wanglab/gogpt-training-data huggingface dataset:
Protein: Increased recombination centers protein 22 (P40006)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Is probably involved in a pathway contributing to genomic integrity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Single-pass type I membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Putative uncharacterized protein YNL266W
- Peptidyl-tRNA hydrolase 2
Sequence:
MRFSMLIGFNLLTALSSFCAAISANNSDNVEHEQEVAEAVAPPSINIEVKYDVVGKESENHDSFLEFYAEDTATLAYNVTNWEDTNITIFGVNGTIVTYPHGYPVADITGASIGPYEMEVNGTSKFGQDVTLNLPEGQYFLIPFLLASRFDEIVRIAAPPTLFEIVSPPISFFNPQFLSVQVIFLAIIGGVSYYYMKSKTNQRPSKKSATVKKVDESWLPETYKK
Protein: DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) (PEP) (Plastid-encoded RNA polymerase subunit beta) (RNA polymerase subunit beta) (P50546)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- DNA-directed RNA polymerase subunit beta''
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit alpha
- Large ribosomal subunit protein uL2cz/uL2cy
- Small ribosomal subunit protein uS14c
- Small ribosomal subunit protein uS14m
- ATP synthase subunit b, chloroplastic
- Large ribosomal subunit protein bL20c
- Photosystem I assembly protein Ycf3
- Photosystem II CP47 reaction center protein
Sequence:
MLGDEKEGTSAIPGFNQIQFEGFYRFIDQGLIEELAKFPKIEDIDHEIEFQLFVETYQLVEPLIKERDAVYESLTYSSELYVSAGLIWKTSRNMQEQRIFIGNIPLMNSLGTSIVNGIYRIVINQILQSPGIYYQSELDHNGISVYTGTIISDWGGRLELEIDKKARIWARVSRKQKISILVLSSAMGLNLREILENVCYPEIFLSFLTDKEKKKIGSKENAILEFYQQFSCVGGDPIFSESLCKELQKKFFHQRCELGRIGRRNINWRLNLNIPQNNIFLLPRDVLAAADHLIGMKFGMGTLDDMNHLKNKRIRSVADLLQDQLGLALARLENVVKGTISGAIRHKLIPTPQNLVTSTPLTTTYESFFGLHPLSQVLDRTNPLTQIVHGRKLSYLGPGGLTGRTANFRIRDIHPSHYGRICPIDTSEGINVGLIGSLSIHARIGDWGSLESPFYELFEKSKKARIRMLFLSPSQDEYYMIAAGNSLALNRGIQEEQAVPARYRQEFLTIAWEEVHLRSIFPFQYFSIGASLIPFIEHNDANRALMSSNMQRQAVPLSRSEKCIVGTGLERQVALDSGVPAIAEHEGKILYTDTEKIVFSGNGDTLSIPLIMYQRSNKNTCMHQKPQVRRGKCIKKGQILADGAATVGGELALGKNILVAYMPWEGYNFEDAVLISECLVYGDIYTSFHIRKYEIQTHVTTQGPERITKEIPHLEGRLLRNLDKNGIVMLGSWVETGDILVGKLTPQVAKESSYAPEDRLLRAILGIQVSTSKETCLKLPIGGRGRVIDVRWVQKKGGSSYNPEIIRVYISQKREIKVGDKVAGRHGNKGIISKILPRQDMPYLQDGRPVDMVFNPLGVPSRMNVGQIFECSLGLAGSLLDRHYRIAPFDERYEQEASRKLVFSELYEASKQTANPWVFEPEYPGKSRIFDGRTGDPFEQPVIIGKPYILKLIHQVDDKIHGRSSGHYALVTQQPLRGRSKQGGQRVGEMEVWALEGFGVAHILQEMLTYKSDHIRARQEVLGTTIIGGTIPKPEDAPESFRLLVRELRSLALELNHFLVSEKNFQINRKEV
Protein: V-type proton ATPase subunit C (V-ATPase subunit C) (Vacuolar H(+)-ATPase subunit C) (Vacuolar proton pump subunit C) (Q9SDS7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17151019}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase subunit D
- V-type proton ATPase subunit H
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit F
- V-type proton ATPase subunit c''1
- V-type proton ATPase subunit B1
- V-type proton ATPase subunit d2
- V-type proton ATPase subunit e1
- V-type proton ATPase subunit B2
- V-type proton ATPase subunit a1
Sequence:
MTSRYWVVSLPVKDSASSLWNRLQEQISKHSFDTPVYRFNIPNLRVGTLDSLLALGDDLLKSNSFVEGVSQKIRRQIEELERISGVESNALTVDGVPVDSYLTRFVWDEAKYPTMSPLKEVVDNIQSQVAKIEDDLKVRVAEYNNIRGQLNAINRKQSGSLAVRDLSNLVKPEDIVESEHLVTLLAVVPKYSQKDWLACYETLTDYVVPRSSKKLFEDNEYALYTVTLFTRVADNFRIAAREKGFQVRDFEQSVEAQETRKQELAKLVQDQESLRSSLLQWCYTSYGEVFSSWMHFCAVRTFAESIMRYGLPPAFLACVLSPAVKSEKKVRSILERLCDSTNSLYWKSEEDAGAMAGLAGDSETHPYVSFTINLA
Protein: A-band associated protein (Q24205)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
SSPKKKEKKEKSPSPKLTLKLEIGGGQKASKKMFEQQQQQAKPPPKKSKMVLQMEEQAKAAAKAAEEAAARAKPKGETFEERQKRLQAEKEEQERLEAEQRAQEEAEAEAEAEAEEDEEDPSNVGEEGEEGTEAGYGDEDQEQEYPEDEIEAEPEEDTKKKEKRRGSDSSDDFVRPDPHEEERWQRIAAVEGEEFMQQMRKYSQAKRISEKERDADWQRRREQARNPKFINFLSDRAVEAGQSVRLACAVDGPELSVKWYHNRKQLERDGCHRIINNNNILVLEVLNTTILDSGEYSCVISNQNDETSSSCIVTIYEIFKDEPKPPSIQYIKEYYHLRDDELTIECHVHGYPRPVITWWRGCFQVKPSYKFTMLEEAHGVCKLLIYKPGNKDGGIYTMKAINSSGEAQINHTVEVARNLHYHVPGIFHARDKIQLDSLKQAKKAMEAALKSKADSDQRRAEAEEEQARLHPVKATPERLVPAKQKLAFATQLRDRMALEGSTIKFVATVIGPDPNTRWMKDDKWVVVGGNIKNLSEEGKAILEVGNVTSADSGVYKCVAKNDLSEIETSCYFKVYAAQADGDESEPIFALPLRDVYHASQNDLILDTKVRGNPRPEISWTKDQIPVVLDDRVVQIEHLDGICELIINKPTINDNGIYVCTAKNKLGSQSTTHTVVVDTTHTSRRSSILSAIAIQEGGGGGESADAKAKGKK
Protein: Pre-mRNA-splicing factor SPF27 (B2R7W3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAGTGLVAGEVVVDALPYFDQGYEAPGVREAAAALVEEETRRYRPTKNYLSYLTAPDYSAFETDIMRNEFERLAARQPIELLSMKRYELPAPSSGQKNDITAWQECVNNSMAQLEHQAVRIENLELMSQHGCNAWKVYNENLVHMIEHAQKELQKLRKHIQDLNWQRKNMQLTAGSKLREMESNWVSLVSKNYEIERTIVQLENEIYQIKQQHGEANKENIRQDF
Protein: DNA-directed RNA polymerases I and III subunit RPAC1 (A0A2R8Y5D3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAASQAVEEMRSRVVLGEFGVRNVHTTDFPGNYSGYDDAWDQDRFEKNFRVDVVHMDENSLEFDMVGIDAAIANAFRRILLAEVPTMAVEKVLVYNNTSIVQDEILAHRLGLIPIHADPRLFEYRNQGDEEGTEIDTLQFRLQVRCTRNPHAAKDSSDPNELYVNHKVYTRHMTWIPLGNQADLFPEGTIRPVHDDILIAQLRPGQEIDLLMHCVKGIGKDHAKFSPVATASYRLLPDITLLEPVEGEAAEELSRCFSPGVIEVQEVQGKKVARVANPRLDTFSREIFRNEKLKKVVRLARVRDHYIYGVSLCCSGWRAVARSRLTATSTSRVQAILLPQPLE
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q380X7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MLALLFLALIVSTCPAEPAANDVALEFNALCELIGIARARDKIPKLTLGSKITKQKEFIIALNMSVSSDTFFNQKFDRPDAPTGESPEWQKNKKTWQRLQKIINDKSSGAFGRVIKQPPDTEERELAATLNNQTVAAAEALTEGEVNGPTDKEIQDLLQGAVSGKGGAAPADDTKTFGTVARSCGGNGADNTGQGKSLANDILCLCSHDSSNAGFQGCAGEGATQIITYTRESGVTAALTTVTGKCKINTTQQVTAHRLAAAITNFKALLGRHEEAADLSSMRLGKGHAGNTRDGGGAGGCILYKGLGPNGIHDIPWVKKLEGAQHLLLLRYQAIREEKTVLYGMTTLRMTAEQLHKRALLTKKRPAGTPSKEPETKNQQITDCKQHKNNKTECENAGKCKWEGENETKGECKAKQGSDTPEAGTGDEATGTTTDKCKGKSQTDCKDGCKWDGKECKDSSILATKKFALMVSSSVILVILQHYKDICSIL
Protein: Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT (EC 6.3.5.13) (A0A0H2UQV8)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MNLKTTLGLLAGRSSHFVLSRLGRGSTLPGKVALQFDKDILQNLAKNYEIVVVTGTNGKTLTTALTVGILKEVYGQVLTNPSGANMITGIATTFLTAKSSKTGKNIAVLEIDEASLSRICDYIQPSLFVITNIFRDQMDRFGEIYTTYNMILDAIRKVPTATVLLNGDSPLFYKPTIPNPIEYFGFDLEKGPAQLAHYNTEGILCPDCQGILKYEHNTYANLGAYICEGCGCKRPDLDYRLTKLVELTNNRSRFVIDGQEYGIQIGGLYNIYNALAAVAIARFLGADSQLIKQGFDKSRAVFGRQETFHIGDKECTLVLIKNPVGATQAIEMIKLAPYPFSLSVLLNANYADGIDTSWIWDADFEQITDMDIPEINAGGVRHSEIARRLRVTGYPAEKITETSNLEQVLKTIENQDCKHAYILATYTAMLEFRELLASRQIVRKEMN
Protein: Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) (M0QZ10)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSLGVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIPTMENGPELILRFQKELKEIQVSCRELGNGLGACSLEKLVSHEPLD
Protein: Sodium- and chloride-dependent creatine transporter 1 (CHOT1) (CT1) (Creatine transporter 1) (Solute carrier family 6 member 8) (P28570)
Organism: Rattus norvegicus (Rat)
Function: Creatine:sodium symporter which mediates the uptake of creatine. Plays an important role in supplying creatine to the brain via the blood-brain barrier (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:32115505}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:12433955, ECO:0000269|PubMed:15702372}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanidinoacetate N-methyltransferase
- Glycine amidinotransferase, mitochondrial
Sequence:
MAKKSAENGIYSVSGDEKKGPLIVSGPDGAPSKGDGPAGLGAPSSRLAVPPRETWTRQMDFIMSCVGFAVGLGNVWRFPYLCYKNGGGVFLIPYVLIALVGGIPIFFLEISLGQFMKAGSINVWNICPLFKGLGYASMVIVFYCNTYYIMVLAWGFYYLVKSFTTTLPWATCGHTWNTPDCVEIFRHEDCANASLANLTCDQLADRRSPVIEFWENKVLRLSTGLEVPGALNWEVTLCLLACWVLVYFCVWKGVKSTGKIVYFTATFPYVVLVVLLVRGVLLPGALDGIIYYLKPDWSKLGSPQVWIDAGTQIFFSYAIGLGALTALGSYNRFNNNCYKDAIILALINSGTSFFAGFVVFSILGFMATEQGVHISKVAESGPGLAFIAYPRAVTLMPVAPLWAALFFFMLLLLGLDSQFVGVEGFITGLLDLLPASYYFRFQREISVALCCALCFVIDLSMVTDGGMYVFQLFDYYSASGTTLLWQAFWECVVVAWVYGADRFMDDIACMIGYRPCPWMKWCWSFFTPLVCMGIFIFNVVYYKPLVYNNTYVYPWWGEAMGWAFALSSMLCVPLHLLGCLLRAKGTMAERWQHLTQPIWGLHHLEYRAQDADVRGLTTLTPVSESSKVVVVESVM
Protein: HAUS augmin-like complex subunit 7 (26S proteasome-associated UCH37-interacting protein 1) (UCHL5-interacting protein) (X-linked protein STS1769) (Q99871)
Organism: Homo sapiens (Human)
Function: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}. Note=Localizes to interphase centrosomes and to mitotic spindle microtubules. {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}.
Interaction partners:
- HAUS augmin-like complex subunit 6
- HAUS augmin-like complex subunit 5
- HAUS augmin-like complex subunit 1
- HAUS augmin-like complex subunit 2
- HAUS augmin-like complex subunit 8
- HAUS augmin-like complex subunit 4
- HAUS augmin-like complex subunit 3
- Ubiquitin carboxyl-terminal hydrolase isozyme L5
- 26S proteasome non-ATPase regulatory subunit 8
- Tubulin gamma-1 chain
Sequence:
MAGQDAGCGRGGDDYSEDEGDSSVSRAAVEVFGKLKDLNCPFLEGLYITEPKTIQELLCSPSEYRLEILEWMCTRVWPSLQDRFSSLKGVPTEVKIQEMTKLGHELMLCAPDDQELLKGCACAQKQLHFMDQLLDTIRSLTIGCSSCSSLMEHFEDTREKNEALLGELFSSPHLQMLLNPECDPWPLDMQPLLNKQSDDWQWASASAKSEEEEKLAELARQLQESAAKLHALRTEYFAQHEQGAAAGAADISTLDQKLRLVTSDFHQLILAFLQVYDDELGECCQRPGPDLHPCGPIIQATHQNLTSYSQLLQVVMAVADTSAKAVETVKKQQGEQICWGGSSSVMSLATKMNELMEK
Protein: Solute carrier organic anion transporter family member (Q9W269)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362056}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU362056}.
Interaction partners:
- GH23453p
Sequence:
MVQSENPSSLGAELQDLEHGRRESRDESDVESRLLNNGKSYDKEKEAGNQDGEETTPKTGKSKKKKQKSEQDRLMTAEINKLLAESPLEKNVTCGFWIFKGTFYQRFANQTAYVLLYGIVGCIFSMTYAYFNGTITTIEKRFKIPSKNTGIISVGNDISQTLVSAVLAYYAGKGHRPRWIGFGLLTIVFFCILTTAPHFLYGPGEDALALTSEFGGMPDENATMEAIEEQRSKTLCRLNGGGAECEVGEGNFAPQLLLFVAQFISGIGGSLYYTLGVSYMDDNTKKSKTPALLSLSYFLRMLGPAIGYALASFCLRLYIAPQMHPVINNKDPRWLGAWWLGWLVMGGLLSFSGVFLSMFPKELPRAVARRKVEENRRREKERLSVKSTEKERLTAELDQKTTAEAKASFQDMLKTFRRLITNKTYMCNTLSSIFYLVGYTPYWIFTPKYIEVQYRQSAATSSMVTGTVALAFSAVGVLLSGFIISRYKPRARYMAAWNVIVGFLTVAGILAYAFIGCPGNESSVIVNIHDSSLAGNTTTCNSACSCDYVRYSPVCGENNMTYISACHAGCKKLLVNSEGKKIFYDCSCIPSDDAGNSTSQFKRLTSFDLSNDEVSQNTSVHSQLEALANGQAMPGACPVNCWTQFVAFLAVMCCLKFVGASGRASNFLVSVRCVPEKDKTAAMGFGMTLCSMLAFIPSPIFFGWVFDRVCLVWGKTCTNKGNCWLYDPLSMRYTLNFTAAVFIAIGAIFDLGVWYYAKDLKIFDEDVKEVEMKIVQHEEEANNEKNTEI
Protein: Importin N-terminal domain-containing protein (Q9BIB8)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Nsp1_C domain-containing protein
- GTP-binding nuclear protein ran-1
- Snurportin-1
- Importin subunit alpha-2
- Importin subunit alpha-1
- Importin N-terminal domain-containing protein
- Importin subunit alpha-3
- Exportin-2
- Importin subunit alpha
- Nuclear Pore complex Protein
Sequence:
MAEQAAEQMLTVLEKTVSQNQNDQKQAMDYIAAACQQDFPVFVQCLSMILRTQQCQSFVRQAAGLQLKNVLCAKETETKNVYLQRWLQLTAEVREQVKQNVTGTLGTEPSRPSIAAQCVAAIACAELPQNLWPNVINLLKSNVTESQSGEMLKESSLETLGYICQDIDPRVLETKANDVLTAIIHGMRPEESSANVRFAATNALLNSLEFTNTNFSNEAERNIIMQVVCESTSSSDQRVKVAALQCLVRIMQLYYEHMLSYMGSALFQITLSAMKSQEPEVAMQGMEFWSTVAEEEFDLYMTYEDEVERGAPNPKCASLRFMEQAASHVCPVLLEAMAHHDDGDDDDDWTPAKAAGVCLMLAAQCVRDDIVNHVIPFFKHFQNPDWKYKEAAIMAFGSILDGPDPKKLLPMAQEALPAIVAAMCDKNVNVRDTAAWSLGRVIDTCSELANNAELLQSVLPVLSNGLHQEPRVANNVCWALVSLVKACYESAVANGTDGSGQPDTFALSSVFDPMVGELIKITDRVDGNQSNLRITAYEALMELIKHSPKDCYSAVRNTTVVILKKLESLLQMESQATSEADKAQVRDLQAMLCATLQSVTRKMQPADIPAVGEHIMNGLYQIMNRAAATRSNAVMEEALLAVACLAEHLGKGFLSYMNVLKPYLLEGLSNTDETQVCAAAVGLVTDLSRALEAEIMPFMDELIQKLILCLQSPRLDRNVKVVIIGTFADIAMAIEAHFERYVGSVVPILNNAQNAAVVTDPNDDDQVDYVDRLREACLNSYTGIIQGLKAIPDTTAARNMINVFVEPIVQLITRISSMEPVPPSEALIATTAGIIGDLVQLYEGDIIRFFLTDNVTQMLQKGRKSKVSKTKSMANWATKEIKKHTNNGAATFNFNR
Protein: Uncharacterized protein YGL194C-A (Q2V2P6)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSNKEITCIKPFKIIALILLIVLIINLSYKLFLRRYLKSTVIWCLGIANTDRNDMMWWQVSPLLERWVWQLVDNYESGYE
Protein: Importin subunit beta-1 (Karyopherin subunit beta-1) (Nuclear factor p97) (Pore targeting complex 97 kDa subunit) (PTAC97) (SCG) (P70168)
Organism: Mus musculus (Mouse)
Function: Functions in nuclear protein import, either in association with an adapter protein, like an importin-alpha subunit, which binds to nuclear localization signals (NLS) in cargo substrates, or by acting as autonomous nuclear transport receptor. Acting autonomously, serves itself as NLS receptor. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin FxFG repeats and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin-beta and the three components separate and importin-alpha and -beta are re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. In association with IPO7, mediates the nuclear import of H1 histone. In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Imports SNAI1 and PRKCI into the nucleus (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q14974}. Nucleus envelope {ECO:0000250|UniProtKB:Q14974}.
Interaction partners:
- Importin subunit alpha-1
- Importin subunit alpha-5
- Snurportin-1
- Importin subunit alpha-3
- GTP-binding nuclear protein Ran
- Importin subunit alpha-4
- E3 SUMO-protein ligase RanBP2
- Importin subunit alpha-7
- Sterol regulatory element-binding protein 2
- GTP-binding nuclear protein Ran, testis-specific isoform
Sequence:
MELITILEKTVSPDRLELEAAQKFLERAAVENLPTFLVELSRVLANPGNSQVARVAAGLQIKNSLTSKDPDIKAQYQQRWLAIDANARREVKNYVLQTLGTETYRPSSASQCVAGIACAEIPVSQWPELIPQLVANVTNPNSTEHMKESTLEAIGYICQDIDPEQLQDKSNEILTAIIQGMRKEEPSNNVKLAATNALLNSLEFTKANFDKESERHFIMQVVCEATQCPDTRVRVAALQNLVKIMSLYYQYMETYMGPALFAITIEAMKSDIDEVALQGIEFWSNVCDEEMDLAIEASEAAEQGRPPEHTSKFYAKGALQYLVPILTQTLTKQDENDDDDDWNPCKAAGVCLMLLSTCCEDDIVPHVLPFIKEHIKNPDWRYRDAAVMAFGSILEGPEPNQLKPLVIQAMPTLIELMKDPSVVVRDTTAWTVGRICELLPEAAINDVYLAPLLQCLIEGLSAEPRVASNVCWAFSSLAEAAYEAADVADDQEEPATYCLSSSFELIVQKLLETTDRPDGHQNNLRSSAYESLMEIVKNSAKDCYPAVQKTTLVIMERLQQVLQMESHIQSTSDRIQFNDLQSLLCATLQNVLRKVQHQDALQISDVVMASLLRMFQSTAGSGGVQEDALMAVSTLVEVLGGEFLKYMEAFKPFLGIGLKNYAEYQVCLAAVGLVGDLCRALQSNILPFCDEVMQLLLENLGNENVHRSVKPQILSVFGDIALAIGGEFKKYLEVVLNTLQQASQAQVDKSDFDMVDYLNELRESCLEAYTGIVQGLKGDQENVHPDVMLVQPRVEFILSFIDHIAGDEDHTDGVVACAAGLIGDLCTAFGKDVLKLVEARPMIHELLTEGRRSKTNKAKTLATWATKELRKLKNQA
Protein: Neuropeptide gamma (NPgamma) (Q9PRZ3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Tachykinins are active peptides which excite neurons, evoke behavioral responses, and contract (directly or indirectly) many smooth muscles. Is a potent vasoconstrictor and secretagogue that plays a regulatory role in the central control of ventilation, in particular, the heart rate variability (HRV).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P25421}.
Interaction partners:
Sequence:
SSANPQITRKRHKINSFVGLM
Protein: RRM domain-containing protein (Q385Q3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDKALCTSLSCQSRPKRCRGSDNPQFGTSFSSGSNVPEMSLLSSAVQQAVEKVFSEHASDVGSELLSDEIFTSSVCRAILPSEDGAKPLSDQELQQRVRSCLEVVLAGKVDEERQLLVSEALTHQLAEVLLKAPPLIAATGVSQEENVQPDVKRVRSVFAGSSMSTVRVGVAPVGKVNSSGSLLPPPAPLSSVFSGSAVYPVRVVAFHNLPSKYCEKEALKEQLAEICARIPHSYYLNVHCVQSEHKAIASFGTKEAAAAVAFIVNTSGIHAPQTDGKDAGAPTVSAQPATEEEQEAVWAPLVEQVKALEESWSSWDEKFRANPPYKLYQEWVEAKNRGVGLDEALQQLTATNKVSEGQVTDTASYGVVESGTATVGLTQEGLQKKLVLLQGRLECKKIIERTEECMRELLGDTFSGSLERACSGPTHSTSSATLSNPRKALFIYDLPRPFDDVELVRFLQYVGVEPVHIWRNSAVPTTVCVELPSIGRVFTVLRQLDGTNMKFAGATFSRKYASTPQNASSCPLTVT
Protein: Class E vacuolar protein-sorting machinery protein hse1 (O74749)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Subcellular location: Endosome membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Vacuolar protein sorting-associated protein 27
- ESCRT-I complex subunit vps23
- AMSH-like protease sst2
- Vacuolar protein sorting-associated protein 28 homolog
- Vacuolar protein sorting-associated protein 20
- Polyubiquitin
- Vacuolar protein-sorting-associated protein 36
- Vacuolar-sorting protein dot2
- Vacuolar protein-sorting-associated protein 25
- ESCRT-III complex subunit did4
Sequence:
MFRGKPNSIETLILQATDEKNTKEKWDVIMDACDQLSSTSGDVGRNSIKFLNKRLDTANANIQLLALTLTDAIVKNCKTSIVREISSRTFTDSLLKIASDSTTHNRVRSRIAVLVNEWAEIMKKDPNMSLMQDICEKIRKLDIVDLRAPKKPEKEAMNELELKREEEELQYALALSLSESTAQSNKVENPQSTKDEPLQKTNQRQESNLATSPASTVSRVRALYDFAATEQGELSFKKGDIILVLESVYKDWWKGSCKNAVGIFPVNYVQRVVEPTIEQQRQSAHMEQQVFDALPQIDELLDTLSTTSPDAADDDALQGKYHAMIALRPKLVRLIEKYASQKEELMDLNERLLVARRDYEKLYEQSMSEMRNF
Protein: Leucine-rich repeat-containing protein 70 (Synleurin) (Q7Z2Q7)
Organism: Homo sapiens (Human)
Function: Renders cells highly sensitive to the activation by cytokines and lipopolysaccharide (LPS).
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Importin-11
- Large ribosomal subunit protein uL11
- Importin-5
- Large ribosomal subunit protein uL23
Sequence:
MCGLQFSLPCLRLFLVVTCYLLLLLHKEILGCSSVCQLCTGRQINCRNLGLSSIPKNFPESTVFLYLTGNNISYINESELTGLHSLVALYLDNSNILYVYPKAFVQLRHLYFLFLNNNFIKRLDPGIFKGLLNLRNLYLQYNQVSFVPRGVFNDLVSVQYLNLQRNRLTVLGSGTFVGMVALRILDLSNNNILRISESGFQHLENLACLYLGSNNLTKVPSNAFEVLKSLRRLSLSHNPIEAIQPFAFKGLANLEYLLLKNSRIRNVTRDGFSGINNLKHLILSHNDLENLNSDTFSLLKNLIYLKLDRNRIISIDNDTFENMGASLKILNLSFNNLTALHPRVLKPLSSLIHLQANSNPWECNCKLLGLRDWLASSAITLNIYCQNPPSMRGRALRYINITNCVTSSINVSRAWAVVKSPHIHHKTTALMMAWHKVTTNGSPLENTETENITFWERIPTSPAGRFFQENAFGNPLETTAVLPVQIQLTTSVTLNLEKNSALPNDAASMSGKTSLICTQEVEKLNEAFDILLAFFILACVLIIFLIYKVVQFKQKLKASENSRENRLEYYSFYQSARYNVTASICNTSPNSLESPGLEQIRLHKQIVPENEAQVILFEHSAL
Protein: Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3) (O62807)
Organism: Sus scrofa (Pig)
Function: Nuclear receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the nuclear receptor binds to DNA specific PPAR response elements (PPRE) and modulates the transcription of its target genes, such as acyl-CoA oxidase. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis. ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer. Acts as a critical regulator of gut homeostasis by suppressing NF-kappa-B-mediated pro-inflammatory responses. Plays a role in the regulation of cardiovascular circadian rhythms by regulating the transcription of BMAL1 in the blood vessels.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250}. Note=Redistributed from the nucleus to the cytosol through a MAP2K1/MEK1-dependent manner. NOCT enhances its nuclear translocation (By similarity). {ECO:0000250}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Retinoid X receptor alpha.
- protein acetyllysine N-acetyltransferase
- Actin, cytoplasmic 1
- Retinoic acid receptor RXR-gamma
- Nuclear receptor coactivator 1
- Mediator of RNA polymerase II transcription subunit 1
- Nuclear receptor corepressor 2
- Retinoic acid receptor RXR-gamma
- Actin gamma 1
Sequence:
MGETLGDSLIDPESDAFDTLSANISQEVTMVDTEMPFWPTNFGISSVDLSVMDDHSHSFDIKPFTTVDFSSISTPHYEDIPFPRADPMVADYKYDLKLQDYQSAIKVEPVSPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKNIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
Protein: ATP-dependent zinc metalloprotease FTSH 10, mitochondrial (AtFTSH10) (EC 3.4.24.-) (Q8VZI8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable ATP-dependent zinc metallopeptidase. Involved in the assembly and/or stability of the complexes I and V of the mitochondrial oxidative phosphorylation system.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14671022, ECO:0000269|Ref.9}; Single-pass membrane protein {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14671022, ECO:0000269|Ref.9}; Matrix side {ECO:0000269|PubMed:14630971, ECO:0000269|PubMed:14671022, ECO:0000269|Ref.9}.
Interaction partners:
- ATP-dependent zinc metalloprotease FTSH 3, mitochondrial
- Mitochondrial metalloendopeptidase OMA1
- RHOMBOID-like protein 12, mitochondrial
- Prohibitin-2, mitochondrial
- Prohibitin-3, mitochondrial
- Prostaglandin E synthase 2
- Putative pentatricopeptide repeat-containing protein At5g40405
- Lon protease homolog 4, chloroplastic/mitochondrial
- Mitochondrial intermediate peptidase, mitochondrial
- SPFH/Band 7/PHB domain-containing membrane-associated protein family
Sequence:
MIFSKLGSSLARSSRSKGFVYGGGVRSAVFNQGRLRAPQNLEAAVNQVDGGLGFLRRHFASFAARKGLEAGDLSRAFANPRLRRFFSSQTPKKKNYENYYPKDSKKAPKNEQKSESRDGSKKNENENAGDAFSNEYQNMLIPLMAIALILSTFSLGSREQQQISFQEFKNKLLEAGLVDHIDVSNKEVAKVYVRSSPKSQTTEEVVQGPGNGVPAKGRGGQYKYYFNIGSVESFEEKLEEAQEAIGVNSHDFVPVTYVSETIWYQELLRFAPTLLLVATLIFGARRMQGGLGGLGGPGGKAGRGIFNIGKAQITRADKNSKNKIYFKDVAGCEEAKQEIMEFVHFLQNPKKYEDLGAKIPKGALLVGPPGTGKTLLAKATAGESAVPFLSISGSDFMEMFVGVGPSRVRNLFQEARQCAPSIIFIDEIDAIGRARGRGGFSGGNDERESTLNQLLVEMDGFGTTAGVVVLAGTNRPDILDKALLRPGRFDRQITIDKPDIKGRDQIFQIYLKKIKLDHEPSYYSQRLAALTPGFAGADIANVCNEAALIAARHEGATVTMAHFDSAIDRVIGGLEKKNRVISKLERRTVAYHESGHAVAGWFLEHAEPLLKVTIVPRGTAALGFAQYVPNENLLMTKEQLFDMTCMTLGGRAAEQVLIGRISTGAQNDLEKVTKMTYAQVAVYGFSDKIGLLSFPQREDEFSKPYSNRTGAMIDEEVREWVGKAYKRTVELIEEHKEQVAQIAELLLEKEVLHQDDLTKVLGERPFKSGETTNYDRFKSGFEESEKESQKESVPVKPVEDDGIPPLEPQVVPT