDFNPNKTLRFSRLFAQNIKHTSRAEIWWASRTFSKHQRKKEPEEPLADDVIVGAKKLKLNIIEKVPRVMLADDEEERMRRPILTDAEEMAKKNEEGTVVQPWRTGPAKIWYDMMNLPMTSQAVNYGFKLKKSPQKVSIRSGKPLNYRTPDDLPSTSSGPAPNSAPFLDKVEVIDKSCEASTSEDILLPYQVIEWENDVILDGEEVKDQLLEEFSNGRGCGWIPTQYTRTYEHFVYAANNNAFEQMFDGKSAPINLTGPDSAILPTPGHSIFPSAPCDLDILPWETNIIWDADAMPSTLEPIDFLVDFQDDPLIYGMPEDRRHDEGPDHHHHHHHHRKDGQYTKKSKMILGQVQQRQKQEEDEQMESTMAQFTDNDPFNLSNDDYYVPKATSKTLSNNSLLIQHSTPATNIATHFFPTHPSAFRLRYWHRTPFTRRIVRHWQPMRFQPIQTPVKHQQRVAAMREAMRQAQGGGEVFYMRDVQDLSGKDETLVMIEYSEEHPVILSQPGMASKMKNYFKRRQANDSEPTFTFGELAFSHQIPFLGQLQPGQSLQSIENMLYRAPIYLHKRQNTDFLLIRSMNQWYIRPLPSIFVAGQQCPLYEVPSPNSKRATVFVRDFLFAFIYRLFWASDSSPRRLKMDDVRNAFPHYAESNIRKRLKMCSTFVRQGSETYWSLKPDFRLPSKEEVLSMVTPEMCCAQYSMMAAEQRLKDAGYGEKYFFTPENDEGSEDEVTIEDEIKCAPWNTTRAFLASQREKCLLDQTGIADPTGCGQGFSYVRVSQKPHKDENATPVPKKLVTGTNADLRKLPLKEAKQICRGYGVKEEEISALTRWEIIDVIRTLSTQAAKATKDGEIIAVSGMARFARGNTRFSSADMQEKYRKHCQRIFDQQNQTLANTDPISTDDDSTDADSDNEELASRLESMLEANKGKKNISMSEKAKIDFETEEKEREDLKRMIHGTTNQVEKGEKKEEGEVTAEEKKSASQFGEDVAMSASKISGITANQQLKIYRTCKGPDGKDVTRIEIVTRPQLIEAYTRIRMTRDDTFIQVYAQMDEQYKEEKRKKKRRLQDQIRRMKKNEEKAAHKVQKMTEKKVKPIKPPNPNLQKMRCSACHAYGHMKTNRNCPLYGKDPLTPLKEEDEGSTIMTSVSSASLVAPDAVQVDGTKVKFNLNFAEIRKEQNREEKLKRKLAKMAEAAVRERQMAHLMEYGGGASSSGGAGGGGSGIGGSTGGGITDNDDDDRFSQISGTSSFLNGPPGAIRGGNRNSSVSGSKRRSSMMPEEDYLQGPLKVAHRARADPKVVMSSMLTDIVNELKMISGSDAFVTPVNSKKVVDYYNIIKNPISLQEIKKKISEQSYLLRKDFLDDIKLMFDNSRMYNGDNNILTLTAQQMLQLAGKRMIEREQKFIGLEKQINPLLDTNDLIGFSYLLGEIVQKMKNIPKSALFHTRVDPKKIPAYYLKISDPMDLSIMEQKSKSQEYKSIDEFLKDAEKIYTNSVVFNGAESVYSLKAKEMFEMAEMLVKDQMDTLGELERNINPSAINDAAAAQRGLAMDSDDHMDEMEDHPTEEEEEDDDDEIMDDDMDIDATGYSYDHDDNVAVGQIFNDLAMSDSDEDERAEDVKRPANGDDNLLDSF
Protein: NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 8, mitochondrial (Complex I-ASHI) (CI-ASHI) (NADH-ubiquinone oxidoreductase ASHI subunit) (Q9D6J5)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 beta subcomplex subunit 3
Sequence:
MAAARAAALGVRWLQRTTRGVVPLEARRAFHMTKDMLPGSYPRTPEERAAAAKKYNMRVEDYEPYPDDGMGYGDYPMLPNRSQHERDPWYQWDHSELRMNWGEPIHWDLDMYIRNRVDTSPTPVSWDVMCKHLFGFVAFMVFMFWVGHVFPSYQPVGPKQYPYNNLYLERGGDPTKEPEPVVHYDI
Protein: Holin-like protein TcdE (P16153)
Organism: Clostridioides difficile (Peptoclostridium difficile)
Function: Holin-like protein required for secretion of toxins A and B (TcdA and TcdB). Facilitates the release of toxins to the extracellular environment without causing the bacterial cell lysis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22685398}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MHSSSPFYISNGNKIFFYINLGGVMNMTISFLSEHIFIKLVILTISFDTLLGCLSAIKSRKFNSSFGIDGGIRKVAMIACIFFLSVVDILTKFNFLFMLPQDCINFLRLKHLGISEFFSILFILYESVSILKNMCLCGLPVPKRLKEKIAILLDAMTDEMNAKDEK
Protein: Sorting nexin-7 (Q9CY18)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of endocytosis and in several stages of intracellular trafficking. Together with SNX4, involved in autophagosome assembly by regulating trafficking and recycling of phospholipid scramblase ATG9A.
Subcellular location: Early endosome membrane {ECO:0000250|UniProtKB:Q9UNH6}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95219}; Cytoplasmic side {ECO:0000250|UniProtKB:O95219}.
Interaction partners:
- Sorting nexin-4
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 29
- Sorting nexin-6
- Sorting nexin-32
Sequence:
MDMNSFSPMMPTSPLSMINQIKFEDGPDLKDLFITVDAPESHVTTIETFITYRIVTKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVERFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKVFLTAQAEELSSYKKQGPGLLSRMGQTVRAVASSMRGVKNRPEEFMEMNNFIETFSQKINLIDKISQRIYKEERDYFDEMKEYGPIHILWSASEEELVDTLKGMAGCIEQCCKATEKRMAGLSEALLPVVHEYVLYSEMLVGVMKRRDQIQTELDSKVEALTYKKADIDLLTEEIGKLEDKVECANNALKADWERWKQNMKNDLRSAFTDTAEQNIRYYEQCLATWESFLTSQTDLPSEEDSEEKL
Protein: Vitamin K-dependent protein Z (P22891)
Organism: Homo sapiens (Human)
Function: Appears to assist hemostasis by binding thrombin and promoting its association with phospholipid vesicles. Inhibits activity of the coagulation protease factor Xa in the presence of SERPINA10, calcium and phospholipids.
Subcellular location: Secreted.
Interaction partners:
- Protein Z-dependent protease inhibitor
- Vitamin K-dependent gamma-carboxylase
- Furin
Sequence:
MAGCVPLLQGLVLVLALHRVEPSVFLPASKANDVLVRWKRAGSYLLEELFEGNLEKECYEEICVYEEAREVFENEVVTDEFWRRYKGGSPCISQPCLHNGSCQDSIWGYTCTCSPGYEGSNCELAKNECHPERTDGCQHFCLPGQESYTCSCAQGYRLGEDHKQCVPHDQCACGVLTSEKRAPDLQDLPWQVKLTNSEGKDFCGGVIIRENFVLTTAKCSLLHRNITVKTYFNRTSQDPLMIKITHVHVHMRYDADAGENDLSLLELEWPIQCPGAGLPVCTPEKDFAEHLLIPRTRGLLSGWARNGTDLGNSLTTRPVTLVEGEECGQVLNVTVTTRTYCERSSVAAMHWMDGSVVTREHRGSWFLTGVLGSQPVGGQAHMVLVTKVSRYSLWFKQIMN
Protein: Ras-related protein SEC4 (O42819)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP-bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as the attachment site for the SEC8/SEC15 particle (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome J complete sequence
- Rab GDP dissociation inhibitor
- Candida glabrata strain CBS138 chromosome K complete sequence
- Probable vacuolar protein sorting-associated protein 16 homolog
- Exocyst complex component SEC15
- Exocyst complex protein EXO70
- Protein transport protein SEC9
- Exocyst complex component EXO84
- Exocyst complex component SEC5
- Candida glabrata strain CBS138 chromosome J complete sequence
Sequence:
MSALRTVSGSSGNGKSYDSIMKILLIGDSGVGKSCLLVRFVEDKFNPSFITTIGIDFKIKTVDINGKKVKLQLWDTAGQERFRTITTAYYRGAMGIILVYDVTDERTFANIKQWFKTVNEHANDEAQLLLVGNKSDMDTRVVTYEQGEALAKELGLPFIESSAKNDDNVNEIFFTLARLIQEKIDSNKLSGPNSGKDGNISINANKGDSSKSNCC
Protein: CEA cell adhesion molecule 3 (A0A0G2JW44)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MELSSVLPCKRCTPWRGLLLTASLLTCWLLPTTAQVSIESLPPQVVEGENVLLRVDNLPENLIAFVWYKGLTNMSLGVALYSLTYNVTVTGPVHSGRETLYSNGSLWIQNVTQKDTGFYTLRTISNHGEIVSNTSLHLHVYSCFMSYAGPPTSAQLTVESAPTSVAEGASVLLLAHNLPENLRAIFWYKGAILFKDLEVARYVIGTNSSVPGPAHSGRETMHSNGSLLLQNVTRNDAGFYTLRTLSTDLKAKVVHVQLQVNTSSCCDPLTPAPLTIDPVPRHAAKGESVLLQVRNLPEDLRMFIWFKSVYTSQIFKIAEYSRAINYVFRGPAHSGRETVYTNGSLLLQDATEKDTGLYTLQIIYRNFKIETAHVQVSVHKPVAQPFIRVTESSVRVKSSVVLTCLSADTGTSIQWLFNNQNLRLTQRMLLSQTKCQLSIDPV
Protein: Tenomodulin (TeM) (rTeM) (Chondromodulin-1-like protein) (ChM1L) (rChM1L) (Myodulin) (Q9ESC2)
Organism: Rattus norvegicus (Rat)
Function: May be an angiogenesis inhibitor.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000250}.
Interaction partners:
- Mohawk homeobox
- Scleraxis bHLH transcription factor
- Decorin
- Fibromodulin
- Thrombospondin-4
- Biglycan
- Collagenase 3
- Collagen alpha-1
- Aggrecan core protein
Sequence:
MAKNPPENCEGCHILNAEALKSKKIRKSLKICGLVFGILALTLIVLFWGSKHFWPEVSKKTYGMEHTFYSNGEKKKISMEIDPITRTEIFRSGNGTDETLEVHDFKNGYTGIYFVGLQKCFIKTQIKVIPEFSEPEEEIDENEEITTTFFEQSVIWVPAEKPIENRDFLKNSKILEICDNVTMYWINPTLIAVSELQDFEEDGEDLHFPTSEKKGIDQNEQWVVPQVKVEKTRRTRQASEEDLPVNDYTENGIEFDPMLDERGYCCIYCRRGNRYCRRVCEPLLGYYPYPYCYQGGRVICRVIMPCNWWVARMLGRV
Protein: Epididymal-specific lipocalin-9 (MUP-like lipocalin) (Q8WX39)
Organism: Homo sapiens (Human)
Subcellular location: Secreted.
Interaction partners:
- Epididymal-specific lipocalin-8
- Cystatin-11
- Epididymal-specific lipocalin-6
- Epididymal-specific lipocalin-12
- Epididymal-specific lipocalin-10
- Lipocalin-1
Sequence:
MALLLLSLGLSLIAAQEFDPHTVMQRNYNVARVSGVWYSIFMASDDLNRIKENGDLRVFVRNIEHLKNGSLIFDFEYMVQGECVAVVVVCEKTEKNGEYSINYEGQNTVAVSETDYRLFITFHLQNFRNGTETHTLALYETCEKYGLGSQNIIDLTNKDPCYSKHYRSPPRPPMRW
Protein: Transmembrane protein (Q581D5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Acyl-CoA dehydrogenase, mitochondrial, putative
Sequence:
MLRLRCLLCVPAVAGQRRVIMRSQSWVSVRYVGSSSRVHARFLGRGCSFGAALSEQHRWMRVGAHKRAAGSADETSQGGAEGEDGAPRGDRANTTSGIHSHIQGLKEDIRKFPDIYNSANAFNFILFTAFCLCSTGSNVEEKWWMDNWGIDATFAPWAWLLHSFMMNNFLSAAFSMLLLHTMCHSVLPTIGSRGLVIYCVITAVTSGFIMWVGNKLANNTSEKQFGPWDIVAALFVMQYLHQGFTPVQILNSFTGWLRYACWVGAVCIAYYDWQPTAVGTLMGLALCKGHPRFRVTTGAV
Protein: Serine/threonine protein phosphatase 2A regulatory subunit (Q8IN90)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGKDNQISVIYAPLQANKLKDNTPPYDAPPPTPISKVLNITGTPIVRKEKRQTSARYNASKNCELTALIPLNEKTAASEREELFIQKIQQCCTLFDFSEPLSDLKFKEVKRAALHEMVDFLTNQNGVITEVIYPEAINMFAVNLFRTLPPSSNPNGAEFDPEEDEPTLESSWPHLQLVYELFLRFLESPDFQPSMAKRFIDHQFVLQLLDLFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNVFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKQFLLKVLLPLHKAKSLSVYHPQLTYCVVQFLEKDPSLSEAVIKSLLKFWPKTHSPKEVMFLNELEELLDVIEPAEFQKVMVPLFRQIAKCVSSPHFQVAERALYYWNNEYIMSLITDNSAVILPIMFPALNRNSKTHWNKTIHGLIYNALKLFMEIDQRLFDECSKNYKQEKQMEREKLSQREELWQQVESLAKTNPEWTKARRFNDCLPVSDSRALCDQYSENSDSAYDQSEQRARQPPPPLPPQKQAHQEPREVRQALATLTTLNNY
Protein: Nickel transport system permease protein NikB (P33591)
Organism: Escherichia coli (strain K12)
Function: Involved in a nickel transport system, probably translocates nickel through the bacterial inner membrane.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Nickel import ATP-binding protein NikD
- Nickel-binding periplasmic protein
- Nickel transport system permease protein NikC
- Nickel import ATP-binding protein NikE
- Dipeptide transport system permease protein DppC
- Probable D,D-dipeptide transport system permease protein DdpC
- Glutathione transport system permease protein GsiD
- Putrescine export system permease protein SapC
- Oligopeptide transport system permease protein OppC
- Nickel-responsive regulator
Sequence:
MLRYVLRRFLLLIPMVLAASVIIFLMLRLGTGDPALDYLRLSNLPPTPEMLASTRTMLGLDQPLYVQYGTWLWKALHLDFGISFASQRPVLDDMLNFLPATLELAGAALVLILLTSVPLGIWAARHRDRLPDFAVRFIAFLGVSMPNFWLAFLLVMAFSVYLQWLPAMGYGGWQHIILPAVSIAFMSLAINARLLRASMLDVAGQRHVTWARLRGLNDKQTERRHILRNASLPMITAVGMHIGELIGGTMIIENIFAWPGVGRYAVSAIFNRDYPVIQCFTLMMVVVFVVCNLIVDLLNAALDPRIRRHEGAHA
Protein: At2g15560 (Endonuclease or glycosyl hydrolase) (Q6NQ97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit, cytoplasmic
- Phenylalanine--tRNA ligase alpha subunit, cytoplasmic
Sequence:
MIQNAMSSYYNPSAATTLVSIDSDEQRRIKYLADLNMIATQRHSSTDGPMAILWDMENCPVPSDVRPEDVASNIRMAIQLHPVISGPVVNFSAYGDFNGFPRRVREGCQRTGVKLIDVPNGRKDASDKAILIDMFLFVLDNKPPATIVLVSGDVDFAPALHILGQRGYTVILVIPSSVYVNSALSNAGKFVWDWHSIVHGEGFVPRCKPRVVPYLMGCNIGDNSNMDGLNEDETILYRGNCYSSDPRESSSLMVSQFRNEYSSGVMSCWPSNSGESMACPPSGHLESTMWVAPGDLNGLKGQLVKLLELSGGCIPLMRVPSEYQRKFSKPLFVSDYGVAKLVDLFKKMSDVIVVDGKGNKRFVYLRNSKPNIISPSSPVVLLRRERKGKEPNGVTTNGGVSSDEMSDTGSVQSERNLEEFKFELQDILVSYCCQVQMDCFEAIYKLRYKRPLAYTNMGVNHLEQLFDKLRDVVAIHEDPATGRKLISPV
Protein: Cysteine repeat modular protein 2 (Q8IBR8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Gametocyte-specific protein
Sequence:
MRNSDFFFFFFVLLNCFLNIQPYVSNATSNIIKEKNTSFVKKIYDDPYIKKDVTLQLKNAKYNHINKKISKSKKNVKKKRGISFVSLNLNKILELQDKNPIKLISNIYAKDKSKFLSTCYENNKLNDINNCNRFTISKQICDTPVGFNLNDNFLVKETGGLSSTCLVDNKPEYWKIYNNHIIVESGEYFDLKIRNETFLLQTSIIITKDICMNKTKIESSYFTYQNNHSKIGNPILYKGEVIGMEIKNIKVKDDVEGLFNVCSCYLDNEHHAYNKCSETNKHYMQISSIRIIKKIVHNINILTGKKLHINLQNYVTPYPIKSAFIIKKVEHYSCNNINNKSFNEIQEHFYNNEKKLKFYNIFLYETDLQEFKEDIIFENPGMYLLCYTSNDSQSEYSAELSTILVNGYDISKMNYLYLDLYENKLNLRNSVVLHRYNLNEKLEEIFFKKKETIQCSGEDIIYSNNITETKSYKSDDNSDDDVIIDTIYIYNINLNAYDQILEICSKKYNEYSLIGYTTIKPYILHNYKDINHLTHFNIPPDHVRTYVVDKKSNILTFFPQLLNIFNQNDINDMYMSFSCYSSKNEIIITYSFDKNMTPTFFKYLKISDASSSILYITNKGVYLYVLKKKSQLLFLYDITPEKVKKKKKIITNKKINDDYLELLLSYYLDYYDFTKCEQCLSPILMEPIYDEKQNLKHIFLITSHPLAKLLIVGLDFKIIYKHDNNDVKNVVTTIRGFNFTSDVLKYSSFLITGISCGILKNESLDCFLIDQLNNTIIAIEYLQKQKTIILIDSFQGENKNELNYESINLNDFVFSQSNSYLHTPRNAIAYSFGESYVIFVNENESNELNLLFYDKNKADNNLSYITKINNTYINDGAIENIYKFYDHKDLINRNVLLIMKYYEGDVYFMYIPLRNIANKLELAYDYPTVIQDNGNTYTMKIKSEEIKKMNALVNFQIEVHNVNKSKYVTIDKYDGTIEIKLSEFVGDSVNLTAKLHGFFLELNVNITFTVICSNGMKALNGICIPCPLGSYNNINEYIKNNNIYECTLCHNNSTTKNEGSTSISQCLCLPGYELNNNDLCVPCKRGTWKTKLSNSPCIFHCYPNSYSLVQGSRSEEESKCKCKRGFYFVSKDSINFCDNCNIGYFCPGGYKIGEKKCPKNTTNITQNNFSISSCKCDVGFEPFDSSNLNAYNFKNDPIFNDYKDFLDDVKSSQICVPCKEGFYKNTVSEEKCKRCSDNVYTDGLQSTSISNCKKCEKGYYLQSEDSCIICPDNHYCPGAYINDPKYAIYENQKIPCGDKSLTIPPNNLNVSHLNCLCKKGFEFIKTDDNEFDCLEVPKNYYKSHLGNKEKEPCPENSVTLYTQTKSKVKCLCMPGYYWDLKEFKCIKCPKGHYCPGGYLKNCFNNQNLHSCKPQKKKCPLKNSTTQTKESFSQSSCLCDKGYTINKEELRECIPCPINTYKDVISNAECTKCLTPYTTDGQIGSTKEEDCTCSGGFFFLNHCLPCSDKNTYCKGGKMIVNNKNKTIHYGPSKCPPNTTVSFETERPYNKGFCVCQKGFKHVYTTSDFTKICAPCERGFFKTIIGDFSCESKCKPNSTSFVGTIHETHCFCLENYYFKNGICLNCPDGAYCEGGFQKETLLYMKKNEYYLDTSKIKHIMPVPKENYALYKLKTNIYNTDWFIVECPIKEACLYNEKCHESMTNFLCGECKKGYTNNFSKLNLCIKCSGHIMNILHMIFVSIFILLFTVIMAYLNVFTGANRKSVHSIVIKIAVNYFSCMKIFYVMGISELYFPVTFSSHVNYILKNIKRLLKAKKNYGLYCILTNYFDLSHADAYFYGMVYHAFRPVFLAIILTLLMFIVVEIYKYKVRNETNIKLNITDKIKELGKDKLHEEIMNELPSERALVLFRYIPIPGDSRFKRIKNFLEDMIPMYVTLLFFIHTKTTYYMLTLLDCKALYYNDKFVEQYMSYVPSIKCDLSKSYSKFFILGLTGLIVWGIGIPLMSYLVLYKNRKQLHSENILFKYGFLNNGFNFQFWYWESIVFLRKILVLLISTVPIFKNAKIFGTTMWLFTIISSIFLTLQVILQPFDSRNYHILNKLETYSMVAWTMTLIIFVFLTISNTNVTINFYVLLFLLFFNFVFIAKILISLCYSYIENLRHMKKRIKLPFLRIFFEKMSKIAEEKDYKDPVVSLNTHDNSIQFTRKYKKKYISCSFKNNMLTTEEKNYFLDVISNFIYFGVLNLNFSVFHSYFMEFMLRLSIIDNEMLYRKGGNGILKLIAKDPNKIDKWIKIKEREINKKTFFERHKKILNLFSKSLFVIQNNIKSIVYKGDKHTIISDYEVLINVLKYDEDFITDFKFLYDDNAVKSGLILSDLHLSFTKIKMKDKELIKQLFSLFIAKKNIVQFERDIQLKNKIEQLTSLYDILIKSSEKKKLTFRKNVEDAVKGDPFDYKILENELKSVNDRINNLIENYRKLKDVDYFEGMDNIDEEKMDLNNDSEFFNNKLLELSFKELKDDITENEQNEDISKKEKEKIYDETTNDDQTK
Protein: ATP-dependent DNA helicase II subunit 2 (EC 3.6.4.12) (Q9I7M8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR016570}.
Interaction partners:
- DNA ligase 4
- ATP-dependent DNA helicase 2 subunit 1
- Double-strand break repair protein
- Aprataxin and PNK-like factor
- Exonuclease 1
- Serine/threonine-protein kinase ATM
- Poly [ADP-ribose] polymerase
- FI04011p
- Protein CNPPD1
- FI03211p
Sequence:
MASNKECLIIVLDVRTCAAEEVKLKSAKCVAEILKDKIVCDRKDYVSFVLVGCDTDEIKTEDASHPNVLPFGEPRLCSWQLLLEFFQFVNKTACEDGEWLNGLQAALELQNVATTLRVARRRILLLFDFNDFPQDYEKFNEITDELLGENIELIVGTHNIAYIDNAITSQPQAIFNFSRKCGPDELNNQKYALSLVPRCNATLCSFKEALHTVFKVTNRRPWVWNAKLNIGSKISISLQGIIAMKNQTPVKLVKVWAEKDEIVIRETRHYIKGTEITPLPENLITGYMLGGTPVPYDEAVLEPKEPHPPGLHFFGFIKRNAVPDEYFCGESLYLLVHQKHNQSAAVKLDALVRALVSSDRAILCWKIYSTKFNRPQMVVLLPRLADDTHPATLYMLEVSYTSQHHFWDFPALRTTKTECSEEQLNAIDQLIDSTDLECTLRDTQQPRPWAQNDLLPFDALPSIFEQNVMDILERKVIYDNDKEDKMLKDKNFADVFWRVPDPLEEKSKRAAAIVKKLFPLRYSRAWQEKLLAKEQAENGVAVKSEPAEKEIPLPSDGVGLIDPISDFRRVLASVHTISNATERDARFQALAADTRVVIITLLQRRKQNIGQLGELITLYRQSCIDFNTFLEYDKFAEELKKIALAKNRSEFWQDVMVDKQLGPLVLGEPTLDDELALKAYYTIENWVESGANDMEDVEM
Protein: Hsp70/Hsp90 co-chaperone cns1 (O13754)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Co-chaperone that binds to the molecular chaperones Hsp90 and Hsp70. Stimulates Hsp70 ATPase activity, but not Hsp90 ATPase activity. Involved in only a subset of Hsp90 functions (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Protein HGH1 homolog
- Small ribosomal subunit protein eS7
- Hsp90 co-chaperone Cdc37
- Heat shock protein sti1 homolog
- Chromatin structure-remodeling complex subunit snf21
- Heat shock protein 90 homolog
- 40 kDa peptidyl-prolyl cis-trans isomerase
Sequence:
MAGFQSSEVDPNTKNKNAEEMFNELNKVPFFMQSLEDVGDESENNVQLDALKALAYEGEPHEVAQNFREHGNECFASKRYKDAEEFYTKALAQKCGDKDIEIACYSNRAACNLLFENYRQVLNDCAQVLQRDSTHAKAYYRSAKALVALKRYDEAKECIRLCSLVHPNDPAILALSKELQKKSDDFEKRESEKKRVAQEKVIAAKTVLLALQERHIKTKTTEHPPDLGDAMISLSTFDDPKSELFFPTILLYPLVYQSDFVPSVSENCTPLELLKTVFQSPAPWDVHQLYNPDSLDVFATTDTLGLIKVGKNVPILKALTHPKVTLIDGLVQLHVVPHHLASDWISSWKKNKQENAKN
Protein: Nem (Q94543)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFQRSYSKVWWGSEQSSLTSGGFYSSFSGGSSTSSTSTYPQRQPASLGPLGNLSCIQEEVEDEQNSSKLSWHKHDSPGSLRSQDSGFSDNEESHQVQHQQNLSPPSPQSDKQQTPAATPTSVHSVATPPTVVRRVGNSSFYSPLISVTRRISFTSGQITPKARSGDEDAEDAELEASRSRLFEQLDSMKLDDGEAEAEEDSPPRPAIRRRRRLMRKPMPEPEAASASEEEEVVIAPPPPPPYNNETVYLGEAPPPYNNETVTFGATEQDESLQQQPSPLRVRSLRFTASTSTPKSGSKIAKRGKKHPEPVASWMSEQRWAGEPEVMCTLQHKSIAQEAYKNYTITTSAVCKLVRQLQQQALSLQVHFERSERVLSGLQASSLPEALAGATQLLSHLDDFTATLERRGVFFNDAKIERRRYEQHLEQIRTVSKDTRYSLERQHYINLESLLDDVQLLKRHTLITLRLIFERLVRVLVISIEQSQCDLLLRANINMVATLMNIDYDGFASLSDAFVQNEAVRTLLVVVLDHKQSSVRALALRALATLCCAPQAINQLGSCGGIEIVRDILQVESAGERGAIERREAVSLLAQITAAWHGSEHRVPGLRDCAESLVAGLAALLQPECCTQTLLLCAAALNNLSRMEATSHYSIMSNEAIFRLIDTLEHQTCGTSVFLYEQIVGMLHNMSLNKKCHSHLANGVIINFITSVYQTGILPNLRLTCGKRCPAPHHQDHSAHPDPAGQRFADPRSGAPGAVASAGPAASIPGP
Protein: ETV5-related protein Ets96B (Q8MRW5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required in dopaminergic neurons to regulate expression of genes involved in dopamine signaling. Decreases expression of the dopamine transporter DAT and increases expression of the dopamine transporter Vmat and the tyrosine 3-monooxygenase ple which is involved in dopamine biosynthesis. Also involved in negatively regulating the expression of a group of endoplasmic reticulum proteins, the molecular chaperone Calr and the protein disulfide isomerases CaBP1 and ERp60.
Subcellular location: Nucleus {ECO:0000255, ECO:0000255|PROSITE-ProRule:PRU00237}.
Interaction partners:
- Taiman, isoform G
- Small conductance calcium-activated potassium channel protein
Sequence:
MTISWRALSHFLIPQSDYGEAKTHLEQLQQTLTHLDHPHHHHAHHPHHHLGLYHGALPNTSTITTDSVVSCVSSTLPAVAKAISASSSCDGLQSERKKCPISDLDSGGHGHGQGHGLMEAICAGQKTSPIPPPPPPCCLTLGESSSSPNPIATAALMNASTSGSSSAGGASASLCNDLTRESSWYAHHHHHHHHHHHQLPDELVMYATPTPTPAIGKFGLDTSTEGYLNARYNVNVKGVRHDRTSSFFDIPAVTHPHNHPHPHPHPHPHPYCYRFPSSPPAGILKKSDEEATSAAVYCSDVSSGQHFPHHTKIEHADSTTTAAQQQQQQQEQQQQQQQQQQQQQHQQQLQQAAALHPHHHHSHHGHHGHQQAEQQALTHLTPLHAASAFKFSHTAVISSSAVYATPSHYAHQQQTQSQSVYRDLSPTTLAAVSDADLKYDSGPYNAAISSTYPSALRPNVVDSTTSSDAELRLDQFYASNGISTSSNGQAISQRRGSLQLWQFLVALLDEPTTSASCIAWTGRGMEFKLIEPEEVARRWGLQKNRPAMNYDKLSRSLRYYYEKGIMQKVNGERYVYRFVCDPDALFNMAYGHLTTGSGKGDQHQLTLSLAKTPPTSGDSQTQSPRVAKSEYYDTAALHKY
Protein: Prosaposin (A0A0J9YXB8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADICKNYISQYSEIAIQMMMHMQDQQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVEPIKKHEVPAKSDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEVVDT
Protein: Isoliquiritigenin 2'-O-methyltransferase (MsCHMT) (EC 2.1.1.154) (Chalcone O-methyltransferase) (ChOMT) (Licodione 2'-O-methyltransferase) (MsLMT) (EC 2.1.1.65) (P93324)
Organism: Medicago sativa (Alfalfa)
Function: Methylates the 2'-hydroxyl of isoliquiritigenin and licodione. Does not methylate narigenin chalcone, caffeic acid or daidzein. Involved in the root nodulation initiation by promoting the biosynthesis of nod-inducing molecules.
Interaction partners:
Sequence:
MGNSYITKEDNQISATSEQTEDSACLSAMVLTTNLVYPAVLNAAIDLNLFEIIAKATPPGAFMSPSEIASKLPASTQHSDLPNRLDRMLRLLASYSVLTSTTRTIEDGGAERVYGLSMVGKYLVPDESRGYLASFTTFLCYPALLQVWMNFKEAVVDEDIDLFKNVHGVTKYEFMGKDKKMNQIFNKSMVDVCATEMKRMLEIYTGFEGISTLVDVGGGSGRNLELIISKYPLIKGINFDLPQVIENAPPLSGIEHVGGDMFASVPQGDAMILKAVCHNWSDEKCIEFLSNCHKALSPNGKVIIVEFILPEEPNTSEESKLVSTLDNLMFITVGGRERTEKQYEKLSKLSGFSKFQVACRAFNSLGVMEFYK
Protein: Zinc finger CCCH domain-containing protein 49 (AtC3H49) (Q9M0G2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT3g17750/MIG5_4
- Vacuolar protein sorting-associated protein 20 homolog 2
- Polyadenylate-binding protein 3
- At5g46710
- Pumilio homolog 11
- Putative pumilio homolog 10
- Pumilio homolog 9
Sequence:
MMIGETRRTYPTVEIPPWPVLEELTTSEFFSPVMNSPDCSMLEALAGLQRYLPSNEPDPESYPDLLGPDSPIDAYSCDHFRMYDFKVRRCARGRSHDWTECPYAHPGEKARRRDPRKYHYSGTACPDFRKGGCKKGDSCEFAHGVFECWLHPARYRTQPCKDGGNCLRKICFFAHSPDQLRFLHTRSPDRVDSFDVSSPIRARAFQLSISPVSGSPPMSPRADSESSPMTQSLSRSLGSCSINDVVPSFRNLQFNSVKSFPRNNPLFGFGSPRGSILGPGFQSLPTTPTRPGNLDIWEYGLEEEPVMERVVESGRELREKMREKLHKENCMDRVAQDPDQNLGEAPDVGWVSDLLM
Protein: C-type lectin domain-containing protein (Q3LFM3)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein.
- SCP domain-containing protein
- NR LBD domain-containing protein
- Nose resistant-to-fluoxetine protein N-terminal domain-containing protein
- CYtochrome P450 family
- Nuclear receptor domain-containing protein
Sequence:
MFFNFLIFSVIAGLSNAACLDSNDQEIQGFCFKFVAQQMTYSDARNWCRYKNPAGSSYLAYVPNKDTSNYLAFYARSAFGTSAEYFWIGLSRNESSGSLSWDNGLPVVYTNLGSYLGQNYFSEKISNTKWDTLGDNSTNYFVCSYASTSDQATSTEPPTNNCQPGGQQTILFAYSNDLDPSVVTDTLINSYLSSQPVTFAVSRFDLRQPEDIGYFNTYNEAASYVSTHRPDSTKRLGDNSTGSDVLDVINKFYNNTQLSPCESVVMVLSKRYPNTTDISNIVSKVRKYHGIVNFLASNTPSGGTQTRVLFDLASKTNGIYSIESDSNFSHFIEWMPLRERYPIYAVNARVLGQGSQALPSMSVPVYAEYLLMIALQNHMPVSNVQSVSLSWYNQFSVDSSSFDMQPLGWAYVDSNSDGTREHLGTVVYNMTIDYVYNDIDVETMQVRFYSPYATDFWQPYSD