wanglab/gogpt-training-data huggingface dataset:
Protein: Bleomycin hydrolase (BH) (BLM hydrolase) (BMH) (EC 3.4.22.40) (Q13867)
Organism: Homo sapiens (Human)
Function: The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31875550}. Cytoplasmic granule {ECO:0000269|PubMed:31875550}. Note=Co-localizes with NUDT12 in the cytoplasmic granules. {ECO:0000269|PubMed:31875550}.
Interaction partners:
- NAD-capped RNA hydrolase NUDT12
- Caspase-14
- Keratocan
Sequence:
MSSSGLNSEKVAALIQKLNSDPQFVLAQNVGTTHDLLDICLKRATVQRAQHVFQHAVPQEGKPITNQKSSGRCWIFSCLNVMRLPFMKKLNIEEFEFSQSYLFFWDKVERCYFFLSAFVDTAQRKEPEDGRLVQFLLMNPANDGGQWDMLVNIVEKYGVIPKKCFPESYTTEATRRMNDILNHKMREFCIRLRNLVHSGATKGEISATQDVMMEEIFRVVCICLGNPPETFTWEYRDKDKNYQKIGPITPLEFYREHVKPLFNMEDKICLVNDPRPQHKYNKLYTVEYLSNMVGGRKTLYNNQPIDFLKKMVAASIKDGEAVWFGCDVGKHFNSKLGLSDMNLYDHELVFGVSLKNMNKAERLTFGESLMTHAMTFTAVSEKDDQDGAFTKWRVENSWGEDHGHKGYLCMTDEWFSEYVYEVVVDRKHVPEEVLAVLEQEPIILPAWDPMGALAE
Protein: Histone acetyltransferase (EC 2.3.1.48) (A0A8I5Y222)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR003048}.
Interaction partners:
Sequence:
MAEAGGVGPPALPPAPPHGSPRTLATAAGSSASCGPATAVAAAGTAEGPGGGGSARIAVKKAQLRSAPRAKKLEKLGVYSACKAEESCKCNGWKNPNPSPTPPRGDLQQIIVSLTESCRSCSHALAAHVSHLENVSEEEMNRLLGIVLDVEYLFTCVHKEEDADTKQVYFYLFKLLRKSILQRGKPMVEGSLEKKPPFEKPSIEQGVNNFVQYKFSHLPSKERQTTIELAKMFLNRINYWHLEAPSQRRLRSPNDDISGYKENYTRWLCYCNVPQFCDSLPRYETTKVFGRTLLRSVFTIMRRQLLEQARQEKDKLPLEKRTLILTHFPKFLSMLEEEVYSQNSPIWDQDFLSASSRTSPLGIQTVISPPVTGTALFSSNSTSHEQINGGRTSPGCRSSSGLEANPGEKRKMNNSHAPEEAKRSRVMGDIPVELISEVMSTITDPAGMLGPETNFLSAHSARDEAARLEERRGVIEFHVVGNSLNQKPNKKMLMWLVGLQNVFSHQLPRMPKEYITRLVFDPKHKTLALIKDGRVIGGICFRMFPSQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHEILNFLTYADEYAIGYFKKQGFSKEIKIPKTKYVGYIKDYEGATLMGCELNPQIPYTEFSVIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKDGVRQIPIESIPGIRETGWKPSGKEKSKEPKDPEQLYSTLKNILQQVKSHQSAWPFMEPVKRTEAPGYYEVIRFPMDLKTMSERLRNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCASVLEKFFFSKIKEAGLMDK
Protein: Sca1 complex scaffold protein scaA (Q54XY4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Component of the Sca1 complex, a regulator of cell motility, chemotaxis and signal relay. The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells where it regulates F-actin dynamics and signal relay by controlling the activation of rasC and the downstream target of rapamycin complex 2 (TORC2)-Akt/protein kinase B (PKB) pathway. ScaA acts as a molecular scaffold, bringing together gefA, gefH and phr with PP2A.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20493808}. Note=The Sca1 complex is recruited to the plasma membrane in a chemoattractant- and F-actin-dependent manner and is enriched at the leading edge of chemotaxing cells (PubMed:20493808). Membrane localization of the Sca1 complex is regulated by scaA phosphorylation by PKB and PKB-related PKBR1 (PubMed:20493808). {ECO:0000269|PubMed:20493808}.
Interaction partners:
- Ras guanine nucleotide exchange factor A
- Ras guanine nucleotide exchange factor H
- Protein phosphatase 2A catalytic subunit B
- Protein phosphatase 2A scaffold subunit
- Ras guanine nucleotide exchange factor C
- Sca1 complex protein phr
Sequence:
MSSLDPSLSTTPSTNRRGTFSKAKSFRRAALNLEPQGTPGQPHAFRFLSGEEYSGPDIIENIKKPININIESEEYKTPLFLGANGTLYNKYYIPIKIIGIDEPLPQTGLSPSLSSSSSSSSSPSPPTTTSTTPPPPNNNNNSKQIKKNNSISDLTPYLNFNSTDQIYTSFPESMAFDDYMDYEESLVEWKRQVEQNLGIIQLPHSIGRTYPRPKVIHEQLFRKNSEASNDDSISYDIERKLTDSDIKETNSSVNDDGESFSHSPTLRGNNGSSLSVGGGGDNHDNTSNKDNASSQGTNHGVTLNHPNSGINLRERSNSDTSTGSFEGTQLDGSSPMDGSPSTGSLAGFVANGTRSRTNSITYFDQRNQRSNSLSPKHSMLQSRLADSQSLDSSMYGKMGRSGSGFGMDHESWFLQKDPWDSQLILTEPHPDLFSTYEEYEYAMKNWAHEVITKTSILPPHPGQFIQLPKNSELSTDDGSGGGSGGSGVDGVGGNHQLGGSARHMLEMDFEMAKNQSNWTLRPIIRPIITEETMIFNRILSQSNLKHTEYDHLFSIDQELPPSQVWKTLDSDEKLKITETIDRWYRKKLTIQRQTSTWFRGGLWANHFLMPNIQSGWRESVSKKSSILPPLSLKALRRLDINSEADGKRVEHSFPIPELPINFNKLLAPDMNLQYFLGMLEMPTAHSLSSATGGQQQGGSGGGSGGSGSGSGSGSGLNMSGTSGSSGKSEKDKDKETANYIAMHSINNTTNVGTKEDRRQYTKILQTYEQRLQFSFRLDALNSWSEGGYTPMELQEKKLDIEQLVAAPGFDLQNGVWSLVNNSAHFLDKFQETFDQVDLRLYAPAIPMLPAIVPSVFINAGGGSGGGSGGASGGGISTSSGTSPNIVRPGSSSIGGGQPPSSPHIPSGSSLLSSPPNRQGSTGSFSFIGSPGGGGKISPTNSSSLESPRTQSQLAAVVERGSSPRSHSGGSISTHPNTPSVSSNTFLSLINTDSFPELLKFLDLTNEKLALGKISSLVLLVLTSELKGTMVIENILFSKDLQSLYRLARAISFFDAVPLDLFTYPTHLNEMLTPSIFKGSTQEVVRLVFVYYYLGIIQERLNFFSNNVGILGFVNSSRKDAAERIGIQFQNDREFLYKIFKALGRKSILVSNCFLFVLIQLIKMSESPTVQSLLKGELLTHIRDLSASKFSHSRFAAKRLYQILQEDPWKEFLMASYAESIKKNESQHLTDLTTMKEGPKLAIPSISLISELTFNFCVGVLENINSTPIPKPIYKFILNDSIFFQLCNAIVKCKNFTQSTQIVSKVFASLCKVLAKFNLFKNSDSIKSGGKVDPKKQNDVETGVAISPTLLFEIIGFLQNSSLDNNRYCSIIKTNMLIALRQLLKQSEIFDSIKKEGNLYNKFLIPACRDGKNVEFNRNVWRLFFQMIRFHHGHIEYLEKSKYLNALMDIISLNAGNVVLTNALHYLSKLFSLVSYETRKNALRAPGTLSIDTKYSEKDVKSLLNFFVERSCFIKFHMIYKKLTENTEGIQIDQRLLINITTFYRIISFLPSCQKLLKDTLKNPEYKTGIIQVSKMYKPSETF
Protein: Secretory component protein psh3 (Q9Y876)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in amino acid permease processing and required for the efficient translocation of structurally related amino acid permeases from the endoplasmic reticulum to the plasma membrane.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11069779}; Multi-pass membrane protein {ECO:0000269|PubMed:11069779}.
Interaction partners:
- Probable electron transfer flavoprotein subunit alpha, mitochondrial
- Probable electron transfer flavoprotein subunit beta
- Acetyl-CoA acetyltransferase
- Putative acyl-CoA-binding protein
- Probable acetyl-coenzyme A synthetase
- Uncharacterized protein C18G6.12c
- Uncharacterized protein C14C4.04
- Rik1-associated factor 1
- DASH complex subunit spc19
- DASH complex subunit dad3
Sequence:
MAKRSIFRFADEKGLKVAARYGVLMSTSFIFALLFHSSVADVNTLWSPGPESAFDAAETYYTLVAGSHFIVKYTVYTIMGLNMIFHLIQATGAKGDDKLFFYSSTLLYLTALILFIVNVAPSMLVVKLQNYVQFPRNMHLSVLAASHVLVEFLLAGVILIQLGYVFGYHVQSIQQREYAEDMREQELAEKAKLESESATTQSVETVSTESVSKRK
Protein: Cytidyltransferase-like domain-containing protein (Q381Q8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDPLLLGTSAGLERNCTVLFSHLTALCGTKPAGEPHNPLQVHLRVDDGHRDTALQHIKVLYDVAVRHNPRTSVTVVPLAPLEYYETPNRNTNSREGHKLPLFTASLMTPNCGFNPVYKGVAVGGTFDRLHGGHKLLLTTALLHATQVLRIGVTVSTMLTTKIHADLIEPFEVRCAAVTKFAHLLRPDLGLEVAGIADRAGGADSDPSLEALVVSPETVGALPSINTARLSVGLKPLECVLVPYVGVCDDEESRVSSTNIRKRLCELST
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0B4KHL4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Low-density lipoprotein receptor-related protein
- Axin
- Protein smoothened
- Kinesin-like protein costa
- Transcriptional activator cubitus interruptus
- Protein wingless
- Segment polarity protein dishevelled
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- Proteasome inhibitor PI31 subunit
- Frizzled
Sequence:
MQRRERQASGGGPQTTTAGPSAGNVANATTALAGGKSSSNNMYSTRQSVSTTTGVLMVGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKMEPMKSKAPQLHLEYRFYKLLGSHADNAPDGIPRIYHLGTCGGRYNAMVLELLGLSLEDLFNICARKFSLKTVLMIAKQLLHRIEYVHSRHLIYRDVKPENFLIGRTSTKREKIIHIIDFGLAKEYIDLDTNRHIPYREHKSLTGTARYMSINTHMGREQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCDGHPEEFATYLRYVRRLDFFETPDYDFLRRLFQDLFDRKGYTDEGEFDWTGKTMSTPVGSLQTGHEVIISPNKDRHNVTAKTNAKGGVAAWPDVPKPGATLGNLTPADRHGSVQVVSSTNGELNPDDPTAGHSNTPITQQPEVEVVDETKCCCFFKRKKKKSTRQKXLDGVQCSPEREAVTLLRATSHSNSRDSVLNNPSQDYIQQATSQHTLRYPPSASMLTPTPTTNTPTLPL
Protein: MOR2-PAG1_N domain-containing protein (Q5DX48)
Organism: Caenorhabditis elegans
Interaction partners:
- Serine/threonine-protein kinase sax-1
- CP-type G domain-containing protein
Sequence:
MSSIVKKGRLGRRKSDPGTLTVRSTADKIATCELPWGGTRMVTLGPLELTQMSGPFVGQASLMDLFNIFERKLHIVTEEEPLEKMLNKTLQRGGDLYFDNLCHTLHGLSEICLPPILKVLVEWYEKYDESLCLSMLSPIATPELRLKLHKKLLAVNYLFCLVLIEILPQVEFHLPQCDPLIKKVLEICFKNVQYREPSAVGINKTNHLVVAETYGEVVGVLSSTYFTHIHRIFMTHITELKKDVSQTAAQQIVALIMSMKFLRINSSQVEDFENGLKFLDDLGSLLLEVKDKDVKHAVMGLLVEILLPVAAQIKRETNIPALISLVQKLYTTTNDMISKKQHKLAAFPLITCLLCVSQKHFFLANWVQFLNSCLSHLKNKDPQVARVALESLYRLLWVYMIRNNADGNAATRSRLDSICGSLFPKGNRYIVPRDAPLNIFVKIIHFISQQKLDFAFKEIIFDLLCVNNRTQRSLYAERMNVGIRALMVIADGLQQKDDPPAMPKSMGPSASGTVHKTKRKQYITRPLTNEISKSIGIDQFYPQCRKAFDSILRLLDTQIGKPLMMSSIQNRGKEPDELISGDAKPKLDLFRTCIAAIPRLLPDPMSHVDLIDLLTRLTVHLDEELRNMSGITLQTIIGEFPDWREQVFISHISLIQSHIYDFFPQILDDSLRLMLQSLTTWKTAITAEKKREAEKIIPTSPPSCHSSHVTSNSTHSTHISVSFPNTVTSASSILSNSSSPHQPTPSLCSLPESSSLHSIPTAMTSLSTTTTPTHSQGAPSTSTPIGGSGNSTLSVLHQMEGLAIVYLCQTRSNPRAIAVKILKEIQLIYDLLGIEMIDTPVIDVLDQATPYVVKKYIEHVPIKERMSWNMDFSSVCDKISTIETDNTLVNSDRGNEYFQWDPWGCALSGYAEIKHLLTKCPSAVAAAWPILFSRLNAVSGYVDPNNPQNESRSSLLRGSKSKGTSSILGEQLGQEACLALWQKYLIMCCALAPAPYNLSQRSFSPTNSMDGPVDVFRSVSASLRSSRTPVPNSLSQLISKVCMILRWENLTDIRDSVVLGVGSINPLAFDMMLEELKSNGILREATEKKAETNLRRRKRKDLLRLQIIRVIEVAIFRGLLLVHSAGSSDFILHPHVVDFIDSMRVNLESDHDRDITVVTKLRLHFAKLIHLIIDSTPHLSRHTLFSDERRHKLFYLFINWCSRAIAADRKFRDKEVGSYVEQKSVLAMSRILCCGPIFEPAKSIGEDGYLYGWLEKLIISTNPTMQAEVEEMLAWMLELNESGVLLDWLMMQCYTQPPTVACRCFRALVRVFSRRDFPCEFVSLFVLCQSMLAVNSVTDCALHMIEILRKQFLETSNIHATSPAQQVTPIVQMRNQADVLTNIYNGCHILPIEQHDVCTRLANSYPHLTVTIFSEVSYRLETESCSNKSQLLALLQPWISNLELVDQNVVEEAAEGPRGWGSEEATQLVLNNLLYLTVTLSNDHEKELAEESLLPFTKRICVMMSQVVGTRISSILLEWLSTVHDSSKITLDRSEIPPYYRWKDENSERKANEGSIARDSLEREEPTKEGVRLLPMPAYGGHYSPLSQFLPPVVQPVQFFNKSEVGLLLVCDIIRTRCSVDWSESMALLLHFSILRLDSLRPALCRHARQTIINVIMLYMEKNQLALVSSILLKNEMIYGTETSPIIGEIAVGVCRGESPSFARATADEYRKMIFASPSLFSQNDLLSAVVFCMSEEMDTPFWANEDANSRNWRVPSFEQLSCTVHHIVRLLINKMPMIEVIWTQLAMKMALSTSNRHLAGRCFQIVSALEQPPGPWIPSLMSRLVETAGEQHDETQSYVTDLMLCLTDCSPYISPTIMEAIEMRQVISPTHMRSTSYTPAFVRQSVIYSRVQQSDKKNARLSLLVADQESWASKSPDALVRSKSAEQLQSENDVNEETMSRMQILAIAVSMMESGIENEFLLALNLLNKVLDVPTSQKVQCLAKYDKMVGQLEWKNFNGIISLITRGAIIPTAYESSIQAMIQLSDVLSEEVVGGPNGIAIFVTHTLPYLATNFDAPNSLCINVANAIAAFCDESIKTQSGAPADHPFVHLSTIMRQYAMRTFMKDAQQFMKCVLQYICDGCIALNVETLMCLLAEMTERGITGLNGSVLHMLFLLLQHNHHSISPLLINAQVIRSVSRFLQGNNWPDVSKIYKTIVEKWRNENPDQNAHFSLEVTGPTGTSGVVTVKPSEEIGKSEKVSEEKSSEKPSIEVATTSLKRYPPAHMRVRDKLVGILSASGLRIGLPSSVSLVFSRSDLGSATSSTERICASSQEVASTMSLPDPSQSGITDSFPRVFKEFDFLEAEHDSVSETADSCFGWLSTMRPTREKDDERASIRSSLRNLSSGGQGGEEEEEEPEEDEESESHEEEENSESDDLPRKVEDDDLEEEDEDEEERTPCPSECCDDDREDVEMMLRQDIEAYASRGGSVAASSMADDDLRSRLTNNIVSISSQMTEHRHLEEENTSVDGSSVCAYSNASMLASEYYPNRTRSLRIQCSHHLDSRIEREFSMSVNEINESNDCNLLAYGTLLSTQLYKSSCGKVCALLRDASHILTNRAMSRSFASAQETLCNVVDIPFLFVTEQFLRNSPICQRLKFTLNELKEHWETFDERRDQCQKGINSLRSAYKLSALGGSTSSFSLTSELDLGKLLNKLVFQVKLMIDALKDMSDAVKNSTSSQTYSLSPAILEHHRELLMCASDDAASSVNSSLSRLNIDDSISRSQHSCDSLVLLLANKRYTQALQAVRQLRRTYGEEYGCCETVDVDVLLLLFCRSHSLKAWALVGASSEELTRQSELLREANAELASCLRRNAQSLQNMERMTPSMGSASMTESFAQLPSSSDHYD
Protein: Peroniin-1.1a (P86488)
Organism: Litoria peronii (Emerald spotted tree frog) (Hyla peronii)
Function: Induces contraction of intestinal smooth muscle in isolated guinea pig ileum.
Subcellular location: Secreted {ECO:0000269|PubMed:19642086}.
Interaction partners:
Sequence:
DAQEKRQPWLPFG
Protein: L-type lectin-like domain-containing protein C126.08c (O94401)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Golgi apparatus {ECO:0000269|PubMed:16823372}. Vacuole {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Golgi apparatus membrane protein tvp15
- T-complex protein 1 subunit zeta
- Ribosome-associated protein oga1
- Vacuolar protein sorting-associated protein 54
- Ribosome-associated molecular chaperone sks2
Sequence:
MFFSVKNVFLLGIFGFVLGALAETSHLERLSLEAPYINHGMRNLWWEYGGSTVIDRKNGIFLTQDVQNQQGWISTRLPTPSSSFEVLFQFRINSESTSLFGDGLAFFLAAERAKPGPVFGFTDKFNGYGIFIDTYNNHRPGTLFPRVIVMKGDGHTPYDYENDGKANEIASCSALNVRGNDYNLGKLKYDKNAKKLRFEIAYQGSSSFIKCFDLNEVELPLTTFMSFSAHTGDLSESHEIASILSRTITDIDDEGTPEIPAEELKGTTYGQKKGSFKKRLIILLLSLIVIFSIFALRSYQVQQEKNRRTTVL
Protein: E3 ubiquitin-protein ligase UBR1 (EC 2.3.2.27) (N-recognin-1) (Ubiquitin-protein ligase E3-alpha-1) (Ubiquitin-protein ligase E3-alpha-I) (Q8IWV7)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. May be involved in pancreatic homeostasis. Binds leucine and is a negative regulator of the leucine-mTOR signaling pathway, thereby controlling cell growth.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16311597}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 B
- E3 ubiquitin-protein ligase TRIP12
- Ubiquitin-conjugating enzyme E2 A
- E3 ubiquitin-protein ligase UBR5
- ATP-dependent DNA helicase Q4
- E3 ubiquitin-protein ligase UBR4
- E3 ubiquitin-protein ligase MARCHF6
- E3 ubiquitin-protein ligase UBR2
- E3 ubiquitin-protein ligase listerin
- ZZ-type zinc finger-containing protein 3
Sequence:
MADEEAGGTERMEISAELPQTPQRLASWWDQQVDFYTAFLHHLAQLVPEIYFAEMDPDLEKQEESVQMSIFTPLEWYLFGEDPDICLEKLKHSGAFQLCGRVFKSGETTYSCRDCAIDPTCVLCMDCFQDSVHKNHRYKMHTSTGGGFCDCGDTEAWKTGPFCVNHEPGRAGTIKENSRCPLNEEVIVQARKIFPSVIKYVVEMTIWEEEKELPPELQIREKNERYYCVLFNDEHHSYDHVIYSLQRALDCELAEAQLHTTAIDKEGRRAVKAGAYAACQEAKEDIKSHSENVSQHPLHVEVLHSEIMAHQKFALRLGSWMNKIMSYSSDFRQIFCQACLREEPDSENPCLISRLMLWDAKLYKGARKILHELIFSSFFMEMEYKKLFAMEFVKYYKQLQKEYISDDHDRSISITALSVQMFTVPTLARHLIEEQNVISVITETLLEVLPEYLDRNNKFNFQGYSQDKLGRVYAVICDLKYILISKPTIWTERLRMQFLEGFRSFLKILTCMQGMEEIRRQVGQHIEVDPDWEAAIAIQMQLKNILLMFQEWCACDEELLLVAYKECHKAVMRCSTSFISSSKTVVQSCGHSLETKSYRVSEDLVSIHLPLSRTLAGLHVRLSRLGAVSRLHEFVSFEDFQVEVLVEYPLRCLVLVAQVVAEMWRRNGLSLISQVFYYQDVKCREEMYDKDIIMLQIGASLMDPNKFLLLVLQRYELAEAFNKTISTKDQDLIKQYNTLIEEMLQVLIYIVGERYVPGVGNVTKEEVTMREIIHLLCIEPMPHSAIAKNLPENENNETGLENVINKVATFKKPGVSGHGVYELKDESLKDFNMYFYHYSKTQHSKAEHMQKKRRKQENKDEALPPPPPPEFCPAFSKVINLLNCDIMMYILRTVFERAIDTDSNLWTEGMLQMAFHILALGLLEEKQQLQKAPEEEVTFDFYHKASRLGSSAMNIQMLLEKLKGIPQLEGQKDMITWILQMFDTVKRLREKSCLIVATTSGSESIKNDEITHDKEKAERKRKAEAARLHRQKIMAQMSALQKNFIETHKLMYDNTSEMPGKEDSIMEEESTPAVSDYSRIALGPKRGPSVTEKEVLTCILCQEEQEVKIENNAMVLSACVQKSTALTQHRGKPIELSGEALDPLFMDPDLAYGTYTGSCGHVMHAVCWQKYFEAVQLSSQQRIHVDLFDLESGEYLCPLCKSLCNTVIPIIPLQPQKINSENADALAQLLTLARWIQTVLARISGYNIRHAKGENPIPIFFNQGMGDSTLEFHSILSFGVESSIKYSNSIKEMVILFATTIYRIGLKVPPDERDPRVPMLTWSTCAFTIQAIENLLGDEGKPLFGALQNRQHNGLKALMQFAVAQRITCPQVLIQKHLVRLLSVVLPNIKSEDTPCLLSIDLFHVLVGAVLAFPSLYWDDPVDLQPSSVSSSYNHLYLFHLITMAHMLQILLTVDTGLPLAQVQEDSEEAHSASSFFAEISQYTSGSIGCDIPGWYLWVSLKNGITPYLRCAALFFHYLLGVTPPEELHTNSAEGEYSALCSYLSLPTNLFLLFQEYWDTVRPLLQRWCADPALLNCLKQKNTVVRYPRKRNSLIELPDDYSCLLNQASHFRCPRSADDERKHPVLCLFCGAILCSQNICCQEIVNGEEVGACIFHALHCGAGVCIFLKIRECRVVLVEGKARGCAYPAPYLDEYGETDPGLKRGNPLHLSRERYRKLHLVWQQHCIIEEIARSQETNQMLFGFNWQLL
Protein: Ankyrin repeat domain-containing protein 6 (Diversin) (Q9Y2G4)
Organism: Homo sapiens (Human)
Function: Recruits CKI-epsilon to the beta-catenin degradation complex that consists of AXN1 or AXN2 and GSK3-beta and allows efficient phosphorylation of beta-catenin, thereby inhibiting beta-catenin/Tcf signals.
Interaction partners:
- Axin-1
- Segment polarity protein dishevelled homolog DVL-1
- Casein kinase I isoform epsilon
- Glycogen synthase kinase-3 beta
- Prickle-like protein 4
- Prickle-like protein 2
- Prickle planar cell polarity protein 3
- Prickle-like protein 1
- Vang-like protein 2
- Vang-like protein 1
Sequence:
MSQQDAVAALSERLLVAAYKGQTENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQVLRFSRGRSLRKKRERLKEERRAQSVPRDEVAQSKGSVSAGDTPSSEQAVARKEEAREEFLSASPEPRAKDDRRRKSRPKVSAFSDPTPPADQQPGHQKNLHAHNHPKKRNRHRCSSPPPPHEFRAYQLYTLYRGKDGKVMQAPINGCRCEPLINKLENQLEATVEEIKAELGSVQDKMNTKLGQMENKTQHQMRVLDKLMVERLSAERTECLNRLQQHSDTEKHEGEKRQISLVDELKTWCMLKIQNLEQKLSGDSRACRAKSTPSTCESSTGVDQLVVTAGPAAASDSSPPVVRPKEKALNSTATQRLQQELSSSDCTGSRLRNVKVQTALLPMNEAARSDQQAGPCVNRGTQTKKSGKSGPTRHRAQQPAASSTCGQPPPATGSEQTGPHIRDTSQALELTQYFFEAVSTQMEKWYERKIEEARSQANQKAQQDKATLKEHIKSLEEELAKLRTRVQKEN
Protein: Voltage-dependent calcium channel subunit alpha-2/delta-1 (Voltage-gated calcium channel subunit alpha-2/delta-1) [Cleaved into: Voltage-dependent calcium channel subunit alpha-2-1; Voltage-dependent calcium channel subunit delta-1] (P13806)
Organism: Oryctolagus cuniculus (Rabbit)
Function: The alpha-2/delta subunit of voltage-dependent calcium channels regulates calcium current density and activation/inactivation kinetics of the calcium channel. Plays an important role in excitation-contraction coupling.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P54289}.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit beta-1
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent L-type calcium channel subunit alpha-1C
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
- Voltage-dependent L-type calcium channel subunit beta-2
- Voltage-dependent N-type calcium channel subunit alpha-1B
- Voltage-dependent L-type calcium channel subunit beta-3
- Voltage-dependent R-type calcium channel subunit alpha-1E
- Ryanodine receptor 1
Sequence:
MAAGRPLAWTLTLWQAWLILIGPSSEEPFPSAVTIKSWVDKMQEDLVTLAKTASGVHQLVDIYEKYQDLYTVEPNNARQLVEIAARDIEKLLSNRSKALVRLALEAEKVQAAHQWREDFASNEVVYYNAKDDLDPEKNDSEPGSQRIKPVFIDDANFRRQVSYQHAAVHIPTDIYEGSTIVLNELNWTSALDDVFKKNREEDPSLLWQVFGSATGLARYYPASPWVDNSRTPNKIDLYDVRRRPWYIQGAASPKDMLILVDVSGSVSGLTLKLIRTSVSEMLETLSDDDFVNVASFNSNAQDVSCFQHLVQANVRNKKVLKDAVNNITAKGITDYKKGFSFAFEQLLNYNVSRANCNKIIMLFTDGGEERAQEIFAKYNKDKKVRVFTFSVGQHNYDRGPIQWMACENKGYYYEIPSIGAIRINTQEYLDVLGRPMVLAGDKAKQVQWTNVYLDALELGLVITGTLPVFNITGQFENKTNLKNQLILGVMGVDVSLEDIKRLTPRFTLCPNGYYFAIDPNGYVLLHPNLQPKPIGVGIPTINLRKRRPNVQNPKSQEPVTLDFLDAELENDIKVEIRNKMIDGESGEKTFRTLVKSQDERYIDKGNRTYTWTPVNGTDYSSLALVLPTYSFYYIKAKIEETITQARYSETLKPDNFEESGYTFLAPRDYCSDLKPSDNNTEFLLNFNEFIDRKTPNNPSCNTDLINRVLLDAGFTNELVQNYWSKQKNIKGVKARFVVTDGGITRVYPKEAGENWQENPETYEDSFYKRSLDNDNYVFTAPYFNKSGPGAYESGIMVSKAVEIYIQGKLLKPAVVGIKIDVNSWIENFTKTSIRDPCAGPVCDCKRNSDVMDCVILDDGGFLLMANHDDYTNQIGRFFGEIDPSLMRHLVNISVYAFNKSYDYQSVCEPGAAPKQGAGHRSAYVPSIADILQIGWWATAAAWSILQQFLLSLTFPRLLEAADMEDDDFTASMSKQSCITEQTQYFFDNDSKSFSGVLDCGNCSRIFHVEKLMNTNLIFIMVESKGTCPCDTRLLIQAEQTSDGPDPCDMVKQPRYRKGPDVCFDNNVLEDYTDCGGVSGLNPSLWSIIGIQFVLLWLVSGSRHCLL
Protein: Small ribosomal subunit protein uS2 (40S ribosomal protein S2) (40S ribosomal protein SA) (Q8IJD4)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (Probable). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (Probable). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (Probable). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable). Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03015, ECO:0000269|PubMed:24913268}.
Interaction partners:
- Elongation factor 2
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L27a, putative
- Large ribosomal subunit protein uL22
- 60S ribosomal protein L28
- Ribosomal protein L15
- Ubiquitin-60S ribosomal protein L40
- 40S ribosomal protein S25
- 60S ribosomal protein L23
- 60S ribosomal protein L11a, putative
Sequence:
MSNKKGQSPKEESIAKMLICKVHIGTKNLENKMKRYVYTRAKDGVHIINLAKTYEKLQLAARIIVAISNPADVVVVSARPFGSRAVLKFAQYTGAQAIAGRWTPGMLTNQIIQKFTEPRLLIVTDPRTDAQSVKESAYANIPVIALCDSDSPLEHVDIAIPCNNKGKESIALMYWLLAQEVLYLKGVIPRSEPWNVMVDMFLWRDPEQFELKNLANEENTPTAPHLIENQYAAEAPYDEWTKKEEWNDNTNEDWKNPIAAEEW
Protein: GM14473p (Q8MZ49)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYGKSKTSAVPSDAQAREKLALYVYEYLLHVGAQKAAQTFLSEIRWEKNITLGEPPGFLHTWWCVFWDLYCAAPERRDQCDHSSEAKAFHDYGFVSSGYGVNGIGPGGPHNAGGPAPSPLGQMPPGGDGGPMGPGGPMGPNFFPNSTMRPSPPTHASSPQPPPSQMMPGQPPFMGGPRYPGGPRPGVRMQGMGNEFNGPPGQPMMPNSMDPTRPGGGMGPMNPRMNPPRGPGGMGPMGYGGPGGMRGPAPGPGGMPPMGMGGAGGRPPQWQPNASAPLNAYSSSSPGNYGPGSNGPPGPGTPIMPSPQDNTQGGPVGGPGDSMYALMKPEFPMGGGPDGGGGGGGPGGMGPMGGGPNSMGPVLNGGGGPDGSGLDGMKNSPANGGPGTPREDSVSGMGDYNLGGFGGPGENDQTESAAILKIKESMHEEAKRFEKDTDHPDYFMP
Protein: T-cell surface glycoprotein CD5 (Lymphocyte antigen 1) (Ly-1) (Lyt-1) (CD antigen CD5) (P13379)
Organism: Mus musculus (Mouse)
Function: May act as a receptor in regulating T-cell proliferation.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- B-cell differentiation antigen CD72
- B-lymphocyte antigen CD19
- T-cell surface glycoprotein CD8 alpha chain
- T-cell antigen CD7
- T-cell surface glycoprotein CD4
- T-cell surface glycoprotein CD3 epsilon chain
- Leukosialin
- CD27 antigen
- T-cell differentiation antigen CD6
- B-cell linker protein
Sequence:
MDSHEVLLAATYLLGTLAAFCLGQSGRGGLDIQVMLSGSNSKCQGQVEIQMENKWKTVCSSSWRLSQDHSKNAQQASAVCKQLRCGDPLALGPFPSLNRPQNQVFCQGSPWSISNCNNTSSQDQCLPLSLICLEPQRTTPPPTTTPPTTVPEPTAPPRLQLVPGHEGLRCTGVVEFYNGSWGGTILYKAKDRPLGLGNLICKSLQCGSFLTHLSGTEAAGTPAPAELRDPRPLPIRWEAPNGSCVSLQQCFQKTTAQEGGQALTVICSDFQPKVQSRLVGGSSVCEGIAEVRQRSQWEALCDSSAARGRGRWEELCREQQCGDLISFHTVDADKTSPGFLCAQEKLSQCYHLQKKKHCNKRVFVTCQDPNPAGLAPGTVASIILTLVLLVVLLAMCGPLVYKKLVKKFRQKKQRQWIGPTGVNQNMSFHRSHTATVRSQVENPTASHVDNEYSQPPRNSHLSAYPALEGALHRSSTQPDNSSDSDYDLQVAQRL
Protein: Single-stranded DNA-binding protein DdrB (DNA damage response protein B) (Q9RY80)
Organism: Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1)
Function: ssDNA-binding protein that contributes to the ionizing radiation resistance of D.radiodurans. Plays a role in DNA repair and genome reconstitution in a RecA-independent process. Required for recovery from severe genomic fragmentation as a result of exposure to severe levels of ionizing radiation. Binds ssDNA but not dsDNA. Stimulates annealing of complementary ssDNA. Does not complement an ssb disruption.
Interaction partners:
- Single-stranded DNA-binding protein DdrA
- Protein RecA
- DNA damage response protein D
- DNA repair protein PprA
- DNA damage response protein C
- Radiation response metalloprotease IrrE
Sequence:
MLQIEFITDLGARVTVNVEHESRLLDVQRHYGRLGWTSGEIPSGGYQFPIENEADFDWSLIGARKWKSPEGEELVIHRGHAYRRRELEAVDSRKLKLPAAIKYSRGAKVSDPQHVREKADGDIEYVSLAIFRGGKRQERYAVPGGAAGNGQGRPAPQGQPAQARPQATAARPAARPPVQPGQEEETPF
Protein: Sperm-associated antigen 11B (Human epididymis-specific protein 2) (He2) (Protein EP2) (Sperm antigen HE2) (Q08648)
Organism: Homo sapiens (Human)
Function: Has antimicrobial activity against E.coli (By similarity). Plays a role in the defense response in the male reproductive tract, contributing to sperm maturation, storage and protection (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRQRLLPSVTSLLLVALLFPGSSQARHVNHSATEALGELRERAPGQGTNGFQLLRHAVKRDLLPPRTPPYQVHISHREARGPSFRICVDFLGPRWARGCSTGN