wanglab/gogpt-training-data huggingface dataset:
Protein: Afadin, adherens junction formation factor (Q5TIG5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSAGGRDEERRKLADIIHHWNANRLDLFEISQPTEDLEFHGVMRFYFQDKAAGNFATKCIRVSSTATTQDVIETLAEKFRPDMRMLSSPKYSLYEVHVSGERRLDIDEKPLVVQLNWNKDDREGRFVLKNENDAIPPKKAQSNGPEKQEKEGVIQNFKRTLSKKEKKEKKKREKEALRQASDKDDRPFQGEDVENSRLAAEVYKDMPETSFTRTISNPEVVMKRRRQQKLEKRMQEFRSSDGRPDSGGTLRIYADSLKPNIPYKTILLSTTDPADFAVAEALEKYGLEKENPKDYCIARVMLPPGAQHSDEKGAKEIILDDDECPLQIFREWPSDKGILVFQLKRRPPDHIPKKTKKHLEGKTPKGKERADGSGYGSTLPPEKLPYLVELSPGRRNHFAYYNYHTYEDGSDSRDKPKLYRLQLSVTEVGTEKLDDNSIQLFGPGIQPHHCDLTNMDGVVTVTPRSMDAETYVEGQRISETTMLQSGMKVQFGASHVFKFVDPSQDHALAKRSVDGGLMVKGPRHKPGIVQETTFDLGGDIHSGTALPTSKSTTRLDSDRVSSASSTAERGMVKPMIRVEQQPDYRRQESRTQDASGPELILPASIEFRESSEDSFLSAIINYTNSSTVHFKLSPTYVLYMACRYVLSNQYRPDISPTERTHKVIAVVNKMVSMMEGVIQKQKNIAGALAFWMANASELLNFIKQDRDLSRITLDAQDVLAHLVQMAFKYLVHCLQSELNNYMPAFLDDPEENSLQRPKIDDVLHTLTGAMSLLRRCRVNAALTIQLFSQLFHFINMWLFNRLVTDPDSGLCSHYWGAIIRQQLGHIEAWAEKQGLELAADCHLSRIVQATTLLTMDKYAPDDIPNINSTCFKLNSLQLQALLQNYHCAPDEPFIPTDLIENVVTVAENTADELARSDGREVQLEEDPDLQLPFLLPEDGYSCDVVRNIPNGLQEFLDPLCQRGFCRLIPHTRSPGTWTIYFEGADYESHLLRENTELAQPLRKEPEIITVTLKKQNGMGLSIVAAKGAGQDKLGIYVKSVVKGGAADVDGRLAAGDQLLSVDGRSLVGLSQERAAELMTRTSSVVTLEVAKQGAIYHGLATLLNQPSPMMQRISDRRGSGKPRPKSEGFELYNNSTQNGSPESPQLPWAEYSEPKKLPGDDRLMKNRADHRSSPNVANQPPSPGGKSAYASGTTAKITSVSTGNLCTEEQTPPPRPEAYPIPTQTYTREYFTFPASKSQDRMAPPQNQWPNYEEKPHMHTDSNHSSIAIQRVTRSQEELREDKAYQLERHRIEAAMDRKSDSDMWINQSSSLDSSTSSQEHLNHSSKSVTPASTLTKSGPGRWKTPAAIPATPVAVSQPIRTDLPPPPPPPPVHYAGDFDGMSMDLPLPPPPSANQIGLPSAQVAAAERRKREEHQRWYEKEKARLEEERERKRREQERKLGQMRTQSLNPAPFSPLTAQQMKPEKPSTLQRPQETVIRELQPQQQPRTIERRDLQYITVSKEELSSGDSLSPDPWKRDAKEKLEKQQQMHIVDMLSKEIQELQSKPDRSAEESDRLRKLMLEWQFQKRLQESKQKDEDDEEEEDDDVDTMLIMQRLEAERRARQTAMPAISVLDLLQDEERRRQQQLEEMRKREAEDRARQEEERRRQEEERTKRDAEEKVMVL
Protein: Acrosin-binding protein (Acrosin-binding protein, 60 kDa form) (Cancer/testis antigen 23) (CT23) (Cancer/testis antigen OY-TES-1) (Proacrosin-binding protein sp32) [Cleaved into: Acrosin-binding protein, mature form (Acrosin-binding protein, 32 kDa form, mature form)] (Q8NEB7)
Organism: Homo sapiens (Human)
Function: Acrosomal protein that maintains proacrosin (pro-ACR) as an enzymatically inactive zymogen in the acrosome. Involved also in the acrosome formation.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q29016}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q29016, ECO:0000250|UniProtKB:Q3V140}.
Interaction partners:
- Tubulin beta-1 chain
- Trem-like transcript 1 protein
- Platelet glycoprotein IX
Sequence:
MRKPAAGFLPSLLKVLLLPLAPAAAQDSTQASTPGSPLSPTEYERFFALLTPTWKAETTCRLRATHGCRNPTLVQLDQYENHGLVPDGAVCSNLPYASWFESFCQFTHYRCSNHVYYAKRVLCSQPVSILSPNTLKEIEASAEVSPTTMTSPISPHFTVTERQTFQPWPERLSNNVEELLQSSLSLGGQEQAPEHKQEQGVEHRQEPTQEHKQEEGQKQEEQEEEQEEEGKQEEGQGTKEGREAVSQLQTDSEPKFHSESLSSNPSSFAPRVREVESTPMIMENIQELIRSAQEIDEMNEIYDENSYWRNQNPGSLLQLPHTEALLVLCYSIVENTCIITPTAKAWKYMEEEILGFGKSVCDSLGRRHMSTCALCDFCSLKLEQCHSEASLQRQQCDTSHKTPFVSPLLASQSLSIGNQVGSPESGRFYGLDLYGGLHMDFWCARLATKGCEDVRVSGWLQTEFLSFQDGDFPTKICDTDYIQYPNYCSFKSQQCLMRNRNRKVSRMRCLQNETYSALSPGKSEDVVLRWSQEFSTLTLGQFG
Protein: Ankyrin 2 (A0A5F9ZH58)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKELTEELGELEASSDEEAMVTTRVVRRRVIIQGDDMPEIPPETVTEEEYIDEHGHTVVKKDNNE
Protein: Acyl-coenzyme A oxidase 3, peroxisomal (AOX 3) (Acyl-CoA oxidase 3) (EC 1.3.3.6) (Medium-chain acyl-CoA oxidase) (AtCX3) (P0CZ23)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the desaturation of medium-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on C8:0- to C14:0-CoA with a maximal activity on C12:0-CoA.
Subcellular location: Peroxisome {ECO:0000269|PubMed:10918060}.
Interaction partners:
- 3-ketoacyl-CoA thiolase 1, peroxisomal
- Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
- 3-ketoacyl-CoA thiolase 2, peroxisomal
- 3-ketoacyl-CoA thiolase 5, peroxisomal
- Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
- Probable enoyl-CoA hydratase 1, peroxisomal
- Probable acyl-CoA dehydrogenase IBR3
- Acetyl-CoA acetyltransferase 2
- Acetyl-CoA acetyltransferase 1
- Peroxisomal acyl-coenzyme A oxidase 1
Sequence:
MSDNRALRRAHVLANHILQSNPPSSNPSLSRELCLQYSPPELNESYGFDVKEMRKLLDGHNVVDRDWIYGLMMQSNLFNRKERGGKIFVSPDYNQTMEQQREITMKRIWYLLENGVFKGWLTETGPEAELRKLALLEVCGIYDHSVSIKVGVHFFLWGNAVKFFGTKRHHEKWLKNTEDYVVKGCFAMTELGHGSNVRGIETVTTYDPKTEEFVINTPCESAQKYWIGGAANHATHTIVFSQLHINGTNQGVHAFIAQIRDQDGSICPNIRIADCGHKIGLNGVDNGRIWFDNLRIPRENLLNAVADVSSDGKYVSSIKDPDQRFGAFMAPLTSGRVTIASSAIYSAKVGLSIAIRYSLSRRAFSVTANGPEVLLLDYPSHQRRLLPLLAKTYAMSFAANELKMIYVKRTPETNKAIHVVSSGFKAVLTWHNMHTLQECREAVGGQGVKTENLVGQLKGEFDVQTTFEGDNNVLMQQVSKALFAEYVSCKKRNKPFKGLGLEHMNSPRPVLPTQLTSSTLRCSQFQTNVFCLRERDLLEQFTSEVAQLQGRGESREFSFLLSHQLAEDLGKAFTEKAILQTILDAEAKLPTGSVKDVLGLVRSMYALISLEEDPSLLRYGYLSQDNVGDVRREVSKLCGELRPHALALVTSFGIPDSFLSPIAFNWVEANAWSSV
Protein: DNA repair helicase, putative (Q38BP4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
- BRCT domain-containing protein
- DNA repair and transcription factor protein, putative
- General transcription factor IIH subunit 4
- [RNA-polymerase]-subunit kinase
- Chromosome transmission fidelity protein 18 homolog
- TATA box-binding protein-like 1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- RNA polymerase-like protein
Sequence:
MYAAGRFTVPFPFEPYPLQLHAMEAIREGLSAGDVVVLESPTGTGKTQILLNGVLSHMFEPVVTSVEHGIAESHEVTGESRPTGEVCADSGDGCPSFEEHRKHQRKRRKREREKRRKETFNFGGTSSSRDPFLVDQDVREEAQELSRCGALADCLSSSSSSRSSSVSHLGGEGDKSDEDVEVQPLRKPKVYFSSRTHTQLQQVTDELRRTVFCQNLVRRRSCNSVEKDGLASKVFEDAHKSPFVEPRKLRYVHVAGRQQLCLNASLKAAAGGSNERLNELCLEAMAYEYSKEGKTARKQKLQRGCADSSLPDIEDSLGSSTVSRRGCGYCQKEKLKILRDYVNIEPRDLSQMRELGQRVGACPFLVTREVLRGADVVFIPYSYLVSSEMRNALLAGNATNEHPTDLTPQTQVVSQGLSSTCRAGSTSTHSSYPTVPSKQRWEIQNGRRVPILPPDFSGDVIVVDEAHNLVDYCRNVTTAEVTLPELQVIRRLLDGYRLRYEKRLLTRNKQRLREMVAFVDKLAQHLQEAGKKSTPTATASTFINFTFDAEVDTVNVHLFLSFLDESRLLPKLHGLLAQMVAQVEAQISQPSGKTTKWRPTSSYSDENICSDTTNEYADPIEALLHSPAEDRRSIAATLYRFETFLRWYGLSDEYTRVILRRLPSENGSREMCRVTLELLQLELGTHTMFPVLQQAHAAVLAGGTMKPLALTCDLLLKQSAPTKELSVLKNISSLPCGTREEEAGEQAKKIRFTEEGHVVPPSSIAVFTLATGPGGQRLEFQHARRQSWPKIFEGVGTALLNFCRVIPAGMIVFFTSYEIEELFVNTIRSSGMYDTINAVKRIFREPGSARNASSTPGYSSGCQAAASTTVDSMLEEYASWIRSERSSGALLFAVIGGKLSEGINFNDDLGRAVVVVGLPYANISEVDLQLHLRHVADTRVRTLLPSSANIATGSITTDSTDQVTVVPDGEFPASPSSAMEWGLLTDLCMRSVNQSIGRCIRHASDYAAVILLDARYVERRDIRRRIPSWMQPSIHVAQNFGDCFRRVRDFFIERRK
Protein: Abnormal spindle-like microcephaly-associated protein ASH domain-containing protein (Q38AM8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell projection, cilium, flagellum {ECO:0000256|ARBA:ARBA00004230}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSFEPDGREQRKRTLGVDCVGRLLWRHWEPGGEYTQRLRIRNLDMKKQTIVYRLPLRKTVFIMDFPDPVTLSSGMATDIKVSFRPTELVDICDMFEVTVVGRGSFFVKLEGKIPTARVEVPPHHDFGYVPTATTAREIVAMKNVGTTTVSYEWEVPAPFGITPTSGELRENETVDLCITFTPSEACVLIAQAVCKMAACGSLLSTIKISGVAKYPFIRVSKEPSTVTGSTTPDDSCLSGREMQLLQDGRSLLLDFGTVYVGKVHTMEFDVENPSVVDAVFSLEVEREDFSCPFTAAPRTGVIPRGKAQKFKVTFAATSVGAAFSDKLCVKALAGNTVTLLLRGVVVAPTVVASVTSMNFGDIRMEKNIVVYEHRRALRRSFYIKNLSDVSVNFYVLGVSPGASFVVTPTTGELPAKGTQRMWVEFCPTYPMNYLRRLHIIMNLTRHVVFVDLFGSAYDDSIRPMSFGLKEVEEFFWRHEVGLGASEPQDLFLLSKVLRGGKVPDTLMHLLSTSSLAMLRDLHRDPTTSSELVTGGCRKKSGGRISFARWNSSFSTGAPFVLSTEALVFVDSRNEPQYVNVYNRSNTVATAYWCLPADCSFSVTPMQEDILPHSYCTFTVTRSRAAGTSLRDQHLECYVNYKQMQSFLLIEEGSFTPPHYFTVHCQQIIQCSDAEAGSIVSCVGAPKHIVFPKCLVDGTTHTVIELENRGGVIVSFAVALRLESQESKGKDCGSDAISGHGSNSVFGCNPVYGIIPARSRVPLMLSFSAKGAAWMRGEMLVQLSNSPKDELRIVLHGEGFRPELLVEDSSMITMRPACVTGVTERSLRITNPTTVPISFESSPSQPLQGVVFVEPPVGVLQAGMGMNLVVSFCPQDPVLYEGHITFSISTHDETQPSSNATRRAVDPLVGRERESQSSSCNNTPRELSLSDGKRIISCPFMGEGRQSVVEVEPVVIEHEGPAAQEKTFEWTIYNSSVCEVCYEVRWLTKTRRMNWEGEDTPMIHLSNNRCGALAARSHTVVLVTLRPPAGVTDCILYTLVGGRGVDLSSIACPTNLHEVQQHPHCEVRLKGTRPAVQITDVRSLQQHRSQLWCQLAINSINNVLAAPVQSVDVERDSFAFPQYVQGVEPIYMDVGVGCVDDDDKEIMLCVENAGSCAAPFRFWYPIDHEGGNETWFVEDEELEDVQQILSNRLLEISPREGTIPVNSHAVITITYRHVSVGTHCLPVLLRLDKGKKALLVLEGRTVADNTHALAFHHPPVYQLHPIALGDVEPPLQSSTIENTSSHPMTYVVQEDLVEQVCAANCGVPVFQCMNPEGVIPPGGSTQLHWYFRPLEVRTYTIDVGLQIVNGEGYSMRFCGVGYHPKKTSTGEACNTINDAFLPIPVSPSLRLPSRLCPVSLSIDVMRIGAVPRFSLHRRICYVENRHNSFSYSFSWATSLEPGSSTISVSPNSGVVRPGQRVRCVLALQCGKLSQIIEAPIFCRVVNETLIEDKSVSPMYVEAAAAPEDEEADEEDDTDPLLDVKPQTKTRFERSTCTKRRATYMGKKRPSVIEAPPEYQSLRVLSAAAAPALHSGVADHNTMSLPLKKRADEGPVLAHSLEVLVQARIMPVDEYQRLYGECAVRQVYFPPLYENYVRPQSASLVGDRLKQTIKDFTRGNVRIVRRMLEGLLRTVVDCPPVRNAFTETIKEEIPQYRELVSMASNSFVRDPPSSTYGANKSSDPGSGAAGATEAMPPTTGVTQRLTTTAGTPCKDQGVLPPWNNSALLNLVEKLLNDVAVRTITQDMGAGLLGRRS
Protein: ATP-dependent RNA helicase glh-1 (EC 3.6.4.13) (Germline helicase 1) (P34689)
Organism: Caenorhabditis elegans
Function: Probable ATP-binding RNA helicase. May act redundantly with the P-granule component glh-4 to regulate the formation of the granular structure of P-granules in embryos. Plays a role in positively regulating the localization of pgl-1 to P-granules. May play a role in transgenerational epigenetic inheritance. May protect somatic cells from excessive apoptosis during normal development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17699606, ECO:0000269|PubMed:21402787}. Cytoplasmic granule {ECO:0000269|PubMed:17699606}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17699606}. Note=Perinuclear localization in germ cells but disperses into particles in cellularized oocytes. Component of P granules. {ECO:0000269|PubMed:17699606}.
Interaction partners:
- Guanyl-specific ribonuclease pgl-1
- Guanyl-specific ribonuclease pgl-3
- Argonaute protein wago-1
- Piwi-like protein 1
- P-granule-associated protein deps-1
- Protein LSM14 homolog car-1
- Uncharacterized protein
- Female germline-specific tumor suppressor gld-1
- Endoribonuclease dcr-1
- COP9 signalosome complex subunit 5
Sequence:
MSDGWSDSESAAKAKTGFGSGGGFGGGNNGGSGFGGGKNGGTGFGGGNTGGSGFGGGNTGGSGFGGGKTGGSGFGGGNTCGSGFGGGSTGGSPYGGASSGFGGSTATSGFGSGEKSSAFGGSGGFGGSATGFGSGGGSFGGGNSGFGEGGHGGGERNNNCFNCQQPGHRSSDCPEPRKEREPRVCYNCQQPGHTSRECTEERKPREGRTGGFGGGAGFGNNGGNDGFGGDGGFGGGEERGPMKCFNCKGEGHRSAECPEPPRGCFNCGEQGHRSNECPNPAKPREGVEGEGPKATYVPVEDNMEDVFNMQKISEGLMFNKFFDAEVKLTSSEKTVGIKPCKTFAEANLTETMQKNVAHAGYSKTTPIQQYALPLVHQGYDIMACAQTGSGKTAAFLLPIMTRLIDDNNLNTAGEGGCYPRCIILTPTRELADQIYNEGRKFAYQTMMEIKPVYGGLAVGYNKGQIEKGATIIVGTVGRIKHFCEEGTIKLDKCRFFVLDEADRMIDAMGFGTDIETIVNYDSMPRKENRQTLMFSATFPDSVQEAARAFLRENYVMIAIDKIGAANKCVLQEFERCERSEKKDKLLELLGIDIDSYTTEKSAEVYTKKTMVFVSQRAMADTLASILSSAQVPAITIHGAREQRERSEALRQFRNGSKPVLIATAVAERGLDIKGVDHVINYDMPDNIDDYIHRIGRTGRVGNSGRATSFISEDCSLLSELVGVLADAQQIVPDWMQGAAGGNYGASGFGSSVPTQVPQDEEGW
Protein: ORMDL sphingolipid biosynthesis regulator 2 (F8VXD5)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVLLSIPFFSIPVVWTLTNVIHNLATYVFLHTVKGTPFETPDQGKARLLTHWEQMDYGLQFTSSRKFLSISPIVLYLLASFYTKYDAAHFLINTASLLSVLLPKLPQFHGVRVFGINKY
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A3KFJ0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
Sequence:
MDRSKENCISGPVKATAPVGGPKRVLVTQQFPCQNPLPVNSGQAQRVLCPSNSSQRIPLQAQKLVSSHKPVQNQKQKQLQATSVPHPVSRPLNNTQKSKQPLPSAPENNPEEELASKQKNEESKKRQWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVRRN
Protein: Putative uncharacterized protein KIF25-AS1 (KIF25 antisense RNA 1) (KIF25 antisense gene protein 1) (Protein HGC6.1) (Q9Y6Z4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGDIFKNNGVLQGRLRAVACAPHCFGPRLRCLHHDQGLTELAWGTWPHSHPVRHQPQMPSARECCSIVCMAAKEVSAPKAPGSPWMVPGDVAMSGHRVGALDERGHPNPQTGHCRGGSVSVTWSSVSCCRGRLAAVRVMIARDPSTCHLAKGCSPAWGFLPQARGPAGTRTPQRRCSSHEA
Protein: PAR domain protein 1-gamma (PAR-domain protein 1, isoform F) (Q9TVQ4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSEPKENIMDLSVRGKSTSNSKEIICPDDKYKEEGDIWNVEAQTAFLGPNLWDKTLPYDADLKVTQYADLDEFLSENNIPDGLPGTHLGHSSGLGHRSDSLGHAAGLSLGLGHITTKRERSPSPSDCISPDTLNPPSPAESTFSFASSGRDFDPRTRAFSDEELKPQPMIKKSRKQFVPDELKDDKYWARRRKNNIAAKRSRDARRQKENQIAMRARYLEKENATLHQEVEQLKQENMDLRARLSKFQDV
Protein: LYR motif-containing protein 1 (Q9CQB7)
Organism: Mus musculus (Mouse)
Function: May promote cell proliferation and inhibition of apoptosis of preadipocytes.
Interaction partners:
- Electron transfer flavoprotein regulatory factor 1
- LYR motif-containing protein 2
- Succinate dehydrogenase assembly factor 3, mitochondrial
- LYR motif-containing protein 9
- LYR motif-containing protein 4
- Complex III assembly factor LYRM7
Sequence:
MTAATRQEVLCLYRSIFRLARKWQAASGQMEDTIEEKQYILKEARTLFQKNKNLTDPELIKQCIVECTARIEIGLHYQIPYPRPIHLPPMGLTARRGRGLQTQEKLRKLSKPVYLKSHDEVS
Protein: C2HC/C3H-type domain-containing protein (Q388N7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLSSRSKGPAPRPQMRVCYLCGQQFGSASIGIHIPQCYAKKVAQWEVADPATRGKRPKHPDTVNWQGSGVSAEKLMDEQFQEFTNNLVPCDRCGRKFLPDRLPVHLRGCKGDSRCPSASANRSRAGSTRSLASSGRGASPSRDSQRGGQGKRTASMGPGAKPQLPICYLCGQQFGTSSIGIHVPQCYAKKLAQWEAADVETRGKPPKHPDSFNWKGEGCGNVEEHNDAQFAEFVRNLEPCPNCGRKFLADRLVVHLRSCKPGSTARPPPAPSAPQSRPPTGKVPQPNTGSHVGGATDTAERSQSRGSAIGTDHNRRLSNINPKLKRLPKGGTVDADGRECPRCSAVEYDKNAKYCRECGANLASKNLAKPCAQCGESIPQGSRFCGTCGVPVNGASADERGEGAENVNAPTVRVLTCPACRAICDADSNFCDNCGGALGDAEPLAVGGARTPAKTTKEVMYCKGCGETVEELSAKYCEECGEVLERKTIEDVSEGPPAAECTLTPHGVKEVSAPQRALSTAPPSTTNDDKRHSAGGFRQANTKIGGSEDNRGGPKVPSRGRGNLSPSSPKKCTQESYTATDYEAAEVGERLECQKCGRKFAPEALQRHERVCASQKQRKVFNMRAQRLAGTEAMSFAKKIDTTASAPAPPKKDWRAESEAFRRSLKEARMVDKVLKSGGNLRNLPPPTYSENSHYTPCPHCGRKFAPDVAERHIPRCANTVNKPKAPPRRRF
Protein: Peptidyl-prolyl cis-trans isomerase FKBP4 (PPIase FKBP4) (EC 5.2.1.8) (52 kDa FK506-binding protein) (52 kDa FKBP) (FKBP-52) (59 kDa immunophilin) (p59) (FK506-binding protein 4) (FKBP-4) (FKBP59) (HSP-binding immunophilin) (HBI) (Immunophilin FKBP52) (Rotamase) [Cleaved into: Peptidyl-prolyl cis-trans isomerase FKBP4, N-terminally processed] (P27124)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Immunophilin protein with PPIase and co-chaperone activities. Component of steroid receptors heterocomplexes through interaction with heat-shock protein 90 (HSP90). May play a role in the intracellular trafficking of heterooligomeric forms of steroid hormone receptors between cytoplasm and nuclear compartments. The isomerase activity controls neuronal growth cones via regulation of TRPC1 channel opening. Acts also as a regulator of microtubule dynamics by inhibiting MAPT/TAU ability to promote microtubule assembly. May have a protective role against oxidative stress in mitochondria (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Mitochondrion {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Shuttles from mitochondria to nucleus; co-localizes in mitochondria with the glucocorticoid receptor. {ECO:0000250}.
Interaction partners:
- peptidylprolyl isomerase
- Glucocorticoid receptor
- Progesterone receptor
- Prostaglandin E synthase 3
- Mineralocorticoid receptor
- Adenylosuccinate lyase
- Stress-induced-phosphoprotein 1
- Androgen receptor
- Serine/threonine-protein kinase mTOR
- Heat shock protein HSP 90-alpha
Sequence:
MTAEEMKAAESGAQSAPLPLEGVDISPKQDEGVLKVIKREGTGTETPMIGDRVFVHYTGWLLDGTKFDSSLDRKDKFSFDLGKGEVIKAWDIAVATMKVGELCRITCKPEYAYGSAGSPPKIPPNATLVFEVELFEFKGEDLTDDEDGGIIRRIRTRGEGYARPNDGAIVEVALEGYYKDRLFDQRELRFEVGEGESLDLPCGLEKAIQRMEKGEHSILYLKPSYAFGNAGKEKFQIPPYAELKYEVHLKSFEKAKESWEMSSEEKLEQSAIVKERGTVYFKEGKYKQALLQYKKIVSWLEYESSFSSEEVQKAQALRLASHLNLAMCHLKLQAFSAAVESCNKALELDSNNEKGLFRRGEAHLAVNDFDLARADFQKVLQLYPSNKAAKAQLAVCQQRIRKQIAREKKLYANMFERLAEEENKAKAEVAAGDHPMDTEMKDERNDVAGSQSQVETEA
Protein: Zinc finger and SCAN domain-containing protein 23 (Zinc finger protein 390) (Zinc finger protein 453) (Q3MJ62)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00187}.
Interaction partners:
- Zinc finger and SCAN domain-containing protein 32
- Zinc finger and SCAN domain-containing protein 20
- Zinc finger and SCAN domain-containing protein 21
Sequence:
MAITLTLQTAEMQEGLLAVKVKEEEEEHSCGPESGLSRNNPHTREIFRRRFRQFCYQESPGPREALQRLQELCHQWLRPEMHTKEQILELLVLEQFLTILPEELQAWVRQHRPVSGEEAVTVLEDLERELDDPGEQVLSHAHEQEEFVKEKATPGAAQESSNDQFQTLEEQLGYNLREVCPVQEIDGKAGTWNVELAPKREISQEVKSLIQVLGKQNGNITQIPEYGDTCDREGRLEKQRVSSSVERPYICSECGKSFTQNSILIEHQRTHTGEKPYECDECGRAFSQRSGLFQHQRLHTGEKRYQCSVCGKAFSQNAGLFHHLRIHTGEKPYQCNQCNKSFSRRSVLIKHQRIHTGERPYECEECGKNFIYHCNLIQHRKVHPVAESS
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (EC 3.1.4.11) (Phosphoinositide phospholipase C-beta-3) (Phospholipase C-beta-3) (PLC-beta-3) (P51432)
Organism: Mus musculus (Mouse)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q99JE6}. Membrane {ECO:0000250|UniProtKB:Q99JE6}. Nucleus {ECO:0000269|PubMed:9714794}. Note=And particulate fractions. {ECO:0000250|UniProtKB:Q99JE6}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Guanine nucleotide-binding protein subunit alpha-14
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Guanine nucleotide-binding protein subunit alpha-15
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Protein kinase C delta type
- Calcium/calmodulin-dependent protein kinase type II subunit gamma
Sequence:
MAGARPGVHALQLEPPTVVETLRRGSKFIKWDEEASSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDTRLEEKLMTVVAGPDPVNTTFLNFMAVQDDTVKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLNFNRSESIRPDEFPLEIFERFLNKLCLRPDIDKILLEIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRSSQARLLIEKYETNKQFLERDQMSMEGFSRYLGGEENGILPLEALDLSMDMTQPLSAYFINSSHNTYLTAGQLAGPSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAEAAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIDPLDKYPLSAGIPLPSPQDLMGRILVKNKKRHRPSTGVPDSSVRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKTSLEPQKSLGEESLSREPNVPMPDRDREDEEEDEEEEETTDPKKPTTDEGTASSEVNATEEMSTLVNYVEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDLPMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIVDGIVANALRVKVISGQFLSDKKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYTEASDYIPDDHQDYAEALINPIKHVSLMDQRAKQLAALIGESEAQASTETYQETPCQQPGSQLPSNPTPNPLDASPRWPPGPTTSSTSSSLSSPGQRDDLIASILSEVTPTPLEELRSHKAMVKLRSRQDRDLRELHKKHQRKAVALTRRLLDGLAQARAEGKCRPSPSALGKATNSEDVKEEEEAKQYREFQNRQVQSLLELREAQADVETKRKLEHLRQAHQRLKEVVLDTHTTQFKRLKELNEREKKELQKILDRKRNNSISEAKTREKHKKEVELTEINRRHITESVNSIRRLEEAQKQRHERLVAGQQQVLQQLEEEEPKLLAQLTQECQEQRERLPQEIRRCLLGETAEGLGDGPLVACASNGHAPGSGGHLSSADSESQEENTQL
Protein: Glyceraldehyde-3-phosphate dehydrogenase, testis-specific (EC 1.2.1.12) (Spermatogenic cell-specific glyceraldehyde 3-phosphate dehydrogenase 2) (GAPDH-2) (Spermatogenic glyceraldehyde-3-phosphate dehydrogenase) (Q64467)
Organism: Mus musculus (Mouse)
Function: May play an important role in regulating the switch between different pathways for energy production during spermiogenesis and in the spermatozoon. Required for sperm motility and male fertility.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Triosephosphate isomerase
- Phosphoglycerate kinase 2
- Phosphoglycerate kinase 1
- Fructose-bisphosphate aldolase A
- Fructose-bisphosphate aldolase
- Fructose-bisphosphate aldolase
- Fructose-bisphosphate aldolase C
- Fructose-bisphosphate aldolase B
- Bisphosphoglycerate mutase
- GDH/6PGL endoplasmic bifunctional protein
Sequence:
MSRRDVVLTNVTVVQLRRDRCPCPCPCPCPCPCPVIRPPPPKLEDPPPTVEEQPPPPPPPPPPPPPPPPPPPPQIEPDKFEEAPPPPPPPPPPPPPPPPPLQKPARELTVGINGFGRIGRLVLRVCMEKGIRVVAVNDPFIDPEYMVYMFKYDSTHGRYKGNVEHKNGQLVVDNLEINTYQCKDPKEIPWSSIGNPYVVECTGVYLSIEAASAHISSGARRVVVTAPSPDAPMFVMGVNEKDYNPGSMTIVSNASCTTNCLAPLAKVIHENFGIVEGLMTTVHSYTATQKTVDGPSKKDWRGGRGAHQNIIPSSTGAAKAVGKVIPELKGKLTGMAFRVPTPNVSVVDLTCRLAKPASYSAITEAVKAAAKGPLAGILAYTEDQVVSTDFNGNPHSSIFDAKAGIALNDNFVKLVAWYDNEYGYSNRVVDLLRYMFSREK
Protein: 5-formyltetrahydrofolate cyclo-ligase (EC 6.3.3.2) (5,10-methenyl-tetrahydrofolate synthetase) (MTHFS) (Methenyl-THF synthetase) (P40099)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Only enzyme known to utilize 5-formyltetrahydrofolate (folinic acid) as substrate. Contributes to tetrahydrofolate metabolism in an alternative way of folate biosynthesis. May regulate carbon flow through the folate-dependent one-carbon metabolic network that supplies carbon for the biosynthesis of purines, thymidine and amino acids.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14576278}.
Interaction partners:
- C-1-tetrahydrofolate synthase, cytoplasmic
- Methylenetetrahydrofolate dehydrogenase [NAD
- C-1-tetrahydrofolate synthase, mitochondrial
- Phosphoribosylglycinamide formyltransferase
- Serine hydroxymethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Sideroflexin FSF1
- Altered inheritance of mitochondria protein 9, mitochondrial
- GTP cyclohydrolase 1
- Folic acid synthesis protein FOL1
Sequence:
MATKQLLRRQIKRVINALDYDIIAAESHTISQAVRSLIASANSRRVACYMSMDKGEVTTGEIIKNLFQDGQEVFLPRCTHTSESKHFKLREDHHPHLIFHRMSSLKMVRDLKPQGPYQLKEPEPHIEESDILDVVLVPGVAFDIKTGARMGHGAGYYDDFFQRYKILHEGQKPLLVGLCLMEQVASPIPLEKHDYSMDCIVCGDGSIHWFQ