wanglab/gogpt-training-data huggingface dataset:
Protein: Formin-F (Diaphanous-related formin dia1) (Q5TJ56)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Formins play an important role in the nucleation of actin and the formation of linear actin filaments.
Interaction partners:
- Rho-related protein racE
Sequence:
MNRIFGRKKKDKDSDEKGSTESENDFLSSLPAKANKRYSMAYSSLQPDGNNSTNSKSADKFDDKGKAVDTPEFFVNTINLLPNIEILAQLCSSLQSKPSAWSKSLIDCNGIEALLNVLAFIERNGQKDSDVILQSLAVTCLLSLLNSKYGIEKAIATPNSMIRLITSMDTPKADTRSSVFEILTAICMISEKGYQLILEAMTHFKQVRKERFRFTFLVESMKKVMNSSDKEYLTTCLTLVNGIVNSSEEIDERIQLRTEFTRLGLDEVISVNKNIPYEEAPDLLTQIDVYEDEQRADQEELSERFEDLDIDINDPQVIFNEIYKQAKDRLHHPLLAILQSLLSISSDTEVGMLSWFLIEKLVLQISVNKPMIGDDDGKVSLEDLLASTAPSVALQSEFQKNIEELAKVKDQLKKANFDLNIANQELSSRSHESSVLKSNMFNTVKQKDQEIIKLRGQMKRIDSNFFSPPGGDGDDHINVINTPEESSPHHESPRKQQQQTSKPPLNPKSSKPPISSSQLKEKSKSNLSSSSSDSLSNDFKSQVEVAQQQQPQQQNIESTLTPEPTQIIKEEPIVTTPPPAPPAPPPPPMMGGGPPPPPPPPMMGGGGPPPPPPPPMMGGGPPPPPPMGGKGGPPPPPGGGGFGLFNSNKPPANAPKFTVSKPTTKVKQFQWTKIPNKKLGETIFTNLGTIKTDWLNVGEIENLFFAPEANSQKKLEASDKKSTSSTKPGTVSVIDPKKSQNLAIYLSKFKCPLEEIKTALYTLDEDIFTMESLKALEQYLPTDEDMEAIKDYLKKDGELKMLTKAEHFLLEMDSVSSLAERVKSFYLKILFPDKLKEIKPDLELFTKTIKDIKNSKNFLKVMEVVLIIGNFLNGGTARGDCFGFKLDALLKLADTKTANNKSNLLVYIISELEQKFPDSLKFMDDLSGVQECVKISMNTISADLNLLKKDLDAVNNGIGKMKRSKEESYFFSTMDDFIKDANIEIKIAFDQFQEAEKNFQELAVLFGEESKIPSEEFFVTINRFIVMFDKCYKDFQRDKEAAERAIKRDEAKAKKAQQLKRMNGKIASSTNNKNPLASSSTSVGDGGMVEDIMQSVRDGDAFKQRRRLKGTKENTDDSSSITTISEQSENSNTSSITITTPSGIELDITPSKSGSRREKKTSKSSDKDKEKEKEKEKQCESTESEDINKKDINVAAKALTIVMRSKQTMHSRIDTFNFDA
Protein: DNA polymerase gamma, catalytic subunit (A0A590UK63)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
KRPQHLPGHPGWYRKLCPRLDDPAWTPGPSLLSLQMRVTPKLMALTWDGFPLHYSERHGWGYLVPGRRDNLAKLPTGTTLESAGVVCPYRAIESLYRKHCLEQGKQQLMPQEAGLAEEFLLTDNSAIWQTVEELDYLEVEAEAKMENLRAAVPGQPLALTARGGPKDTQPSYHHGNGPYNDVDIPGCWFFKLPHKDGNSCNVGSPFAKDFLPKMEDGTLQAGPGGASGPRALEINKMISFWRNAHKRISSQMVVWLPRSALPRAVIRYRLSDEGEWLVRELNLPVD
Protein: At1g24230 (Paired amphipathic helix (PAH2) superfamily protein) (B2GVM8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
Sequence:
MVGGSLSPAFTIDEATSYINAVKEAFGADQPAKYREFLDIMLDLRANRVDLATVVPRMRELLKDHVNLLLRFNAFLPAEAKETFHDVRSYIYSLKESFRDEPAKYAQFLEILNDYSARRVDAPSAVARMTELMKDHRNLVLGFSVLLSTGDTKTTPLEAEPDNNKRIRVANFISKLKARFQGNDGHVYESFLEILTMYQQGNKSVNDLYQEVVALLQGHEDLVMEFSNVFKRTTGPSGSKSARDR
Protein: Intraflagellar transport protein 80 (Q388A9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
- Intraflagellar transport protein 57/55
- IFT80/172/WDR35 TPR domain-containing protein
- Intraflagellar transport protein IFT88, putative
- Intraflagellar transport protein A1
- Uncharacterized protein
- C2H2-type domain-containing protein
- Intraflagellar transport protein component, putative
- Intraflagellar transport protein 56 homolog
- Intraflagellar transport
- Intraflagellar transport protein 22
Sequence:
MRLNITIPNEHHDDACTCVAVSLTGDVLSAGDDFVLRRWSPNGEPMGKVKEFDSCITYIAWVPLQGGRKGRSANTGSVEGKGNYLVACADGTISFMNTSSDRVERTIDAHTGTITGVVYSGDTSSIISSGEDGCVKVWSQAGIPRTTLVSAGRCVYGICWGSETTELGGDCVLYCVGSEVTIKPLNPAVKKQLKWKAHNGIVLAADWSLMTGFIVTGGEDGTYKVWDPYGRSIYVSAAGGHPCTAVKFSADGEMFAVGSFMNIRVCDKTGWSHTYERLSEGSALSLQWTADGTQVVMGCGSGSVCTAQLIDRKMYWSHFCVTLVDGNRLLVQDVLTDAVEEVEQRDKVIKVEVGYGYLVSCTTTQCACYPIDRLSAPVQFDLRDVVITLILGQKHLLLADCNSGMQIYSYEGRLICTLRLQSFLRPEIMAPDLVSLSPDTVAIRNPADPRKILFFDTTNGKAMEDATITHHLDVISLELSQHGELSERKIAFVDRNRDMHFGAVHRKVGAAQKISTMTSSLAWHGEHEILVAIADGRLTTWYYPTILFSDRGLLPTTKTVRDDGGDEFSRNDRIVSFSGTRVSIRRGVDGALLTFNTSPYPSFIFEHVARHDFSSATRLARFLDEKPLWGILAGLALRHGDLNVVEIAYGALFELDKVRYIRYLKSIPTPEGRQAELALFQRRSAEAERILLQAGLIYRCIDMHTRLFNWERALEVAAERKTHVDTVLARRRRYLDAVKRTEDIPLFKELGASVRVDWETVVEKVRQEEEKEAQRPGAKPYQ
Protein: Tubulin-specific chaperone A (TCP1-chaperonin cofactor A) (Tubulin-folding cofactor A) (CFA) (O75347)
Organism: Homo sapiens (Human)
Function: Tubulin-folding protein; involved in the early step of the tubulin folding pathway.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-2A chain
- Tubulin alpha-4A chain
- Tubulin-specific chaperone E
- Tubulin-specific chaperone D
- Tubulin beta-4B chain
- NADH dehydrogenase 1 beta subcomplex subunit 4
- Tubulin beta-2B chain
- Tubulin beta-4A chain
- Tubulin beta-3 chain
- Tubulin beta-6 chain
Sequence:
MADPRVRQIKIKTGVVKRLVKEKVMYEKEAKQQEEKIEKMRAEDGENYDIKKQAEILQESRMMIPDCQRRLEAAYLDLQRILENEKDLEEAEEYKEARLVLDSVKLEA
Protein: GTP-binding protein (Q22743)
Organism: Caenorhabditis elegans
Interaction partners:
- DAF-15
- Target of rapamycin homolog
- Ras-related GTP-binding protein C
- Nitrogen permease regulator 2
- GATOR complex protein NPRL3
- Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5
- Ragulator complex protein LAMTOR2 homolog
- Target of rapamycin complex subunit lst8
- UDENN FNIP1/2-type domain-containing protein
- UDENN FLCN/SMCR8-type domain-containing protein.
Sequence:
MSSKRKVLLMGKSGSGKTSMRSIIFANYIARDCSRLGPTIEVEHAHVKFLGNMVLHLWDCGGQESFMENFLVSQKDQIFKNVQVLIYVFDVESREFEKDLRYYQSCLEALLQNSPNAQVFCLIHKMDLIEEDKREETFKRREADVLRYSELAATPLQNERTNAVCQCFKSSIWDETLYKAWSAIVYHLVPNVGTMEDKLKKFGAILDADEVILFERATFLVIAHAVLREHKDPHRFEKVSNIIKQFKLSCTKMGSKLDSIQVRNSQFSAFIDSFTQNTYVMIVIPDGNASAPMITMNVKNARKVFEAIETKS
Protein: Tetraspanin-12 (Tspan-12) (Tetraspan NET-2) (Transmembrane 4 superfamily member 12) (O95859)
Organism: Homo sapiens (Human)
Function: Regulator of cell surface receptor signal transduction. Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activates the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1) (By similarity). Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Frizzled-4
- Norrin
- Low-density lipoprotein receptor-related protein 5
- Zinc finger protein 408
- Disintegrin and metalloproteinase domain-containing protein 10
Sequence:
MAREDSVKCLRCLLYALNLLFWLMSISVLAVSAWMRDYLNNVLTLTAETRVEEAVILTYFPVVHPVMIAVCCFLIIVGMLGYCGTVKRNLLLLAWYFGSLLVIFCVELACGVWTYEQELMVPVQWSDMVTLKARMTNYGLPRYRWLTHAWNFFQREFKCCGVVYFTDWLEMTEMDWPPDSCCVREFPGCSKQAHQEDLSDLYQEGCGKKMYSFLRGTKQLQVLRFLGISIGVTQILAMILTITLLWALYYDRREPGTDQMMSLKNDNSQHLSCPSVELLKPSLSRIFEHTSMANSFNTHFEMEEL
Protein: Insulin-like growth factor-binding protein 5 (IBP-5) (IGF-binding protein 5) (IGFBP-5) (P24593)
Organism: Homo sapiens (Human)
Function: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
Subcellular location: Secreted {ECO:0000269|PubMed:18930415, ECO:0000269|PubMed:20345844}. Cytoplasm {ECO:0000269|PubMed:20345844, ECO:0000269|PubMed:26103640}. Nucleus {ECO:0000269|PubMed:20345844, ECO:0000269|PubMed:26103640}.
Interaction partners:
- Insulin-like growth factor 1
- Insulin-like growth factor 2
- Insulin-like growth factor-binding protein complex acid labile subunit
- Insulin-like growth factor-binding protein 3
- Pappalysin-1
- Vitronectin
- Pappalysin-2
- Four and a half LIM domains protein 2
- Fibronectin
- Thrombospondin-1
Sequence:
MVLLTAVLLLLAAYAGPAQSLGSFVHCEPCDEKALSMCPPSPLGCELVKEPGCGCCMTCALAEGQSCGVYTERCAQGLRCLPRQDEEKPLHALLHGRGVCLNEKSYREQVKIERDSREHEEPTTSEMAEETYSPKIFRPKHTRISELKAEAVKKDRRKKLTQSKFVGGAENTAHPRIISAPEMRQESEQGPCRRHMEASLQELKASPRMVPRAVYLPNCDRKGFYKRKQCKPSRGRKRGICWCVDKYGMKLPGMEYVDGDFQCHTFDSSNVE
Protein: Transcriptional adapter 2 (C8V3C2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR025024}.
Interaction partners:
- Transcriptional regulator Ngg1, putative
- Transcription initiation factor TFIID subunit 9
- SAGA-like transcriptional regulatory complex subunit Spt3, putative
- SAGA complex component
- histone acetyltransferase
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 12
- Transcriptional activator spt7
- Transcription initiation factor TFIID subunit 6
- Transcriptional co-activator
Sequence:
MGVIRKKTATRGTEAGTKYHCDVCSVDVTSTVRISCAHPSCPEYDLCVPCFAAGEKTKNHDPSTHPFQVIEQNSVPIFQEDWGADEELLLLEGAEIYGLGSWADIADHIGGYRTKEEVRDHYLSTYIDSPNFPLPERADPEDTRLQDSISKEEFQARKKRRIEERKEAAKAAPPTTPKQKPTASVPACHEVQGYMPGRLEFETEFMNDAEEAVQHMTFEPGAGETPNGETDAEMELKMTVVDIYNTRLTARTERKKILFEHNLLEYRKNTALEKKRTKEERELLNKAKPFARMMNHEDFEEFNKGLEYEHNLRLAIAQLQEWRQMGIADLKGGEKYEQEKQQRAQRLMPQGSFDRFASTRPKQNQQSEQPTAANQLTTPELPLRLQKAADASSKAQEPNVPLNDFDRMFAANGDGPATQPPKTKFVVQPLNGVIPWKLENEGAPDLHLLTKEEVELCDALHIQPKPYLVIKETLLKESMKAGGSLKKKDARALCKIDGNKSSRIFDFMVHSGWINKG
Protein: DNA double-strand break repair helicase HerA (EC 3.6.4.12) (Q97WG8)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Involved in DNA double-strand break (DSB) repair. Acts probably with NurA to stimulate resection of the 5' strand and produce the long 3' single-strand that is required for RadA loading (By similarity). Exhibits DNA-dependent ATPase activity and DNA helicase activity.
Interaction partners:
- DNA double-strand break repair nuclease NurA
- DNA double-strand break repair Rad50 ATPase
- DNA double-strand break repair protein Mre11
- Ferritin-like diiron domain-containing protein
Sequence:
MIIGYVIGQATTQEALILAERPVRLGTYVVLEYDNVKALGLITNVTRGSPMLDDNMNDIEIVQRLKQFNNSIPVYTKAKVKMLCDMNNHFLMPDIPPFAGTPAREAEDEELKSIYSQDGQIRIGSLIGKNVEVKLNINSFARHLAILAATGSGKSNTVAVLSQRISELGGSVLIFDYHGEYYDSDIKNLNRIEPKLNPLYMTPREFSTLLEIRENAIIQYRILRRAFIKVTNGIREKLKEGQIPFSTLNSQFYELMKDELETQGNSDKKSSAKDEVLNKFEEFMDRYSNVIDLTSSDIIEKVKRGKVNVVSLTQLDEDSMDAVVSHYLRRILDSRKDFKRSKNSGLKFPIIAVIEEAHVFLSKNENTLTKYWASRIAREGRKFGVGLTIVSQRPKGLDENILSQMTNKIILKIIEPTDKKYILESSDNLSEDLAEQLSSLDVGEAIIIGKIVKLPAVVKIDMFEGKLLGSDPDMIGEWKKVEESEKIAKGFADFGTEIGD
Protein: CUB_2 domain-containing protein (O62153)
Organism: Caenorhabditis elegans
Interaction partners:
- Nose resistant-to-fluoxetine protein N-terminal domain-containing protein
- Regulator of Cold-induced Diapause
- Uncharacterized protein
- CUB_2 domain-containing protein
- Arrestin C-terminal-like domain-containing protein
- CUB-like domain-containing protein
Sequence:
MVLLTLLAFSTLFISCFAQQLIKLSSFKGLRVHNEINVEAPFHMYLSAQSDSYSILRQIFLITEDGSTTLSSLTQYNGQINPFVVEKSVYLTTTLNDDVMKTLNGVIFISSKKKRADSCLGVYNIGHETGIGNDNIYVCTYLILNTSLNKYVISQWSQDPTSKAYLYAGIPQDSPEPENTQIFSNPVHTNEGDFYFYYVNDFSLSMTAFYVKRFNNVFFVIDQENSSNRVVNGSWTRDVTSTGFYMKPLGSADNTTIVNIKRDTKHTGFSGANVVGNLPNGGSVTVGFYGDGTKYERTVTPNTSITSWTIPYIERTFQVSSTNGKDGEYYVQYFVSEGSLNGSIVTTTSPPPSTTSKFRIEATTTSKFRIEATTRSTGLVRFVLSMATLMMFWL
Protein: Tetraspanin-14 (Tspan-14) (Transmembrane 4 superfamily member 14) (Q8QZY6)
Organism: Mus musculus (Mouse)
Function: Regulates maturation and trafficking of the transmembrane metalloprotease ADAM10. Negatively regulates ADAM10-mediated cleavage of GP6. Promotes ADAM10-mediated cleavage of CDH5.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8NG11}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 10
Sequence:
MHYYRYSNAEVSCWYKYLLFSYNIVFWLAGVVFLGVGLWAWSEKGVLSDLTKVTRLHGIDPVVLVLMVGVVMFTLGFAGCVGALRENICLLKFFCGAIVLIFFLELAVAVLAFLFQDWVRDRFREFFESNIKSYRDDIDLQNLIDSLQKANQCCGAYGPEDWDLNVYFNCSGASYSREKCGVPFSCCVPDPAQKVVNTQCGYDVRIQLKSKWDEFIFTKGCIQALEGWLPRNIYIVAGVFIAISLLQIFGIFLARTLISDIEAVKAGHHF
Protein: Scrapie-responsive protein 1 (Scrapie-responsive gene 1 protein) (ScRG-1) (O88745)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2
Sequence:
MMKSVVLVILGLTLLLETQAMPSSRLSCYRKLLKDRNCHNLPEGRADLKLIDANVQHHFWDGKGCEMICYCNFSELLCCPKDVFFGPKISFVIPCNNH
Protein: Ornithine aminotransferase, mitochondrial (EC 2.6.1.13) (Ornithine--oxo-acid aminotransferase) (P04182)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reversible interconversion of L-ornithine and 2-oxoglutarate to L-glutamate semialdehyde and L-glutamate.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P04181}.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate synthase
- Arginase-2, mitochondrial
- Arginase-1
- Argininosuccinate lyase
- N-acetylglutamate synthase, mitochondrial
- Argininosuccinate synthase
- Ornithine decarboxylase
- Antizyme inhibitor 2
- Ornithine transcarbamylase, mitochondrial
- Glutamate dehydrogenase 1, mitochondrial
Sequence:
MLSKLASLQTVAALRRGLRTSVASATSVATKKTEQGPPSSEYIFERESKYGAHNYHPLPVALERGKGIYMWDVEGRQYFDFLSAYGAVSQGHCHPKIIEAMKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYNKVLPMNTGVEAGETACKLARRWGYTVKGIQKYKAKIVFAVGNFWGRTLSAVSSSTDPTSYDGFGPFMPGFETIPYNDLPALERALQDPNVAAFMVEPIQGEAGVIVPDPGYLTGVRELCTRHQVLFIADEIQTGLARTGRWLAVDHENVRPDIVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHGSTYGGNPLGCRIAIAALEVLEEEHLAENADKMGAILRKELMKLPSDVVTAVRGKGLLNAIVIRETKDCDAWKVCLRLRDNGLLAKPTHGDIIRLAPPLVIKEDEIRESVEIINKTILSF
Protein: Probable circularly permuted 1,3-beta-glucanase TOS1 (EC 3.2.1.39) (Secreted protein TOS1) (A0A1D8PJA8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Secreted {ECO:0000269|PubMed:26453650, ECO:0000303|PubMed:17905924}.
Interaction partners:
- Secreted beta-glucosidase SUN41
- Cell surface mannoprotein MP65
- Ecm33p
- Secreted beta-glucosidase SIM1
Sequence:
MKFSSTTLLAGLSSLTATVSAGCSFEGGNYYCSETKKVIYKGIGFSGTYMDVTNMDESTGKCTQQSYSFSGNLSPLDEELSVHFRGPLTLLQFGVYYPSSSGNSKRQIDDQDCNVKHVHHKHKRATEVVQVTQTVFVDGNGNTVTSQALQTSTVESSPAVSSAAADDNANSGSGSGSSAGSGSGYGSVSALDGEGKAYRSDISTKSAPTSTSAQPSSSETASVDGAWTRDSYYTPGSTDNCVFLNYHGGSGSGVWSAKFGNSLSYANADNSGGSSTPVPLEETTIKSGEEYIIFSGSKCGSSSDCGYYRKGTVAYHGFKGASKIFVFEFEMPSDTNGNGYNQDMPAVWLLNAKIPRTLQYGEATCSCWKTGCGELDLFEVLSSGSNKMISHLHDGQGSSQNSNNGGGGSQDYFERPTSGTFKGVVIFEGDEIHILQVDDETEFGSSLDEETVNAWLKEAGSVATIGY
Protein: Protein kinase, putative (Q583H1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSYTTESAFYRKYHLTDRTPIGKGTFALVYKCVNRITKESYAVKIVDKNMTLPNDIQSVSLEVHIMKQIGNHPHVARLVDYFETRESIYIVMDLLSGGMVFDRIAELSHYDEKIAADLVRNVLSGLVHIHSRGIIHRDLKPENLLLRPQRDSDDTSWLSDVCISDFGLASTGPGKACCGTAKYIAPEVVKVGYYGTVKGTYDNKCDVWSLGVITFVLLSGKMPFYGATHREIFRRIVDGKWSFGGPIWNTISLMGKSFIRSCLTRDPAKRPSARELLNHPWITDDQPDKHLGESIEEIRSLTAITKLRGATAVIRTSHEMLGGIDSCASFTKHLRHKDKLSTIIEVVSQTDPTVVHLVDFGKVLASRGGHKLQDCCSCSSQTVCRHIQNVHEYLFVGNRRRKVYPFLYSLRAMQSNAELDVKLSLGKDDRAGKVLSAVEKIIEAAFAFSTALEAVPQERLKGNVPIDCEWRQVSERTKALVSGCK
Protein: Ewing's tumor-associated antigen 1 (Ewing's tumor-associated antigen 16) (Q9NY74)
Organism: Homo sapiens (Human)
Function: Replication stress response protein that accumulates at DNA damage sites and promotes replication fork progression and integrity. Recruited to stalled replication forks via interaction with the RPA complex and directly stimulates ATR kinase activity independently of TOPBP1. Probably only regulates a subset of ATR targets.
Subcellular location: Nucleus {ECO:0000269|PubMed:27601467, ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720}. Note=Localizes at sites of DNA damage following replication stress (PubMed:27601467, PubMed:27723717, PubMed:27723720). Recruited to stalled replication forks via interaction with RPA1 and RPA2 subunits of the RPA complex (PubMed:27601467, PubMed:27723720). {ECO:0000269|PubMed:27601467, ECO:0000269|PubMed:27723717, ECO:0000269|PubMed:27723720}.
Interaction partners:
- ATR-interacting protein
- Replication protein A 32 kDa subunit
- DNA topoisomerase 2-binding protein 1
- Replication protein A 70 kDa DNA-binding subunit
- Serine/threonine-protein kinase ATR
- Breast cancer type 1 susceptibility protein
Sequence:
MSRRRKHDDSPSPKKTPHKTVAAEECGSVVEPGRRRLRSARGSWPCGAREGPPGPVRQREQPPTAALCSKSNPEERYETPKRALKMDSLSSSFSSPNDPDGQNDIFWDQNSPLTKQLGKGRKKQIYTTDSDEISHIVNRIAPQDEKPTTNSMLDMWIGETAIPCTPSVAKGKSRAKISCTKLKTQSQEEELMKLAKQFDKNMEELDVIQEQNKRNYDFTQMISETEILSNYKDNIQMWSLHNIVPEIDNATKKPIKGNTKISVANNQNSSQKPFDQIAEAAFNAIFDGSTQKCSGQLSQELPEAFWSTSNTTFVKTNALKEEKIITNETLVIEKLSNKTPRSLSSQVDTPIMTKSCVTSCTKEPETSNKYIDAFTTSDFEDDWENLLGSEPFAMQNIDMPELFPSKTAHVTDQKEICTFNSKTVKNTSRANTSPDARLGDSKVLQDLSSKTYDRELIDAEYRFSPNSNKSNKLSTGNKMKFENSSNKIVIQDEIQNCIVTSNLTKIKEDILTNSTEASERKSALNTRYSNEQKNKCILNQSIKAPVNTDLFGSANLGSKTSVSNPNQTSASKVGSFFDDWNDPSFANEIIKACHQLDNTWEADDVDDDLLYQACDDIERLTQQQDIRKDSKTSESICEINNNSEHGAKLTQQQDIRKDSKTSESICEINNNSEHGAKNMFAISKQGSNLVQSKHLNPGSISVQTSLTNSSQIDKPMKMEKGEMYGNSPRFLGATNLTMYSKISNCQINNLHVSYTNTDVPIQVNSSKLVLPGSSSLNVTSDHMNTEITTYKKKLSTNQPCHKTVTDEAQSNLNTTVGFSKFTFTRMKNSQILSQFNQNCITGSMSDTKITQGVEKKKGVNPLLEEAVGQQSLVKLSESLKQSSKEEEEKNRKCSPEEIQRKRQEALVRRMAKARASSVNAAPTSFL
Protein: Fcgbp protein (Q6IS34)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
ERLCECGPDGQVTCQEGADCEPYEECRIENGVQACHPTGCGHCLANGGLHYVTLDGRVYDLHGSCSYVLASVCHPKPGDEEFSIVLEKNSAGDPQRVVVTVAGQVVGLARGPQVTVDGEVVTLPVATGHVSVTAEGRNIVLQTNKGMKVLFDGDAHILMSIPSSFRGRLCGLCGNFNGNWSDDFVLPSGAVAPNVEAFGTAWRAPGSSLGCGEGCGPQGCPVCLAEETQAYEKNDACGKIRDPHGPFAACHKVLSPLEYFRQCVYDMCAHKGDKAYLCRSLAAYTAACQAAGAAVKPWRTDSVCPLQCPAHSHYSICTRSCQGSCAALSGLTGCTTRCFEGCECDDHFLLSHGVCIPAQDCGCVHNGQYMPVNSSLMSSDCSERCFCSPNNGLTCHEAGCPSGHVCEIQAGVRECQAARGLCSISVGANLTTFDGAHNAISSPGVYELSSRCPGLQKNVPWYRVLADVQPCHNNDKIVSKVHIFFQDGLVTVIPSKGAWVNGLRVDLPATVLTSVSVRRMPDGSMLVHQKAGVTVWLGKDGLLDVMVGDDLAAMLCGACGNFDGDQTNDAYGSQGKTPIEKWRAQDFSPCSN
Protein: Auxin-responsive protein SAUR28 (Protein SMALL AUXIN UP RNA 28) (Q9SRW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as positive effectors of cell expansion through modulation of auxin transport (By similarity). Involved in thermo-responsiveness of plant architecture. Enhances plasma membrane H(+)-ATPase.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FJG1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9FJG1}.
Interaction partners:
Sequence:
MALVRSIFSAKKILGGSLARTSKAPKGFLAVYVGENQEKKQRYFVPVSYLKQPSFQALLSKCEEEFGFDHPMGGLTICCPEYTFISITSRIQ
Protein: Protein-glutamine gamma-glutamyltransferase E (EC 2.3.2.13) (Transglutaminase E) (TG(E)) (TGE) (TGase E) (Transglutaminase-3) (TGase-3) [Cleaved into: Protein-glutamine gamma-glutamyltransferase E 50 kDa catalytic chain; Protein-glutamine gamma-glutamyltransferase E 27 kDa non-catalytic chain] (Q08189)
Organism: Mus musculus (Mouse)
Function: Catalyzes the calcium-dependent formation of isopeptide cross-links between glutamine and lysine residues in various proteins, as well as the conjugation of polyamines to proteins. Involved in the formation of the cornified envelope (CE), a specialized component consisting of covalent cross-links of proteins beneath the plasma membrane of terminally differentiated keratinocytes. Catalyzes small proline-rich proteins (SPRR1 and SPRR2) and LOR cross-linking to form small interchain oligomers, which are further cross-linked by TGM1 onto the growing CE scaffold (By similarity). In hair follicles, involved in cross-linking structural proteins to hardening the inner root sheath.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q08188}.
Interaction partners:
- Caspase-14
- Corneodesmosin
- Loricrin
- Small proline-rich protein 3
Sequence:
MSALQIQNVNWQVPMNRRAHHTDKFSSQDSIVRRGQPWEIILVCNRSLESGEDLNFIVSTGPQPSESARTKAVFSISGRSTGGWNAALKANSGNNLAIAIASPVSAPIGLYTLSVEISSRGRASSLKLGTFIMLFNPWLQADDVFMSNHAERQEYVEEDSGIIYVGSTNRIGMVGWNFGQFEEDILNISLSILDRSLNFRRDPVTDVARRNDPKYVCRVLSAMINGNDDNGVISGNWSGNYTGGVDPRTWNGSVEILKNWKKSGFRPVQFGQCWVFAGTLNTVLRCLGVPSRVITNFNSAHDTDRNLSVDVYYDAMGNPLEKGSDSVWNFHVWNEGWFVRTDLGPTYNGWQVLDATPQERSQGVFQCGPASVNAIKAGDVDRNFDMIFIFAEVNADRITWIYNNRNNTQKQNSVDTHSIGKYISTKAVGSNSRMDVTDKYKYPEGSSEERQVHQKALDKLKPNASFGATSSRNPEGEDKEPSISGKFKVTGILAVGKEVSLSLMLKNMTNDRKTVTMNMTAWTIVYNGTLVHEVWKDSATISLDPEEEIQYPVKIAYSQYERYLKADNMIRITAVCKVPDEAEVVVERDVILDNPALTLEVLEQAHVRKPVNVQMLFSNPLDQPVNNCVLLVEGSGLLRGSLKIDVPSLRPKEKSRIRFEIFPTRSGTKQLLADFSCNKFPAIKAMLPIDVSE
Protein: Ribonucleoside-diphosphate reductase large subunit-like protein (H2A2P4)
Organism: Murid herpesvirus 1 (MuHV-1) (Mouse cytomegalovirus)
Subcellular location: Virion {ECO:0000256|HAMAP-Rule:MF_04027}. Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04027}.
Interaction partners:
Sequence:
MDRQPKVYSDPDNGFFFLDVPMPDDGQGGQQTATTAAGGAFGVGGGHSVPYVRIMNGVSGIQIGNHNAMSIASCWSPSYTDRRRRSYPKTATNAAADRVAAAVSAANAAVNAGAAAAAAGGGGGANLLAAAVTCANQRGCCGGNGGHSFPPTRTPKTNATAAAAPAVAGASNAKSDNNHANAASGAGSAAATPAATTPAAAAVEKRRPSPSPSTASTAPCDEGSSPRHHRPSHVSVGTQATPSTPIPIPAPRCSTGQQQQQPQAKKLKPAKADPLLYAATMPPPASVTTAAAAAVAPESESSPAASAPPAAAAAMATGGDDEDQSSFSFVSDDVLGEFEDLRIAGLPVRDEMRPPTPTMTVIPVSRPFRAGRDSGRDALFDDAVESVRCYCHGILGNSRFCALVNEKCSEPAKERMARIRRYAADVTRCGPLALYTAIVSSANRLIQTDPSCDLDLAECYVETASKRNAVPLSAFYRDCDRLRDAVAAFFKTYGMVVDAMAQRITERVGPALGRGLYSTVVMMDRCGNSFQGREETPISVFARVAAALAVECEVDGGASYKILSSKPVDAAQAFDAFLSALCSFAIIPSPRVLAYAGFGGSNPIFDAVSYRAQFYSAESTINGTLHDICDMVTNGLSVSVSAADLGGDIVASLHILGQQCKALRPYARFKTVLRIYFDIWSVDALKIFSFILDVGREYEGLIAFAVNTPRIFWDRYLDSSGDKMWLMFARREAAALCGLDLKSFRNVYEKMERDGRSAITVSPWWAVCQLDACVARGNTAVVFPHNVKSMIPENIGRPAVCGPGVSVVSGGFVGCTPIHELCINLENCVLEGAAVESSVDVVLGLGCRFSFKALESLVRDAVVLGNLLIDMTVRTNAYGAGKLLTLYRDLHIGVVGFHAVMNRLGQKFADMESYDLNQRIAEFIYYTAVRASVDLCMAGADPFPKFPKSLYAAGRFYPDLFDDDERGPRRMTKEFLEKLREDVVKHGIRNASFITGCSADEAANLAGTTPGFWPRRDNVFLEQTPLMMTPTKDQMLDECVRSVKIEPHRLHEEDLSCLGENRPVELPVLNSRLRQISKESATVAVRRGRSAPFYDDSDDEDEVACSETGWTVSTDAVIKMCVDRQPFVDHAQSLPVAIGFGGSSVELARHLRRGNALGLSVGVYKCSMPPSVNYR
Protein: Cadherin-like and PC-esterase domain-containing protein 1 (A4D0V7)
Organism: Homo sapiens (Human)
Interaction partners:
- Protein Wnt-16
Sequence:
MVCRPVFPCRRRFCPRPFLVGLVVAICLFYQTLTLRGSRKLTAAAPGAVPHTSTETQASRCKKGFSQDKQCFLLSGNAQETRKVKESMETHFGSHGRRAILYRPPFYSKTELQLHQHILTQHGYTVVIAEERLNAGLGPGLLEQGDLGSWDLLICLSSKKAEGTPCISKEVMCQLGLHQKANRLPEIQQPLCRKEGLCQIVRRFPELQLPVSPSVCLDQGMQLKPSTSSHLLKTVKPRVWKPGDWSREQLNETTVLAPHETIFRAEDLSVILKAYVLVTSLTPLRAFIHSTGTVWNPPKKKRFTVKLQTFFETFLRASSPQQAFDIMKEAIGKLLLAAEVFSETSTLGPKTFHRCRFCFQLLTFDIGYGSFMYPVVLQVHEHLNFQDYDNMDFEDQNTEEFLLNDTFNFLFPNESSLSIFSEIFQRLYRSDVFKGENYQKELNQCLSLEEINSIMTFIKELGSLGQFQLLFPSTTPGIQSLMHEFYDVANPVGNPGSVLTQYWSLLNVFEQFQFMNKKTQPHPLEWNSFTEDKNIEKPQVPFDAIENKKAAVPQIKNENKEIHCSDDENTPCHIKQIFTHPHLELNPDFHPKIKDYYCEVPFDVVTVTIGVETPKCLCKVHLYEQAGPSFASYPLGLGMNKISIFVVDESPAHGETLITYKLTIYREDRPSLPLFEAFTACGFVQDCGLLIHPEETCGLQPISSDYIEAILQSELKRCPSGDMKGQWIVPCLSCSDNRTCDWREITWQPHNCQYGVLTKPQLQQCLGGRKILFIGDSTNRGIMYYLIERLNETLQEWQKVHGTKFYHNVNGGKTLISYSYYPQFWISPSLRPTFENALEHLLQRSRPLENTGQTVLVVGGVQWLNSNHLQIIHKVLKRENLLNILVIIKTLGIGFHLPVDGVHFLTQSEVQNLWKENLIILDTAKKHGYEVVDTFTITMGRYKEFLQGKCGCHFHEVVKSKLSKEYNFIKMKRSRNHIMGRYFSNQSKLQQGTVTNFRSPYHVRGPINQVCSEILLSRMCANKRTM