wanglab/gogpt-training-data huggingface dataset:
Protein: Heat shock 70 kDa protein 6, chloroplastic (Chloroplast heat shock protein 70-1) (cpHsc70-1) (Heat shock protein 70-6) (AtHsp70-6) (Q9STW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts redundantly with HSP70-7 in the thermotolerance of germinating seeds. Plays an important role in the protein precursor import into chloroplasts.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18997426, ECO:0000269|PubMed:20506024}.
Interaction partners:
- 20 kDa chaperonin, chloroplastic
- Heat shock protein 90-5, chloroplastic
- Chaperonin 60 subunit alpha 1, chloroplastic
- Chaperone protein ClpC1, chloroplastic
- GrpE protein homolog
- AT4g39960/T5J17_130
- Chaperone protein ClpB3, chloroplastic
- Chaperonin 60 subunit beta 1, chloroplastic
- Heat shock 70 kDa protein 17
- Chaperonin 60 subunit beta 2, chloroplastic
Sequence:
MASSAAQIHVLGGIGFASSSSSKRNLNGKGGTFMPRSAFFGTRTGPFSTPTSAFLRMGTRNGGGASRYAVGPVRVVNEKVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKSGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMNEVDEESKQVSYRVVRDENNNVKLECPAINKQFAAEEISAQVLRKLVDDASRFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGLEVLRIINEPTAASLAYGFDRKANETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRVVDWLAAEFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTNMSLPFITATADGPKHIETTLTRAKFEELCSDLLDRVRTPVENSLRDAKLSFKDIDEVILVGGSTRIPAVQELVRKVTGKEPNVTVNPDEVVALGAAVQAGVLAGDVSDIVLLDVTPLSIGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSVSAVDKGTGKKQDITITGASTLPKDEVDQMVQEAERFAKDDKEKRDAIDTKNQADSVVYQTEKQLKELGEKIPGEVKEKVEAKLQELKDKIGSGSTQEIKDAMAALNQEVMQIGQSLYNQPGAGGPGAGPSPGGEGASSGDSSSSKGGDGDDVIDADFTDSQ
Protein: Prolyl 3-hydroxylase 2 (C9JSL4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEMQQNIENYRATAGVEALQLVDREAKPHMESYNAGVKHYEADDFEMAIRHFEQALREYFVEDTECRTLCEGPQRFEEYEYLGYKAGLYEAIADHYMQVLVCQHECVRELATRPGRLSPIENFLPLHYDYLQFA
Protein: Cypemycin cysteine dehydrogenase (decarboxylating) (EC 1.3.99.36) (E5KIB9)
Organism: Streptomyces sp
Function: Involved in the biosynthesis of the lanaridin cypemycin.
Interaction partners:
Sequence:
MNVEKFEGAELHVHVTGSISAALVPWWIHWLREFQPELVVNVSVTPAASRFLAVRALRHLANGKVWVDSWDDPDVPPEVNSGKSGASECFLVFPATLDTVMRLAQGRADSPALMMLQLTDAPLVIADTFPGSNEIVENNVQTLKLRPNVEFAPRVNGVRASNRQTAEVGFNLPGALAAANRMRKEGRSGE
Protein: Iron-sulfur cluster insertion protein ErpA (P0ACC3)
Organism: Escherichia coli (strain K12)
Function: Probably involved in the insertion of Fe-S clusters into apoproteins in vivo including IspG and/or IspH. Essential for growth under aerobic conditions and for anaerobic respiration but not for fermentation. In vitro it binds Fe-S clusters and transfers them to apo-IspG, which is involved in quinone biosynthesis among many other cell components. Experiments indicate that it is probably also involved in the insertion of other Fe-S clusters than IspG/IspH.
Interaction partners:
- Fe/S biogenesis protein NfuA
- Iron-sulfur cluster assembly scaffold protein IscU
- HTH-type transcriptional regulator IscR
- Iron-sulfur cluster assembly protein SufB
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- Cold shock protein CspA
- Glutaredoxin 4
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- 2Fe-2S ferredoxin
- Iron-sulfur cluster assembly protein SufD
Sequence:
MSDDVALPLEFTDAAANKVKSLIADEDNPNLKLRVYITGGGCSGFQYGFTFDDQVNEGDMTIEKQGVGLVVDPMSLQYLVGGSVDYTEGLEGSRFIVTNPNAKSTCGCGSSFSI
Protein: T. brucei spp.-specific protein (Q38EJ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLPLIFYFWFDIILPVFLFFSFLFFFFFCSVRTVACHEFYLTRKAHDILLLCYCHICFCFACVSICVCVCVFFICFSSTGSIFLVYHFYYYCYYYYYCYNNFSLFFVVLLLLFCMALNEKDLYIYIYKRNDVTRDEFVGGASQLVATCNYNKNSKE
Protein: Purine permease (P48777)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Able to transport with low efficiency all natural purines as well as purine analogs.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein
- Got1 family protein
- Cytoplasmic tRNA 2-thiolation protein 2
- allantoinase
- Dihydroorotate dehydrogenase
- Uricase
Sequence:
MDGPDQIGPDVRPRRTFGDRVRRAARAFTTRDGLIGDYDYGFLFTPRLPFVKQKRRAAPFFGLEDKIPLVLALLLGLQHALAMLAGVITPPILLAGSSGANFGADESQYLVSTSLIVSGLLSAVQMFRLHVYKTRYYVGTGLVSVVGTSFATITVATGTFNQMYSTGYCPVDGSGNRLPCPKGYGALLATSCLCSLLEIGLSFMSSRLLKALFPPIVTGPTVFLIGASLIGNAMKDWAGGSGTCSSNPGNGALCPSADAPHPLPWGSAEFIGLGFLVFATIILCERFGSPIMKSCAVIVGLLVGCIVAAACGYFDRSGIDAAPVASFIWVKTFPLTIYAPLILPLLAVYMVIMMESIGDITATCDVSRLQVEGATFDSRIQGGVLGNGITCLLAGLCTITPMSVFAQNNGVIALTRCANRKAGYCCCFFLVVMGIFAKFAAALVAIPSSVLGGMTTFLFSSVAISGVRIMCSVDWTRRNRFILTASFAVGMAATLVPDWFSYFFTYSGDNHALEGLLQAVELVMANGFAVTGFLGLLLNLILPEDMEEDVVESEEDYEATTVVGMQGGSEPGSSGQNVKA
Protein: Serpentine Receptor, class T (Q9GYI7)
Organism: Caenorhabditis elegans
Interaction partners:
- SUMO-activating enzyme subunit uba-2
- Ran GTPase-activating protein 2
- Small ubiquitin-related modifier
- Transcellular chaperone signaling
- E3 SUMO-protein ligase gei-17
- SUMO-activating enzyme subunit aos-1
- Tar DNA-binding protein homolog 1
- Exportin-T
- GILT-like protein F37H8.5
- RRM domain-containing protein
Sequence:
MSEETLDFSGSMPEEVQTLLTNSEMDPGLLSNETATTMITDVISTTTTTLAPVLIGYQPNPFRIGLLAFKCLLIILIFTLSCTIRKDFFKFFVLFLIIPLFIEAGFDIFTEIHASTAIFGAQQFDWQYLNLSPRANDTVTDWQKYAVDGFGEILQKYTTYQVYTKDQLFSIVSYVAGDFIFWSLLFSTYTVFFFAHKAIARPEQITYEPIGSVFFKAQITPVIFTAFDTLISIYQIPQWAYLSIISSIRLTACIVSFGIVTQMFASLFLFCRRKDEVTKTSPYEHVRNSKLRLFLFLLFSICVHVLTAPYLIWSGLTIAFDVGQLLGFNWYLPMHFASEMFPLHLTFFLLRPFIFLILALILLNPYRRRFVKFFFPCCRRH
Protein: Polyadenylate-binding protein 1 (H0YBN4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDES
Protein: Major capsid protein (P17499)
Organism: Autographa californica nuclear polyhedrosis virus (AcMNPV)
Function: Most abundant structural protein of the nucleocapsid produced during the infection cycle. The monomers are arranged in stacked rings around the nucleoprotein core.
Subcellular location: Virion {ECO:0000269|PubMed:25142609}.
Interaction partners:
Sequence:
MALVPVGMAPRQMRVNRCIFASIVSFDACITYKSPCSPDAYHDDGWFICNNHLIKRFKMSKMVLPIFDEDDNQFKMTIARHLVGNKERGIKRILIPSATNYQDVFNLNSMMQAEQLIFHLIYNNENAVNTICDNLKYTEGFTSNTQRVIHSVYATTKSILDTTNPNTFCSRVSRDELRFFDVTNARALRGGAGDQLFNNYSGFLQNLIRRAVAPEYLQIDTEELRFRNCATCIIDETGLVASVPDGPELYNPIRSSDIMRSQPNRLQIRNVLKFEGDTRELDRTLSGYEEYPTYVPLFLGYQIINSENNFLRNDFIPRANPNATLGGGAVAGPAPGVAGEAGGGIAV
Protein: Tyrosine-protein phosphatase non-receptor type 12 (EC 3.1.3.48) (G3V7Q4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR000932}.
Interaction partners:
- SHC-transforming protein 1
- Proline-serine-threonine phosphatase-interacting protein 1
- Leupaxin
- Focal adhesion kinase 1
- Growth factor receptor-bound protein 2
- Breast cancer anti-estrogen resistance protein 1
- Protein-tyrosine kinase 2-beta
- Paxillin
- Transforming growth factor beta-1-induced transcript 1 protein
Sequence:
MEQVEILRRFIQRVQAMKSPDHNGEDNFARDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPRAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQLYEIHGAQKITDGNEISTGNMVSSIDSEKQDSPPPKPPRTRSCLVEGDAKEEILQPPEPHPVPPILTPSPPSAFPTVTTVWQDSDRYHPKPVLHMASPEQPPTDLNRNYDKSADLMGRSESAVEHTDKKLEQNLSFEIKKVPLQEGPKSFDGNTLLNRGHAIKIKSASSSVVDKSSKPQELSSGDLKVHDVSQNSCADCSASHLDNAPESSEESQNSHTPPRPDCLPLDKKGHVTWSLHGPENATPVSDSPDNHSQTLKTVSSTPNSTAEEESHDLTEHHNSSPLPRAPLSFTNPLHSDDSDSDEGNSDGAVTKNKTSISTASATVSPASSTESACTRRVLPMSIARQEMAGRRHSGAEKDADVSEESPPPLPERTPESFVLADMPIRSDWHELPSQECSEHRESEGLITSGNDKHDAGVSHTAACSPTFSDKKEEITESLTEVTDIGFGNRCGKPKGPRDPPSEWT
Protein: Uncharacterized protein (Q382F2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus envelope {ECO:0000256|ARBA:ARBA00004259}.
Interaction partners:
- WD repeat protein mio zinc-ribbon like domain-containing protein
- Uncharacterized protein
- Nuclear pore protein
- Nucleoporin
- Nuclear pore complex protein
- Vacuolar membrane-associated protein Iml1 N-terminal domain-containing protein
- Nucleoporin
- Nucleoporin NSP1-like C-terminal domain-containing protein
- Protein transport protein Sec13, putative
- Protein transport protein sec13, putative
Sequence:
MYSCKTAHTTFVHHMAVNSSGTLLASGSSDKGVNVFYRPPSEVVTGSWSLCCVLKDHVATVTRVAWCQHREHGSMLATVGADRWIYVYKINVTTQDGKVVGNAVRYSPVRGYEKDVITDVAFVPPRQHQVLLLSTASLDGWVRLYDIQPLQFLCKYTVTQESDICRPLGTRSGGITSTAWFPSSVDETMTLAVGCMNGCFYLYKFCKERNQFKRVYNALPQRIESTIHHIVWAPPVGRCFQLLSLCCRSSVYIVRLNCVSPSVEDYQCEVFVWPHGAVCTAWSHSATLLYLIDDDNPPRVTVLQARDLTDHQSWEKLLSKPTE
Protein: 5-hydroxytryptamine receptor 1D (5-HT-1D) (5-HT1D) (Serotonin 1D alpha receptor) (5-HT-1D-alpha) (Serotonin receptor 1D) (P28221)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for ergot alkaloid derivatives, various anxiolytic and antidepressant drugs and other psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling inhibits adenylate cyclase activity. Regulates the release of 5-hydroxytryptamine in the brain, and thereby affects neural activity. May also play a role in regulating the release of other neurotransmitters. May play a role in vasoconstriction.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10452531, ECO:0000269|PubMed:1565658, ECO:0000269|PubMed:1652050}; Multi-pass membrane protein {ECO:0000269|PubMed:10452531, ECO:0000269|PubMed:1565658, ECO:0000269|PubMed:1652050}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 1B
- Guanine nucleotide-binding protein G
- Sodium-dependent serotonin transporter
- Guanine nucleotide-binding protein G
- Tryptophan 5-hydroxylase 1
- 5-hydroxytryptamine receptor 3A
- Amine oxidase [flavin-containing] B
- Guanine nucleotide-binding protein G
Sequence:
MSPLNQSAEGLPQEASNRSLNATETSEAWDPRTLQALKISLAVVLSVITLATVLSNAFVLTTILLTRKLHTPANYLIGSLATTDLLVSILVMPISIAYTITHTWNFGQILCDIWLSSDITCCTASILHLCVIALDRYWAITDALEYSKRRTAGHAATMIAIVWAISICISIPPLFWRQAKAQEEMSDCLVNTSQISYTIYSTCGAFYIPSVLLIILYGRIYRAARNRILNPPSLYGKRFTTAHLITGSAGSSLCSLNSSLHEGHSHSAGSPLFFNHVKIKLADSALERKRISAARERKATKILGIILGAFIICWLPFFVVSLVLPICRDSCWIHPALFDFFTWLGYLNSLINPIIYTVFNEEFRQAFQKIVPFRKAS
Protein: 1,4-alpha-glucan-branching enzyme (EC 2.4.1.18) (Glycogen-branching enzyme) (Q6FJV0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P32775}. Note=Localizes to glycogen granules in the cytoplasm. {ECO:0000250|UniProtKB:P32775}.
Interaction partners:
- glycogenin glucosyltransferase
- Alpha-1,4 glucan phosphorylase
- Glycogen [starch] synthase
- Glycogen [starch] synthase
- Glycogen debranching enzyme
- ornithine carbamoyltransferase
- glucan 1,4-alpha-glucosidase
- ATP synthase subunit beta
- phosphoglucomutase
- GDP-Man:Man
Sequence:
MSLTKIPENVQGAVSIDPWLEPFADVLSERRYLADKWLYDIKHATPDGSEQSLVDFARNAYKTYGLHANQQTKEIVYREWAPNAQRAFLVGEFNNWNEESHEMKHKDEFGVFSITLAPLENGDFAIPHDSKIKVMFVLPDGSKVYRIPAWITRATQPSKETAQKYGPTYEGRFWNPPNSYQFKHQRPKFNLANDSIKIYEAHIGISSPEPKVASYKEFTQNVLPRIKHLGYDAIQLMAIMEHAYYASFGYQVTNFFAISSRYGTPEDLKELIDTAHSMGILVLLDVIHSHASKNSEDGLNMFDGSDHQYFHSLTSGRGEHPLWDSRLFNYGSFEVQRFLLANLAYYIDVYQFDGFRFDGVTSMLYLHHGVGAGGAFSGDYNEYLSRDRSGVDHEALAYLMLANDLVHDLLPESAVTIAEDVSGYPTLCLPRTAGGGGFDYRLAMALPDMWIKLLKTKQDDDWDMGHIVHTLTNRRHGEKVVAYCESHDQALVGDKTLAFWLMDAAMYTDMTVLKEPTLVIDRGIALHKMIRLITHSLGGEAYLNFEGNEFGHPEWLDFPRVGNNDSYHYARRQFNLVDDDLLRYRHLNEFDAAMQNCESKHQWLNTPQAYVSLKHEVDKVIAFERNGHLFVFNFHPTQSFTDYRIGVDVAGTYKIVLNTDRAEFGGHNRIDEAQEFFTTDLEWNNRRNFIQVYIPSRTAIVLTRQM
Protein: SD09402p (Q8T3I6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSVIIRLQNLPWTANARDIRNFFSGLSIPEGGVHIIGGEMGDAFIAFSTDEDARCAMLKDREKLMEIQVRLLLSSRAEMQKVIETARKAASAQAPVAVPVPMPVVVPVTAAKVAGPAAPLPPIIGGLNTFLGQGQVKGVATGTVPSFLTYQQQAGITLSDVTGRRSRSRSSSSDDSDRERERDRQRERERGRKRRSDRLDKSQERELKMVAGGGALPSPWAQPPQNQLPAVGLGLNMGLNLNLPQIPSLQSYTTSTNTTNVTNNYNLEPSATSVQLLTALQQVSSGSAAPAQPSKSESEPIAFASVNPYAQMYPQLFQQQQMLLQQQQTQAKVSPTMGGSPGGGSTPQVVADTCYIRMSGMCQNTSYSDIRKYFQGMYIPHNGIKIMMVNGSRTGVAYVEFSRVSSAQKAVQRNNTMFRDRLIQIVPVGDDEFEMAEERASRQGQDGSRSHGNHNGGDRGERGGGAPVPVPRPVTNVLYIEDLPQTTTEQDIMKMFSASYTVVDILLSPSPKNRRESVAFVLFAREAEADSALQDTSKHYIGFRQLRVRSSSEEDMQNAKEKQRRANEQLLKEEADQREELLKDQQRRQKQQQENENIQANRFAADPRRRQAEDQQQQQQMNMGPNFNSNMSPNMMAPFVNGGNMPFHMPPLQQNGVNNFPFNMNNNYNYNGNSNGNGPNYPNDNGGAGVIQRPRQEDVFVRVHNCEYATRANDLGELFSLEQLRIEHIEQLFNERNQSSGEFIVEFSDPASCKLAIREFHNRRFRGRGLRVVAITPQEIADRMKKPFMDYLPGGNGPRKAETNNANDGAGGNKASAQPSRRRGPSRFDKPQEQPSQQQDRPLSLEREDNSSTSSNAPVKQHFNPFARPDPPLSSSSLSPSNQGQVKPTSPVPVPTSIIPDKFNRPGCVVAMRNVPFKAELKDIMRFFSDYKLSPDDIIRRFNDEGKPTGDTRVAFESPSEARSAFESRRKKQIFNRTVYLDII
Protein: CUB domain-containing protein (SOL-2 protein) (Q9XUU2)
Organism: Caenorhabditis elegans
Interaction partners:
- Suppressor of lurcher protein 1
- CUB domain-containing protein
- STarGazin
- STarGazin
- Glutamate receptor 1
- Lipoma HMGIC fusion partner-like 3 protein
- Glutamate receptor 2
- Protein cornichon homolog 1
- Protein lev-9
Sequence:
MIEYLLFIIINVITLITCSYCPIKHIHSSTPTTGFIESPGYPSAFSAPLDCIFNITTAASNVIQLSFVSFDLASKNQLSDQCLDSYLLVVVVDRHGRQHVGERLCGNQVPLSINTMQSWMQVQFVTTSTNQKHRGFRIQYRILSEAAIQEPSSTLGESMFSGCGGHSTPGQLSGEILSPGYPTTYPKNSTCNWLIRVEARQRIYIRIVHLHLAPTIAECERASLTIIDGYKHEKYGIDRKESTSETSEAKFCGSQLYYAEEGMKSYLSSANRIVVRFITQEGPPSSMIGEERIGFKVVWTAVEGLIGEGDESVNGNSCKDQFMCHGGQVCVEQGHGICASRSRLCIHSSLVCDGIHNCVEGDFSDEQHCYSREIITSAALGFSLIVLTMLVLVCCDQFRKRRRLRVMIRERRAASENGKCKNMNNNSITTRIQPNR
Protein: SSD domain-containing protein (P91129)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Neurotransmitter-gated ion-channel ligand-binding domain-containing protein
- Epimerase domain-containing protein
- F-box domain-containing protein
Sequence:
MAWDCVERRAASLFRQLGFLICDHPLPFFVFPLLFTAAMGVGLLHLNPLSDAVYLFTPLGAQSKMERMSIHEKWPLTDNNYIPGRAVTQSREIQVTALARNDSNILDPKFANAVYQLDKYIQTRVRVLHNGHYYSYKNLCLQYKNGGCPSNKHVHILSDLHNHGFNITYPYFRFGSEGGYIGSSLGGVTVMKGENETDILASAKAWFMIYHLKFHPEEMSYISGEWELELGRMLTQYPEDPYISITYFHSQTLADELKRNADTLIPRFIISITLLIVFSTLCSLSFIDGSFSIDWVLSKPILSILGVVSAGIAILTGVGFLSLMGMPYNDIVGVMPFLVLAVGVDNMFLMVAAVRRTSRTHTVHERMGECLADAAVSILITSSTDVLSFGVGAITTIPAVQIFCVYTGVAIFFAFIYQITFFAACLALAMKHEASGRNSLFLIEAVSAEKKTSLSTFQRLFNLGSVPDHSASHDVKQPLTSRFFGEWYAPVLMHPVVRGIAMVWFVIYLLGASYGCSRIKEGLEPVNLLVEDSYAIPHYRLLEKYFWKYGQQVQIVINNAPDLRNHTSRDRVHAMVLDFATSKHAIGMESVQFWLFEMERYYQKELEVQIIDSSFYGLLHHFLASKTNNPLAEDIYWGPMPDDDNGTMVKSFRFILGMKDLVTTMDQTDATMSFREVAARWPEFNVTTFMPIWMFTDQYIIIIPNTVQNIIIALLVMIVIAVLFIPQPMCSLWVALACASIDFGVIGYMTLWGVNLDAISMITIIMSIGFSVDYSAHIAYGYVVSREDTAAGRVKEALSALGWPLSQGAMSTIIAVSVLADIPAYMIVTFFKTVVLSISLGLLHGLVFLPVLLSIFVRGCCIIPSSPHGHPSAQKIEKQIRIAAISSSPLDLRTVAPLRASSPISFPHRLEYTDESPTVHNRSKNSIKSEHLD
Protein: Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (eIF-3 p48) (E5RHS5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03004}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03004}. Nucleus, PML body {ECO:0000256|HAMAP-Rule:MF_03004}.
Interaction partners:
Sequence:
MAEYDLTTRIAHFLDRHLVFPLLEFLSVKEVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKETIDNNSVSSPLQSLQQRTWLIHWSLFVFFNHPKGRDNIIDLFLYQPQYLNAIQTMCPHILRYLTTAVITNKDVRKRRQVLKDLVKVIQQESYTYKDPITEFVECLYVNFDFDGAQKKLRECESVLVNDFFLVACLEDFIENARLFIFETFCRIHQCISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY
Protein: Uncharacterized oxidoreductase C16H5.14c (EC 1.-.-.-) (Q1MTR7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLNHILLLVISLVCAALTLSWFPLLFRKQSYSCAKGLIVITGGSGILGHAIIQEALDRGFSVASLDSTEPASFLQYNSKFSALKCNITKDKDVEGCVHSLKKMNRTPFALINAAAIAPKNHLLSISRQELQKCFETNVIGQLAITSALFPLLLQDPNPHVVNIASSLAYFSAMGVGAYSSSKAALVSLHETLEEEVLSQHPNFKFSLYVLGQIKSTMFEKDTPNRVLAPLLEPQNLAKIIIQNLYTNKSGRFYYPFYARFMPLLRFFPLPIQKLARLFSGMDKIYS
Protein: Centriolar coiled coil protein 110kDa, isoform F (M9PI43)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDATCRAMEQLLSAVEMGGSHSEATTPTATTTISIWSAPSEGSGSSSMDPVSFRFHLDGQPILPPLMTSAKKREVQLARQMAEALEKRYRLARHSAGSDMASRRSVSQLQQTETLIYDSTRGQARPQTLVFGKQLPTIQVDPPTPQPFVKSIENTSPRRHNRITDRILQFEQSGLGKLLPKVPDKCILRTSPAVAEDQQDQDTKDTTARELGSPLAEPANFQRSRSFTLEEPSQVLVEHMEREALAVKPSQSLANFEKQTIESQAKRVNRSARSISSKISHNSYNSNSSAATKSTIATKTTTAGSSCSRRDREVERIIERALDEHGALEASRKAGVRNYLRGHRERMNQLVIHQEKERRRMQAEFDHQQRQLIEELCAEIDVSSATENPDSLISQSTSTGDLQRFSPSPTLPSFSEDIEDFPTMEDKCQIAGPSSARKRLFSPKPSKDSEPQLLSAPSTPRSLPLRNSSLTNSRRSVQVVRRRSQSVGGSLVKTITAADREVKKSPAKPGGGAGRPKSSPGKNSSIIAKRGSAPPKSASPTKRLGNRKKP
Protein: GH08772p (Q86P90)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLPPPSPTPSHKSLGGWRGSLGGGATPPVPPIATSSANQMNNRPLPDPPRSEGGGSSRSGTPKSVFDTIQRPPSVQLEKIKSKASATLDRMAIPQQRYRQQKARQDLSANSEQAAGAQRRQMSTSVFNLNSNPRRPLSEAQNGGAWLANQRIQQAQSLAQLNCAGCQQSQQHPGWAQHPHQALPQHQHPDQWSQFGSQQQFNNSNLSLNVGPGYMSQQHHPHYPPPVFMTQRGMMPNVYPGAPGYPMMHPGVMGMPPSAASRAASRSRYAASPTPSRKSMSLRRKRNSYVDDELTDDEDSDQDDRRSLVSNRSGMTSASRSQHHQNHIQPRQRRLSSASQLIASDELDGDQVHHKMRNRRGSIAKSVQSEWLPERRENEGTLTRNKTATDSARTSRIYSDLESEGSGARALVQAKIQQKLQEADQHKSSKKAEPKRKPEMKDENTQAAAVVQKVVVPPAHEESASEYEEVVEEVTASESEAEAQTAPDPQEVPDEIGADDLGPPPSTPDHEWECEFCTFVNEPNIKICSICCKTPSKPPVQPNKAKKVEEKPQPPAEKSNNIKASSKTETKPVQKPTTKSQQPSQKSVAAFSKTTHTNSTSSSKASPAVNSKTTSSIPIKTPSKSTLKTSSENESDNSLAKSLLHKGRIQKRISFFEGTKT
Protein: Beta-fructofuranosidase precursor suc1-Aspergillus niger (EC 3.2.1.26) (Beta-fructofuranosidase suc1-Aspergillus niger) (A2QSK6)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MKLQTASVLLGSAAAASPSMQTRASVVIDYNVAPPNLSTLPNGSLFETWRPRAHVLPPNGQIGDPCLHYTDPSTGLFHVGFLHDGSGISSATTDDLATYKDLNQGNQVIVPGGINDPVAVFDGSVIPSGINGLPTLLYTSVSFLPIHWSIPYTRGSETQSLAVSSDGGSNFTKLDQGPVIPGPPFAYNVTAFRDPYVFQNPTLDSLLHSKNNTWYTVISGGLHGKGPAQFLYRQYDPDFQYWEFLGQWWHEPTNSTWGNGTWAGRWAFNFETGNVFSLDEYGYNPHGQIFSTIGTEGSDQPVVPQLTSIHDMLWVSGNVSRNGSVSFTPNMAGFLDWGFSSYAAAGKVLPSTSLPSTKSGAPDRFISYVWLSGDLFEQAEGFPTNQQNWTGTLLLPRELRVLYIPNVVDNALARESGASWQVVSSDSSAGTVELQTLGISIARETKAALLSGTSFTESDRTLNSSGVVPFKRSPSEKFFVLSAQLSFPASARGSGLKSGFQILSSELESTTVYYQFSNESIIVDRSNTSAAARTTDGIDSSAEAGKLRLFDVLNGGEQAIETLDLTLVVDNSVLEIYANGRFALSTWVR
Protein: Angiogenin (EC 3.1.27.-) (Ribonuclease 5) (RNase 5) (P03950)
Organism: Homo sapiens (Human)
Function: Ribonuclease that cleaves tRNA within anticodon loops to produce tRNA-derived stress-induced fragments (tiRNAs) which inhibit protein synthesis and triggers the assembly of stress granules (SGs). Binds to actin on the surface of endothelial cells; once bound, angiogenin is endocytosed and translocated to the nucleus. Stimulates ribosomal RNA synthesis including that containing the initiation site sequences of 45S rRNA. Angiogenin induces vascularization of normal and malignant tissues. Angiogenic activity is regulated by interaction with RNH1 in vivo.
Subcellular location: Secreted {ECO:0000269|PubMed:23047679, ECO:0000269|PubMed:29748193, ECO:0000269|PubMed:3663649}. Nucleus {ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:15735021, ECO:0000269|PubMed:23047679, ECO:0000269|PubMed:23843625, ECO:0000269|PubMed:25372031, ECO:0000269|PubMed:29100074, ECO:0000269|PubMed:8127865}. Nucleus, nucleolus {ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:7945327}. Cytoplasm, Stress granule {ECO:0000269|PubMed:23843625, ECO:0000269|PubMed:27518564, ECO:0000269|PubMed:29100074}. Note=The secreted protein is rapidly endocytosed by target cells following interaction with PLXNB2 receptor and translocated to the cytoplasm and nucleus (PubMed:29100074). In the nucleus, accumulates in the nucleolus and binds to DNA (PubMed:12051708). {ECO:0000269|PubMed:12051708, ECO:0000269|PubMed:29100074}.
Interaction partners:
- Ribonuclease inhibitor
- Ribonuclease 4
- Non-secretory ribonuclease
- Ribonuclease 8
- Eosinophil cationic protein
- Ribonuclease T2
- Plexin-B2
- Interleukin-8
- 2-5A-dependent ribonuclease
- Follistatin
Sequence:
MVMGLGVLLLVFVLGLGLTPPTLAQDNSRYTHFLTQHYDAKPQGRDDRYCESIMRRRGLTSPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFRRP
Protein: WD repeat-containing protein 46 (Q19873)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:22240150}.
Interaction partners:
- rRNA biogenesis protein RRP5
- Periodic tryptophan protein 2 homolog
- Nucleolar protein 14
- U3 small nucleolar RNA-associated protein 13 C-terminal domain-containing protein
- WD_REPEATS_REGION domain-containing protein
- Nucleolar protein 6
- HEAT repeat-containing protein 1 homolog
- WD_REPEATS_REGION domain-containing protein
- KRR1 small subunit processome component
- Small-subunit processome Utp12 domain-containing protein
Sequence:
MPPIKRSKPDGGVKKISITATDVTPAKGVEEKMSWKEYKKMKQHTGGGTRNKLKKKQRPPTENTEGRAKKPKVLTKEQLERHDTGADQIDPSSMRSKLQQEKMKVTKDKFQRRIEATAKAEKRLVENTGFVAPDEEDHSLTYSIRQKDIAESVDLAAATKHFELKLPRFGPYHIDYTDNGRHLVIGGRKGHLAALDWQTKHLHFEQSVMEKVSDVKFLHTENFIAVAQKNYTYVYDNLGTELHCLKTMYDTARLEFLPHHFLLVGSSRNSFLNYVDVSVGKQVASFATKSGTLDVMCQNPANAIIHTGHTNGTVSLWSPNSKEPLVKILTHLSAVKGIAVDDQGNYMATTGLDRKCRIWDVRMFRQLHAYSLPFGVSNVAISQKMNVACAVGNHVQVFRGMHNGTCKEPYLVHNCGGVVTDLRFVPWEDVLGIGHAGGFTSMLVPGAGDPNVDTLRSNPYETKSQRKEREIKQLLDKIQPELISLNPDDINKVNEGLLELEEEERKKILYIRPMAVQYTPRHKMRSKKSGWKMEARKNIVKDQIRMERNMEKHAVEKEVFEAPEVDDEAPKKKHILDRLK
Protein: LD45152p (Splicing factor 3b subunit 2, isoform A) (Splicing factor 3b subunit 2, isoform B) (Q9VQK7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Splicing factor 3B subunit 4
- Splicing factor 3A subunit 1
- Splicing factor 3B subunit 1
- Splicing factor 3B subunit 3
- PHD finger-like domain-containing protein 5A
- LD21442p
- Splicing factor 3B subunit 5
- Splicing factor 3A subunit 2
- Splicing factor 3B subunit 6
- Pre-mRNA-splicing factor syf1 homolog
Sequence:
MADQLNNEPGQPTPLMSIRFDQQQHESAAANGNENGNGNANGDGDASEDAVDAEKTPGELVLPKALEDVLALKDQRAAEFTVDADSQGGSGGATQDGDEADVGEDSEEDADNQVNGSASQKTGKQSKAERNKKKKKRKKQNRKIRHQIEFARQQQLAQAEENEPEAKDSETKAHGSEDEQVAEKEKKDKRKESRSKRRKDRSDEKDTDKKAGEANDENVTIEYVPEKITIADLAPMYRQFYRVFEIFKLENKPKPVEKDKSSHDSESHPRDKKATDKQLEDEDDDGDDDEERKEDKEKLSKRKLKKLTRLSVAELKQLVSRPDVVEMHDVTARDPKLLVQLKAYRNTVQVPRHWCFKRKYLQGKRGIEKPPFDLPAFIKKTGIMEMRESLQEREDAKTLKAKMRERVRPKMGKIDIDYQKLHDAFFKWQTKPRMTIHGDLYYEGKEFETRLKEKKPGDLSEELRIALGMPVGPNSHKIPPPWLIAQQRYGPPPSYPNLKIPGLNAPIPDGTSFGYHAGGWGKPPVDENGKPLYGDVFGTNILDLDNGVDEADIERNQWGELESESEESSEEEEEDGEDLGDQQDETGLVTPVEGLVTPSGLTSVPAGMETPENIELRKKKIEAEMEDNETPVLYQVLPEKRTDRIGASMMGSTHVYDVSGSGANKQPPVRSTTDREGIVELALDPSELDLDNDAMAQRYEQQMREQQNHLQKEDLSDMLAEHVARQKSKRKRQQTDPAKTTKKYKEFKF
Protein: Zinc finger protein kipf (Protein kipferl) (Q8T053)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:36193674}. Chromosome {ECO:0000269|PubMed:36193674}. Note=Localization along chromosomes matches that of rhi/rhino. {ECO:0000269|PubMed:36193674}.
Interaction partners:
- LD17911p
- GEO02462p1
Sequence:
MMHSAKNVCRTCMDETGTLVDIFANVRDPVLDEPEMSLSHILARCTERPVKRGDLLPQFICVSCVLAVQNAFRFKWQSEQSYQHFFRVLNQSGAPENQVHLAACNGDKNQIINQKMQLKSDRQQDTQQMTKTQKPDDDLSQKQTLQAKLQEGNIDGPPESFTLHPRKRTCRTEEQADMIPKEATRSTKMICDADGYYNCPHCSKRFCSQTQLRTHITDLCNRCPYCPRTYMQKSNLKRHLRNHLSKPAHKCFHCSKAFMRKDHLKRHLRTHDSDGPLSCSQCSAVFIEHVQLEIHRREHKQRPGSSKSESTKDPDSDDSDQAQDLKPKWTKNTFNGTCSIPPMLKPKPICDICQKKFSSVYALKRHMLTHNRQHHLKKCTYCSEEFKTEKHLKRHERGHMGDLFRCEFCSLVFVDVNYLRKHKKRIHSNNVIAM