wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclin-dependent kinase 1 (CDK1) (EC 2.7.11.22) (Cell division control protein 2) (Cell division protein kinase 1) (p34 protein kinase) (P04551)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cyclin-dependent kinase that acts as a master regulator of the mitotic and meiotic cell cycles. Required to drive the G1-S and G2-M transitions, and initiation of premeiotic DNA replication and meiosis II. More than 200 substrates have been identified. Substrate specificity is in part regulated by the bound cyclin protein. When complexed with cyclin cig2, it drives the G1-S phase transition. When complexed with cyclin cdc13, it drives the G2-M transition and initiation of meiosis II. Its activity rises throughout the cell cycle and substrate specificity is further influenced by activity thresholds with more sensitive substrates phosphorylated earlier in the cell cycle than less sensitive substrates. Phosphorylates dis1 during metaphase to ensure proper microtubule dynamics and accurate chromosome segregation. Phosphorylates the repetitive C-terminus of the large subunit of RNA polymerase II rpb1 (Probable). Inactivated by checkpoint signaling following detection of cellular damage, leading to cell cycle arrest to allow damage repair. Inactivated during G2 DNA damage checkpoint signaling. Inactivated in response to defective RNA splicing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- M-phase inducer phosphatase
- Cyclin-dependent kinases regulatory subunit
- G2/mitotic-specific cyclin cdc13
- G2/mitotic-specific cyclin cig2
- Cell division control protein 18
- Mitosis inhibitor protein kinase wee1
- WD repeat-containing protein srw1
- Cyclin puc1
- Start control protein cdc10
- G2/mitotic-specific cyclin cig1
Sequence:
MENYQKVEKIGEGTYGVVYKARHKLSGRIVAMKKIRLEDESEGVPSTAIREISLLKEVNDENNRSNCVRLLDILHAESKLYLVFEFLDMDLKKYMDRISETGATSLDPRLVQKFTYQLVNGVNFCHSRRIIHRDLKPQNLLIDKEGNLKLADFGLARSFGVPLRNYTHEIVTLWYRAPEVLLGSRHYSTGVDIWSVGCIFAEMIRRSPLFPGDSEIDEIFKIFQVLGTPNEEVWPGVTLLQDYKSTFPRWKRMDLHKVVPNGEEDAIELLSAMLVYDPAHRISAKRALQQNYLRDFH
Protein: Nuclear pore complex protein (Q386L6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|RuleBase:RU365072}. Nucleus membrane {ECO:0000256|RuleBase:RU365072}.
Interaction partners:
- Importin subunit alpha
- Sperm-associated antigen 6
Sequence:
MLTTFEQQHGMVELPPLGEKVSIYDRGSIFAVHDNWLDTGAANDTNSTSAHPSRAFAEVYLGSVVRSVFTADQFMRWSKRDNRVEESNLWSLLLELLLDAEQAVKYNPDAIGIAKVQPHRQWYVSHQAHIQDLLQRQPLLRRMNIIIRWLERVYRTGNAPLKLASSRTPEEAVLLRQIVLSCLRGGELHRAIDLSVTAKDCMYSCLLSAAQMQTVAEPWFNATPLVPLFGEYGNGEVDLEWACNEHRLDNLSQLYEDSVALSTSSEGQTAGGGLDGLIAAVLCGNLDVMEPAFATGNWKDVVWCHLRSALVLCFTKTLMAARHNVQAPYGALVERLTGSHDSWQDETAQSVVRRLADRLESSYFATVSFEEKLQMRVILHFLSSDNADWTNVLNDLSRVKGVAQSDPNGVRLVSHLLLCLDTAYSEALHSRSVQVYSTSLAEALTRYAESLVQLPHYAPQDAMRAVIAMNLRLRDARQRASVYAAFLVACRCRELQLTKREEVEALEEKLVQMFCKADPVSEVHDEVMRLLNQKVEPATLLTHNPLAEAVMWRAMHADSPDDFIVALRHSLEACGSFWLAEPRAELDAITDVAGIIRRTILPNLRRDSIALSATPTEMELAESHFWMTFAALRTAADQHAKTTARLDLALGGTDRTLEFQLVQDEAALMRELHSLARKALTYGGAVVHRSRSCVTAVTWLLQVFVEEVVLSVRLAASRSSVIVEYLRHVFELIEQINDSGYVEPSLMPQQSARDLFAAVRSLRMACGQKAHDLLVEEAKKVAVTQQQLFVTSQPKW
Protein: Alkaline exonuclease (Deoxyribonuclease) (UL12) (Q68978)
Organism: Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1)
Interaction partners:
Sequence:
MESTGGPACPPGRTVTKRSWALAEDTPRGPDSPPKRPRPNSLPLTTTFRPLPPPPQTTSAVDPSSHSPVNPPRDQHATDTADEKPRAASPALSDASGPPTPDIPLSPGGTHARDPDADPDSPDLDSMWSASVIPNALPSHILAETFERHLRGLLRGVRAPLAIGPLWARLDYLCSLAVVLEEAGMVDRGLGRHLWRLTRRAPPAAADAVAPRPLMGFYEAATQNQADCQLWALLRRGLTTASTLRWGPQGPCFSPQWLKHNASLRPDVQSSAVMFGRVNEPTARSLLFRYCVGRADDGGEAGADTRRFIFHEPSDLAEENVHTCGVLMDGHTGMVGASLDILVCPRDIHGYLAPVPKTPLAFYEVKCRAKYAFDPMDPSDPTASAYEDLMAHRSPEAFRAFIRSIPKPSVRYFAPGRVPGPEEALVTQDQAWSEAHASGEKRRCSAADRALVELNSGVVSEVLLFGAPDLGRHTISPVSWSSGDLVRREPVFANPRHPNFKQILVQGYVLDSHFPDCPPHPHLVTFIGRHRTSAEEGVTFRLEDGAGALGAAGPSKASILPNQAVPIALIITPVRIDPEIYKAIQRSSRLAFDDTLAELWASRSPGPGPAAAETTSSSPTTGRSSR
Protein: Bitesize, isoform H (B7Z0K1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNTMPGMGVGVGVTVGDCENYVQQQQPQQQQPQLEVTPTHHRLQVRRQSTLPAQPTPAIYMSTSPNRLYSRSPERSPGEQQRYPPFMRQTSFPEPPSTYHRTKLLPSTGAPPPTVAPPPLNYESQTSSLASDEQDVGPMPKPRMTRQATLPNPEQHVKLLPTSPPKRQTSPQFRRSPEFMRQQTLPNPEAFSSGNTLTVHSTPPAKFMPISPRAKQNFLFPSVPNPRQFLSQPHVPAVGGTELGSGGSVASTGVVGGGEQYSSSQSVNIHHSRDPHSKMIKVRSHSNEEYSNTKGHPENRRLLPEIPTAVQRPGGRSPSRLVRQDCLKEERTFGEAKQQFHQFPDVTEELDNRPEYVDYFGDSATSFLESDEVQYERNYNAGFSSEPRIIYNNGSDDGSYQNSSQRPIYSAENVLADSGYGGGAGVGLGASGGSGGVPGYYPDMGTPQGFYGGAALPRTPLMHNRIRRRQSRELQMQQEELAQLSQVSDANGKGSGNEGAASGSATDSHAAERRKPEQMRSVSEDSGAKTTPKPVTRRSFSHPEKDTQPTKKTEISKIPSPRPLADILDKTRGNSKIPQARRRNSRTGIGEAEEGSTPQHIYSFHQQLMHRNSDLAMRLKKTEIPVASVASTGQEEEKPHGESGQGSGAEQPVNGKSLESSANKEGGDPNSSAEATHTSTLGEQELQNAVEAAAVVFKKVVLQRRKEKEKAAEEEEAKVAAEELSRSPVIGQRQADGSGSPIQSRASSETWPTQSDEDIDRLVAMHQNRSSLSSLGVRSESMASVYSGAGEGRYGTVVVKGQVEFAMQYNYKLSALEVHVVRCKDLAAVDAKRNRSDPYVKVYLLPDKSKAGKRKTKVKKHTLNPIFDETMRFHTPISSLESRTLWLTVWHSDMFGRNDFLGEVSVNLQGRLFDNPQSQWYLLQERSEPFDEVATYRGDIVVGLKYIPPENIKSSFFSRGSSITGSSSNLRKFGGSIKSVASKSERTSKGGQLHVLVKEAKHLSPIKANGTCDAFCKSYLLPDRTRSSKQKTPVVKRTLHPSWNYTFVYEDVSLEELSERALELTVWDHDRLASNEFVGGIRFSLGTGRSYGRQVEWMDATGKELSLWQNMLDRPNFWVEGSLVLRSSLDGIRANLP
Protein: Myosin 28B1, isoform B (EC 5.6.1.8) (Q8IPH8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Uncharacterized protein, isoform D
- Dyschronic, isoform G
- Cadherin-99C
- Calcium and integrin-binding family member 2
- LD20463p
Sequence:
MDAGYSPRKGEYVWVKPQNTTSEFAVPFGARIVRTEKTQTLVCDDRNKQFWVPAGDVLKAMHITSQEDVEDMITLGDLQEYTILRNLQNRYAKQLIYTYTGSMLVAINPYQILPIYTNREIQLYRNKSLAELPPHIFAISDNAFQRLQRLKENQCVVISGESGAGKTESTKLILQYLAAISGKHSWIEQQIIEANPIMEAFGNAKTVRNDNSSRFGKYIEIRFTPQGAIQGARIQQYLLEKSRIVFQSRDERNYHIFYCMLAGLSTAERERLKLQEQSPSQYHYLAQGGCFTLPGRGDAKDFADIRAAMKVLSFKPEEVWSILSLLAAILHLGNLRFTATEVANLATAEIDDTPNLQRVAQLLGIPISALNAALTQRTIFVHGEHVTTSLSKEAAIEGRDAFVKSLYDGIFVRIVRRINETINKQVDQPMNSIGVLDIFGFENFDNNSFEQLCINYANENLQQFFVGHIFKMEQDEYQNEHINWQHIEFQDNQQILDLIGMKPMNLMSLIDEESKFPKGTDQTLLEKLHVQHGNRSIYVKGKTTQTSLFGIRHYAGVVMYNPLGFLEKNRDSFSGDLRTLVQRSTNKYLVDIFPHEMPMDTAKKQPTLCVKFRNSLDMLMRTLSQAHPYFIRCIKPNEYKEPKNFDKELCVRQLRYSGMMETARIRRAGYPIRHAYRAFVERYRLLVPPVGPLEQCDCRKLARQICEVALPADSDRQYGKTKLFLRDEDDASLELQRSQLMLKSIVTIQRGIRRVLFRRYMKRYREAIITVQRYWRGRLQRRKYQVMRQGFHRLGACIAAQQLTTKFTMVRCRTIKLQALSRGYLVRKDFQKKLLERRKQNQLKKEELLKLAKMKEAEELLRLQQLKEQKEREQREQQEKRLQEEQRLKAEAAARNALAMAAVQQKRRTKPVKQEAPKAPTLQARNSLPPPPTTLIVAAPLPTRPASAVTRINTIPESPGTIDVESSKQMVDDVFRFLNDEPDAALRKLNNISSGDTIRLPKSVPNNIDTSDFSYLKYAATYFGGGATAQHERKPLKKSLLKHEHPIDEMASKAIWLTILRFMGDLPDVVSSPTLHVFDNENLMSDLASLLNTSDSYKPRLFVRQSQRRIPKPLASGEKEAQEFYQHWLNVPTSHLEKIHFIIGHGIIKNSLRDEILAQICKQLYLNPSRSSYSRGWLLLSLCLSCFPPSKEFEPHLRSFMKQGTAQLQATPSLQRLERTLVNGPRCQPPSLFELHAIRGRHPLRLDIHLMDGQQRRLQVDAASTAREAVNQLCQGMGLTDTFGFGLVMSLNGKLMPLGAGQEHVLDAISECEQRQLDAPWKLYIRKEMFATWYDPSMDPKATQLIYKQILNGLKCGEYRCRSEKDIAMVCALACFVEYGPGEILRLKPSEITAFVPSDLLAPGERAIENWSRLIAATYEKSSYVKEEQNDLLLEAQKRAKEDICLFAHLSWPMRHSRLFEVVRKEGPKLQSDELMLGINSAGLFLIDETEQVLASCCFSEVLKVHVESDDKLHVMTFQHVNFVLQCSSAQDANEVINYMLDNLRQRSSYGVALDPVVEGDLEDCLVLNPGDLIEFEAGVTGAQLMAGNAQDCYRGCVNGQWGQFLAGNVRVLATLTKPSEKLQDILREGRFQEPPKPTPRANYSRRRQHNISQLAESHFREPLDSDKAPLSKFSPEPLKAPLLKAVVKVPPLFQQALVMHHHILKYMGDIARSNLPVNTDLIFQPALQHPLLCDELYCQLMKQLSDNPSSESEKRGWDLLYLATGLVAPSVLVMRELIILLRMRADALADACLKRLKRSLAQGQRKKAPHLIEVEGIQQRCLHIYHKIYFPDDTVEAFEIESHTRGAELIADIAQRLELKSPVGYSIFLKTGDRVYAMPEEEFVFDFITQLIYWLRQQRTIRSISDGQYQLHFMRKLWLNNHPGEDLNGDMIFSYPQELHKYLKGYYPIDCEQASRLAILVYSADHDVSLQRLPEVLTRLIPEDLIPLQTVAEWRQQILPKVHRDHLTEDHAKILFLQELSHFACFGSTFFVVKQQNDDALPETLLIAINSTGFHMLDPTTKEILRSYEYSQLGIWSSGKNHFHIRFGNMIGASKLLCSTTQGYKMDDLLASYVKYFNEHE
Protein: Tetraspanin-15 (Tspan-15) (Tetraspan NET-7) (Transmembrane 4 superfamily member 15) (O95858)
Organism: Homo sapiens (Human)
Function: Regulates maturation and trafficking of the transmembrane metalloprotease ADAM10. Promotes ADAM10-mediated cleavage of CDH2 (By similarity). Negatively regulates ligand-induced Notch activity probably by regulating ADAM10 activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26686862, ECO:0000269|PubMed:30463011, ECO:0000269|PubMed:31792032}; Multi-pass membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:26686862}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 10
- Tetraspanin-14
- Tetraspanin-5
- CD9 antigen
- Prostaglandin F2 receptor negative regulator
Sequence:
MPRGDSEQVRYCARFSYLWLKFSLIIYSTVFWLIGALVLSVGIYAEVERQKYKTLESAFLAPAIILILLGVVMFMVSFIGVLASLRDNLYLLQAFMYILGICLIMELIGGVVALTFRNQTIDFLNDNIRRGIENYYDDLDFKNIMDFVQKKFKCCGGEDYRDWSKNQYHDCSAPGPLACGVPYTCCIRNTTEVVNTMCGYKTIDKERFSVQDVIYVRGCTNAVIIWFMDNYTIMAGILLGILLPQFLGVLLTLLYITRVEDIIMEHSVTDGLLGPGAKPSVEAAGTGCCLCYPN
Protein: Chaperone DnaJ-domain superfamily protein (F4I8D6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At4g34790
- Transcription initiation factor TFIID subunit 13
- Auxin-responsive protein SAUR27
- SAGA-associated factor 11
- Heat shock 70 kDa protein 17
- Heat shock 70 kDa protein 5
- Heat shock 70 kDa protein 8
- Transcriptional regulator of RNA polII, SAGA, subunit
- Transcriptional regulator of RNA polII, SAGA, subunit
- Heat shock 70 kDa protein 7, chloroplastic
Sequence:
MEGGIRQTYYEILGVAVDSSAEQIRRAYHKLAKIWHPDRWTKDPFRSGEAKRRFQQIQEAYSVLSDERKRSSYDVGLYDSGEDEGYFDFVQEMVSLMSQTKREEKQYSLEELQTMVDDMVYEFQSEPLFQNQSMQMNFDLNQTPDWHSQMSLPLSSFEFYSQSSY
Protein: Putative lipoate-protein ligase A (EC 6.3.1.20) (Altered inheritance rate of mitochondria protein 22) (P47051)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes.
Interaction partners:
- Lipoyl synthase, mitochondrial
- Glycine cleavage system H protein, mitochondrial
- Octanoyltransferase, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Hydroxyacyl-thioester dehydratase type 2, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- mRNA-binding protein PUF3
- Pyruvate dehydrogenase complex protein X component, mitochondrial
Sequence:
MSMMLSNWALSPRYVGQRNLIHCTTLFHTLTRWAKDADDKYHDINSMYENMFTPSNDNVSILQDEGKSDYDTTKASSMEEDISAFNKDLYNFYNIGYAKQIMSASQLENIVKAKGRFVIQSLSTSPYYNLALENYVFKNTPRAKRGPDNCRLLFYINDRCAVIGKNQNLWQEVDLAKLKSKNFELLRRFSGGGTVLHDLGNVNYSYLTSREKFETKFFNKMIIKWLNSLNPELRLDLNERGDIIQDGFKISGSAYKIAGGKAYHHATMLLNADLEQFSGLLEPSLPNNMEWESSGVHSVKSKIKNVGIITPNQFIAVVSERFQKTFKVDGEIPIYYCDEFKSINDEIKDAMNTLQSEQWKYFSGPKFSVKIKDKGLTIKVEKGMIYDCDRNDLIGLEFKGFLENIDSYT
Protein: Hemolysin, chromosomal (P09983)
Organism: Escherichia coli
Function: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by forming a pore.
Subcellular location: Secreted {ECO:0000269|PubMed:3894051}. Host cell membrane {ECO:0000305|PubMed:12598051, ECO:0000305|PubMed:2121650}; Multi-pass membrane protein {ECO:0000305|PubMed:2121650}.
Interaction partners:
Sequence:
MPTITAAQIKSTLQSAKQSAANKLHSAGQSTKDALKKAAEQTRNAGNRLILLIPKDYKGQGSSLNDLVRTADELGIEVQYDEKNGTAITKQVFGTAEKLIGLTERGVTIFAPQLDKLLQKYQKAGNKLGGSAENIGDNLGKAGSVLSTFQNFLGTALSSMKIDELIKKQKSGGNVSSSELAKASIELINQLVDTAASLNNVNSFSQQLNKLGSVLSNTKHLNGVGNKLQNLPNLDNIGAGLDTVSGILSAISASFILSNADADTGTKAAAGVELTTKVLGNVGKGISQYIIAQRAAQGLSTSAAAAGLIASVVTLAISPLSFLSIADKFKRANKIEEYSQRFKKLGYDGDSLLAAFHKETGAIDASLTRISTVLASVSSGISAAATTSLVGAPVSALVGAVTGIISGILEASKQAMFEHVASKMADVIAEWEKKHGKNYFENGYDARHAAFLEDNFKILSQYNKEYSVERSVLITQQHWDTLIGELAGVTRNGDKTLSGKSYIDYYEEGKRLEKKPDEFQKQVFDPLKGNIDLSDSKSSTLLKFVTPLLTPGEEIRERRQSGKYEYITELLVKGVDKWTVKGVQDKGSVYDYSNLIQHASVGNNQYREIRIESHLGDGDDKVFLSAGSANIYAGKGHDVVYYDKTDTGYLTIDGTKATEAGNYTVTRVLGGDVKVLQEVVKEQEVSVGKRTEKTQYRSYEFTHINGKNLTETDNLYSVEELIGTTRADKFFGSKFADIFHGADGDDHIEGNDGNDRLYGDKGNDTLSGGNGDDQLYGGDGNDKLIGGAGNNYLNGGDGDDELQVQGNSLAKNVLSGGKGNDKLYGSEGADLLDGGEGNDLLKGGYGNDIYRYLSGYGHHIIDDDGGKDDKLSLADIDFRDVAFRREGNDLIMYKAEGNVLSIGHKNGITFKNWFEKESGDISNHQIEQIFDKDGRVITPDSLKKALEYQQSNNKASYVYGNDALAYGSQGNLNPLINEISKIISAAGNFDVKEERAAASLLQLSGNASDFSYGRNSITLTASA
Protein: Caspase recruitment domain-containing protein 18 (Caspase-1 inhibitor Iceberg) (P57730)
Organism: Homo sapiens (Human)
Function: Inhibits generation of IL-1-beta by interacting with caspase-1 and preventing its association with RIP2. Down-regulates the release of IL1B.
Interaction partners:
- Caspase-1
- Putative caspase recruitment domain-containing protein 17P
- Caspase recruitment domain-containing protein 16
- Apoptosis-associated speck-like protein containing a CARD
Sequence:
MADQLLRKKRRIFIHSVGAGTINALLDCLLEDEVISQEDMNKVRDENDTVMDKARVLIDLVTGKGPKSCCKFIKHLCEEDPQLASKMGLH
Protein: Uncharacterized protein Rv0966c (P9WKM1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Carbamoyl phosphate synthase small chain
- Dihydroorotase
- Uncharacterized protein Rv3412
- Ribonuclease VapC2
- Uncharacterized protein Rv0965c
Sequence:
MSNSAQRDARNSRDESARASDTDRIQIAQLLAYAAEQGRLQLTDYEDRLARAYAATTYQELDRLRADLPGAAIGPRRGGECNPAPSTLLLALLGGFERRGRWNVPKKLTTFTLWGSGVLDLRYADFTSTEVDIRAYSIMGAQTILLPPEVNVEIHGHRVMGGFDRKVVGEGTRGVPTVRIRGFSLWGDVGIKRKPRKPRK
Protein: DNA repair protein complementing XP-C cells homolog (Mutagen-sensitive 209 protein) (XPCDM) (Xeroderma pigmentosum group C-complementing protein homolog) (Q24595)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in DNA excision repair. May play a part in DNA damage recognition and/or in altering chromatin structure to allow access by damage-processing enzymes (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Uncharacterized protein, isoform B
- DNA repair endonuclease XPF
- UV excision repair protein RAD23
- General transcription factor IIH subunit 1
- UV excision repair protein RAD23
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB
- General transcription and DNA repair factor IIH helicase subunit XPD
- Dipeptidase
- DNA excision repair protein ERCC-1
- FI23547p1
Sequence:
MSDEEEDSVSEGFSASEDEWKPSKDVKGGESSDDDDSDFDELQAEGGAAGSSGRSSAVAGKRGDHKAPSGIKGSSVKKRKPTGQSLRSKLYNKYRPPPKTFPTSPSQQKENTPRASGSKNAKTPNESGARNQHGPADSSSESSVEDYLVNPADLDLHSTFFAGGQKEKSPAPQFDCNAGITNLSDSGSEDNNESSFEDKAGNAFDFRGLLENANSLERTRDALSKRNVTATPPRSQAATMDVNALLALGENQNYQSVEVEEREGNQRKKAGRGAPAAPPTLDEPSRLSKTKSTRIKRHTKTRPVSTVVANAGDTDDSDFEEVADADLSSDQDDGETPNISGDLEIRVGLEGLRPTKEQKTQHELEMALKRRLNRDIKDRQILLHKVSLMCQIARSLKYNRLLSESDSLMQATLKLLPSRNAYPTERGTELKYLQSFVTWFKTSIKLLSPNLYSAQSPATKEAILEALLEQVKRKEARCKQDMIFIFIALARGMGMHCRLIVNLQPMPLRPAASDLIPIKLRPDDKNKSQTVESERESEDEKPKKDKKAGKPAEKESSKSTISKEAEKKNNAKKAEAKPLSKSTTKGSETTKSGTVPKVKKELSLSSKLVEKSKHQKAYTSSKSDTSFDEKPSTSSSSKCLKEEYSELGLSKKLLKPTLSSKLVLKSKNQSSFSSNKSDTSFEENPSTSSSSKSLKEETAKLSSSKLEDKKVASPAETKTKVQSSLLKRVTTQNISESGDSKKPKVAPVDTFSPVAGRTRRATVKPKTEEKPQVVGSPVIPKLMLSKVKQLNAKHSDTENASPANKHLQEQRNTRETRSRSKSPKVLISPSFLKKKSDGADSTSDPQKHQMAPETKARISPNFLSEALPARQLRSRGQKASSLAIPQLDGGDDVPLPKKRPKLEKLKNSQDSDEVFEPAKPVKKAPVLPKSVQNLRKDRRVMSTDDEGGSRLNRKTDASDMWVEVWSDVEEQWICIDLFKGKLHCVDTIRKNATPGLAYVFAFQDDQSLKDVTARYCASWSTTVRKARVEKAWLDETIAPYLGRRTKRDITEDDQLRRIHSDKPLPKSISEFKDHPLYVLERHLLKFQGLYPPDAPTLGFIRGEAVYSRDCVHLLHSREIWLKSARVVKLGEQPYKVVKARPKWDRLTRTVIKDQPLEIFGYWQTQEYEPPTAENGIVPRNAYGNVELFKDCMLPKKTVHLRLPGLMRICKKLNIDCANAVVGFDFHQGACHPMYDGFIVCEEFREVVTAAWEEDQQVQVLKEQEKYETRVYGNWKKLIKGLLIRERLKKKYNF
Protein: Growth hormone (A4GX93)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
AFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVAFCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRELEDVTPRAGQILKQTHDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASCAF
Protein: Ankyrin repeat and SAM domain-containing protein 4B (Harmonin-interacting ankyrin repeat-containing protein) (Harp) (Q8K3X6)
Organism: Mus musculus (Mouse)
Function: As part of the intermicrovillar adhesion complex/IMAC plays a role in epithelial brush border differentiation, controlling microvilli organization and length. Plays a role in assembly of the complex (By similarity). May play a role in cellular response to endoplasmic reticulum stress.
Subcellular location: Cell projection, microvillus {ECO:0000269|PubMed:26812018}. Note=Localizes at the tip of microvilli (PubMed:26812018). May associate with endoplasmic reticulum membranes (PubMed:22589549). {ECO:0000269|PubMed:22589549, ECO:0000269|PubMed:26812018}.
Interaction partners:
- Unconventional myosin-VIIb
- Harmonin
Sequence:
MSTRYHQAASDSYLELLKEATKRDLNLSDEDGMTPTLLAAYHGNLEALEIICSRGGDPDKCDIWGNTPLHYAASNGHTHCISFLVNFGANIFALDNDLKSPLDAAASREQKECVALLDKAATVQNTMNPKRVTRLKEQALKNARKQMKECERLQERHQNKMARTYSKEDSGTISSSHSTLSRSFLSTTSAGRFGSLSKGIKDTFKIKSKKNKDTTEQLEKDGRSGQRPVMEVFREEEEDSFPKDFKEKLHFSVEEDDDVQHESILNRPGLGSIVFSRNRVLDFEDISDSKRELGFKMPSELFQRQGAAGTVEEEEEEEEEEEEEKREANGTAGDLPWDEEEVEWEEDAVDATPLEVFLQSQHLEEFLPIFMREQIDLEALLLCSDEDLQNIHMQLGPRKKVLSAIDKRKQVLQQPGQLVDTSL
Protein: Catenin alpha-2 (Alpha N-catenin) (Neural alpha-catenin) (P30997)
Organism: Gallus gallus (Chicken)
Function: May function as a linker between cadherin adhesion receptors and the cytoskeleton to regulate cell-cell adhesion and differentiation in the nervous system.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1638632}; Peripheral membrane protein {ECO:0000305|PubMed:1638632}; Cytoplasmic side {ECO:0000305|PubMed:1638632}. Cytoplasm {ECO:0000250|UniProtKB:Q61301}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q61301}. Cell junction, adherens junction {ECO:0000269|PubMed:1638632}. Cell projection, axon {ECO:0000305|PubMed:1638632}. Nucleus {ECO:0000250|UniProtKB:P26232}.
Interaction partners:
- Catenin beta 1
- Afadin, adherens junction formation factor.
- Cadherin-2
- Actin, cytoplasmic 1
- Alpha-actinin-4
- Alpha-actinin-1
- Tight junction protein 1
- Actin, cytoplasmic 2
- Uncharacterized protein.
- Catenin alpha 1.
Sequence:
MTSATSPIILKWDPKSLEIRTLTVERLLEPLVTQVTTLVNTSNKGPSGKKKGRSKKAHVLAASVEQATQNFLEKGDQIAKESQDLKEELVAAVEDVRKQGETMRIASSEFADDPCSSVKRGTMVRAARALLSAVTRLLILADMADVMRLLSHLKIVEEALEAVKNATNEQDLANRFKEFGKEMVKLNYVAARRQQELKDPHCRDEMAAARGALKKNATMLYTASQAFLRHPDVAATRANRDYVFKQVQEAIAGISNAAQATSPTDENKGHTGIGELAAALNEFDNKIILDPMTFSEARFRPSLEERLESIISGAALMADSSCTRDDRRKRIVAECKRAVRQALQDLLSEYMNNTGRKEKGDPLNIAIDKMTKKTRDLRRQLRKAVMDHISDSFLETNVPLLVLIEAAKSGNEKEVKEYAQVFREHANKLVEVANLACSISNNEEGVKLVRMAATQIDSLCPQVINAALTLAARPQSKVAQDNMDVFKDQWEKQVRVLTEAVDDITSVDDFLSVSENHILEDVNKCVIALQEGDVDTLDRTAGAIRGRAARVIHIINAEMENYETGVYTEKVLEATKLLSETVMPRFAEQVEVAIEALSANVPQPFEENEFIDASRLVYDGVRDIRKAVLMIRTPEELEDDSDFEQEDYDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEEKAKIAEQVEIFHQEKSKLDAEVAKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVINAAKKIAEAGSRMDKLARAVADQCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELIVSGLDSATSLIQAAKNLMNAVVLTVKASYVASTKYQKVYGTAAVNSPVVSWKMKAPEKKPLVKREKPEEYQTRVRRGSQKKHISPVQALSEFKAMDSF
Protein: 116 kDa U5 small nuclear ribonucleoprotein component (U5 snRNP-specific protein, 116 kDa) (Q9VAX8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- U5 small nuclear ribonucleoprotein 200 kDa helicase
- Pre-mRNA-processing-splicing factor 8
- U5 small nuclear ribonucleoprotein 40 kDa protein
- Pre-mRNA-processing factor 6
- U4/U6 small nuclear ribonucleoprotein Prp31
- Protein crooked neck
- Probable small nuclear ribonucleoprotein Sm D1
- Pre-mRNA-splicing factor Syf2
- RE11167p
- Pre-mRNA-splicing factor syf1 homolog
Sequence:
MDSDLYDEFGNYIGPDLDSDEEDEQSIYGQPDVQDDPEDAMDEDEVEPQEDEDKEVTAVVLHEDKRYYPSAVEVYGPDVETIVQEEDAQPLDKPLIEPVKKLKFQIKEQDMQETTYDMEFMADLMDTPPLIRNVALVGHLHHGKTTFVDCLIRQTHPQFETMEERQLRYTDTLFTEQERGCSIKATPVTLVLQDVKQKSYLLNIFDTPGHVNFSDEATAAMRMSDGVVLFIDAAEGVMLNTERLLKHAVQERQAITVCINKIDRLILELKLPPQDAYFKLKHIVEEVNGLLSTYGAPDDNLLVSPILGNVCFASSLYGFCFTLKSFAKLYADTYEGVAYLDFAKRLWGDMYFNSKTRKFSKKQPHNSAQRSFVEFILEPMYKLIAQVVGDVDTTLSDTLAELNVRVSKEEMKSNIRPLLRLVCNRFMGDCSGFVDMCVEHIKSPLENAKRKVDHIYTGPKEGDIYRDMISCNQYGTLMVHSSKMYPNDDCTFFQVLARIVSGTLHAGQEVRVLGENYTLQDEEDSRILQVGRLWVFESRYKVELNRVPAGNWVLIEGIDQCIVKTSTIVDINVPEDLYIFRPLKFNTQSIIKIAVEPVNPSELPKMLDGLRKVNKSYPLLSTRVEESGEHVILGTGELYLDCVMHDLRKMYSEIDIKVADPVVAFCETVVETSSLKCFAETPNKKNKITMISEPLEKGLAEDIENGTVCINWNKKRIGEFFQVNYDWDLLAARSIWAFGPDSTGPNILVDDTLPSEVDKNLLTAVKDSIVQGFQWGTREGPLCEEPIRNVKFKILDGVIANEALHRGGGQIIPTARRVAYSAFLMATPRLMEPYLFVEVQAPADCVSAVYTVLARRRGHVTQDAPVSGSPIYTIKAFIPAIDSFGFETDLRTHTQGQAFCLSVFHHWQIVPGDPLDKSIIIRPLEPQQASHLAREFMIKTRRRKGLSEDVSINKFFDDPMLLELARQDVLINYPL
Protein: ATP-dependent RNA helicase dbp6 (EC 3.6.4.13) (Q76PD3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 25
- Ribosome biogenesis protein erb1
- Large ribosomal subunit protein eL14
- Probable nucleolar pre-ribosomal-associated protein 2
- Multiple RNA-binding domain-containing protein 1
- Uncharacterized protein C14G10.02
- Large ribosomal subunit protein eL6
- ATP-dependent RNA helicase mak5
- Putative ATP-dependent RNA helicase PB1A10.06c
- ATP-dependent RNA helicase dbp9
Sequence:
MSVEVDKSSHSKPKIEKKSKRNKRKWLNDENKTHVTASEAAIERLKKSASFSQAAQQALKQSRKEDNERDIEMQDVDAEAQPHDLLPIPQPSVEDFVDSKPHVKNITSVLPKWLAEPITVDPNTTVEFSSLNISSKLVERLQKQNITRGFAVQAAVLPLLLQDGRHGPMYSYGGDVCVSAATGSGKTLSYVIPIVQCLSHRTVPRLRCVVIVPTRELTVQVAKTFEYYMSGAGLQVCAWTGQKSLRHETYQLNGDENECRIDVLVSTPGRLVDHIRNDESFSLQHLRYMVIDEADRLLDQSFQDWVDTVMMEISHPKCLQNKSNILDLDQNISPTFLPDIDTLLPYRLPSPLQKLVFSATLTRDPSKIASLKLHNPRLVLVQNKDMEVDDGGEIEDDAIVFSVPPTLQEYHVSVSSEKPILLYHLIHSKNLTNILCFVKSNEAAARLHRLLELIHESLNQSFSCGLFTSSLSRDERKKIISRFATGDLNLLVCSDLMARGIDVANTQNVINYDPPLSVRSYVHRIGRTARAGREGFAWTLVQSHEGHHFSKLVKQLRRTLPIKRIKIEFSHISEEFVVAYDKALEALRVEVFNSRYPQQKSFLT
Protein: Defensin-like protein 16 (Low-molecular-weight cysteine-rich protein 77) (Protein LCR77) (Plant defensin 1.2) (Plant defensin 1.2a) (Q9FI23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Confers broad-spectrum resistance to pathogens. Has antifungal activity in vitro.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Putative defensin-like protein 15
- Ethylene-responsive transcription factor ERF094
- Hevein-like preproprotein
- Defensin-like protein 17
- Basic endochitinase B
- Pathogenesis-related protein 5
- Pathogenesis-related protein 1
- Vegetative storage protein 2
- Pathogenesis-related protein 1
- CAP superfamily protein
Sequence:
MAKFASIITLIFAALVLFAAFDAPAMVEAQKLCEKPSGTWSGVCGNSNACKNQCINLEGAKHGSCNYVFPAHKCICYVPC
Protein: 2-vinyl bacteriochlorophyllide hydratase (EC 4.2.1.-) (P26165)
Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Interaction partners:
- Light-independent protochlorophyllide reductase subunit N
- Light-independent protochlorophyllide reductase subunit B
- 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase
- Bacteriochlorophyll synthase 33 kDa chain
- Chlorophyllide reductase 35.5 kDa chain
- Light-independent protochlorophyllide reductase iron-sulfur ATP-binding protein
- Chlorophyllide reductase subunit Z
- Magnesium-chelatase subunit H
- Chlorophyllide reductase 52.5 kDa chain
- Magnesium protoporphyrin IX methyltransferase
Sequence:
MPNSPQNPSRKALYTEEERARRDATPWTLVQAILAPLQFLAFGVSLVLVVRFLFTGEGYEAATISILIKTLLLYTIMVTGAIWEKVVFGQYLFAPAFFWEDVFSFGVIALHTAYLWALFTGQPDNMQMFIALAAYATYVINAGQFLWKLRQARLQAASEDAGTLVMERGTR