wanglab/gogpt-training-data huggingface dataset:
Protein: Superkiller protein 3 (O94474)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the SKI complex involved in 3'-mRNA degradation pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative ATP-dependent RNA helicase C550.03c
- Meiotic recombination protein rec14
- Uncharacterized GTP-binding protein P8A3.05
- Exosome complex component csl4
- Exosome complex component rrp45
- Exosome complex component ski6
- Exosome complex component rrp46
- Exosome complex component rrp42
- Small ribosomal subunit protein RACK1
- Exosome complex component rrp40
Sequence:
MAKPALKAAKEALVVKNYELAIEQSKKALSFDANNYNANVFLGVAYFSTKQLSESKEAYLDAIKIDEKAVLAWQGLWNLYESTHDISELHKITPILASKFLELEEQNKCLNTVNKYMEVVKKYGNKADEFKALKLLTPEEGEIYEYLEGRVLPLQTVYMQMVDIQESMDRCYFESEVNKRKTRLGARLEQVMRDVELEIYKDSPLETLYNQIINYAETDEIRRLTESKLLHMYNKLLILSEIKEKSHWRERIWDLIQGMVTLHIPEQAAWTIYFEWQDHSDISFFQSAELQEYIELFPGSPLAQALFAFRNSDLWHKEHPIQLEDSNNSAELAKETKEEDDSENSVDKKENEEDIISSTMMPQDEVLANLTEAYENAPQSTIISECLAKYYIHLKEYEYAIGLSKAALEVLKRLQQDTGVKLDKLTRIFQLCLAIGYSHYEVPRYLFQAMHYYDILLAADPRNYHALLGKGLVQIENEQYSDAVKTLGLLLDDHENDPSLSELSWCYFKTGNLPKAISTVEKCLDVLLSMDVERFKIAEAYYRYGIYILNRKSENYLEDSFSAFVSSLRKDPNYAPAYTSLGLYYRDIHDMVRATKCFQKAFELDASQVEAAEALAKTFAEANEWELVEVISRRVLNTSENDLKRKKKFNWHHTSLGVLELNAKNFHKAIVHFQSALRISPKDTNAWSGLGEAYARSGRYVSALKAFNRASILDPDDWYVKYFIATLEKDMGEYEVAVSTLSEILAVRSKELCVQVSLAETYVRLAKLYHARGFYSRAADSLEKSIQICCNVLKEDITSIFSWEILGDACLSFCQLKNYHNRFPNSLISDILFTTEAMKCANNGRQFENMIYLPDLETSSGAIFIAAVAITCFTIHLSLVADDKLLLPVSWYNLGSSYYRFYECDTTKDATLQVAINCIKQAIKLEAKNYVFWNMLGVLFSQTKAVRSAQHCYIQSLLLNERSSGVWANYGALCIQNHDVECANAAFTRSISIDPDNSQAWLGKAYCSIAVGSIRKAVQIIHHAFEISSGKMPDVNYWYADTMLHAVNTEDFVTTDGDIWSATYAIKRYLGENPTDTFAYYIKASLLEHLGETTDSVPSAIRLCELLEQEYDVSESPVILKRFIDAKALLGRLYLAKKSFENSVEQAGIALDLLEGEEDEDIKRTTLGLNLTCGTASFFLNKLEKSLDCFEKALLVSDSNADVVVLVSKVLWALGSENGKQAAREQLFEALEQSPSHIGSLLCLGAIAIYDEDDAVCSAIEDSIAHLKKDEVLRSGALKQVQIMEVLLTKKIDESMIKSLLQRFLHVYPFAASSWTLLTNRYASKSLANAFATTLYTHPSRPDDLAQSYRLQNSIDRAQVAIHLVPWDSANWKALHGVTHEALVSSDAS
Protein: Non-specific lipid-transfer protein (A7TUG4)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MASSMSLKLACVAVLCMVVGAPLAQGAVTCGQVTSSLAPCIGYLTGNGAGGVPPGCCGGIKSLNSAAQTTPDRQAACKCIKSAAAGISGINYGIASGLPGKCGVNIPYKISPSTDCNSVK
Protein: Ran-binding protein 1, putative (Q386H3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- GTP-binding nuclear protein
- Leucine-rich repeat protein
- Nuclear pore protein
- Nucleoporin
- Nuclear pore complex protein
- Nucleoporin
- Nucleoporin NSP1-like C-terminal domain-containing protein
- Small GTP-binding protein RAB6, putative
- Small ubiquitin protein, putative
- Uncharacterized protein
Sequence:
MADGKAENELMEIEEIAVSDGGAARFAPVEVKSGEEKYNIVWEETGKLLRFDEGENAWKERGQGMAKILQKKEDSGVYMFVFRREGVGKLAAQHYLLRGMTIKVHPQSEKALLWTAFKDYSDDEEGFPERFVLRFASKELADSGLKAFNDALSKTTT
Protein: Probable polysaccharide biosynthesis protein EpsC (P71052)
Organism: Bacillus subtilis (strain 168)
Function: Involved in biofilm formation.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Putative pyridoxal phosphate-dependent aminotransferase EpsN
- Uncharacterized sugar transferase EpsL
- UDP-N-acetylbacillosamine N-acetyltransferase
- Putative glycosyltransferase EpsE
- Putative glycosyltransferase EpsD
- Putative tyrosine-protein kinase YveL
- Putative glycosyltransferase EpsF
- Uncharacterized protein YveK
- Putative pyruvyl transferase EpsO
- Uncharacterized glycosyltransferase EpsJ
Sequence:
MIIALDTYLVLNSVIAGYQFLKDSYQFYDSGALLLTAVSLLLSYHVCAFLFNQYKQVWTYTGLGELIVLLKGITLSAAVTGVIQYAVYHTMFFRLLTACWVLQLLSIGGTRILSRVLNESIRKKRCASSRALIIGAGSGGTLMVRQLLSKDEPDIIPVAFIDDDQTKHKLEIMGLPVIGGKESIMPAVQKLKINYIIIAIPSLRTHELQVLYKECVRTGVSIKIMPHFDEMLLGTRTAGQIRDVKAEDLLGRKPVTLDTSEISNRIKGKTVLVTGAGGSIGSEICRQISAFQPKEIILLGHGENSIHSIYTELNGRFGKHIVFHTEIADVQDRDKMFTLMKKYEPHVVYHAAAHKHVPLMEHNPEEAVKNNIIGTKNVAEAADMSGTETFVLISSDKAVNPANVMGATKRFAEMIIMNLGKVSRTKFVAVRFGNVLGSRGSVIPIFKKQIEKGGPVTVTHPAMTRYFMTIPEASRLVIQAGALAKGRQIFVLDMGEPVKIVDLAKNLIHLSGYTTEQVPIEFTGIRPGEKMYEELLNKNEVHAEQIFPKIHIGKAVDGDWPVLMRFIEDFHELPEADLRARLFAAINTSEEMTAASVH
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (FK506-binding nuclear protein) (FKBP-70) (Nucleolar proline isomerase) (Proline rotamase) (P38911)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Proline isomerase that belongs to an abundant class of enzymes that catalyze the cis-trans isomerization of X-Pro peptide bonds and can accelerate the refolding of proline-containing polypeptides. Specifically binds nuclear localization sequences. May be involved in the assembly or folding of ribosomal proteins.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:8051210}.
Interaction partners:
- FK506-binding protein 4
- UBX domain-containing protein 2
- ERAD-associated E3 ubiquitin-protein ligase DOA10
- Cell division control protein 48
- Ribosome biogenesis protein NOP53
- Ribosome biogenesis protein RPF2
- Casein kinase II subunit alpha'
- H/ACA ribonucleoprotein complex subunit CBF5
- U3 small nucleolar RNA-associated protein 10
- Nucleolar protein 58
Sequence:
MSDLLPLATYSLNVEPYTPVPAIDVTMPITVRITMAALNPEAIDEENKPSTLRIIKRNPDFEDDDFLGGDFDEDEIDEESSEEEEEEKTQKKKKSKGKKAESESEDDEEDDDEDDEFQESVLLTLSPEAQYQQSLDLTITPEEEVQFIVTGSYAISLSGNYVKHPFDTPMGVEGEDEDEDADIYDSEDYDLTPDEDEIIGDDMDDLDDEEEEEVRIEEVQEEDEEDNDGEEEQEEEEEEEQKEEVKPEPKKSKKEKKRKHEEKEEEKKAKKVKKVEFKKDLEEGPTKPKSKKEQDKHKPKSKVLEGGIVIEDRTIGDGPQAKRGARVGMRYIGKLKNGKVFDKNTSGKPFAFKLGRGEVIKGWDIGVAGMSVGGERRIIIPAPYAYGKQALPGIPANSELTFDVKLVSMKN
Protein: Heterogeneous nuclear ribonucleoprotein U-like 1 (Q9BTB7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDVRRLKVNELREELQRRGLDTRGLKAELAERLQAALEAEEPDDERELDADDEPGRPGHINEEAELQPATLQPGRLQPGLHSPTASTSTTTCLQLWELRRLQPGPLYPTATPHRTDLPSAQL
Protein: Diacyltrehalose acyltransferase Chp2 (EC 2.3.1.-) (O50440)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the final steps of polyacyltrehalose (PAT) biosynthesis. Catalyzes the transfer of three mycolipenoyl groups onto diacyltrehalose (DAT) to form PAT.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:25124040, ECO:0000269|PubMed:25331437}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Acyltrehalose exporter MmpL10
- Putative fatty-acid--CoA ligase FadD21
- SL1278 acyltransferase Chp1
- Acyltransferase PapA3-trehalose mycolipenoyltransferase)
Sequence:
MKRVIAGAFAVWLVGWAGGFGTAIAASEPAYPWAPGPPPSPSPVGDASTAKVVYALGGARMPGIPWYEYTNQAGSQYFPNAKHDLIDYPAGAAFSWWPTMLLPPGSHQDNMTVGVAVKDGTNSLDNAIHHGTDPAAAVGLSQGSLVLDQEQARLANDPTAPAPDKLQFTTFGDPTGRHAFGASFLARIFPPGSHIPIPFIEYTMPQQVDSQYDTNHVVTAYDGFSDFPDRPDNLLAVANAAIGAAIAHTPIGFTGPGDVPPQNIRTTVNSRGATTTTYLVPVNHLPLTLPLRYLGMSDAEVDQIDSVLQPQIDAAYARNDNWFTRPVSVDPVRGLDPLTAPGSIVEGARGLLGSPAFGG
Protein: PNUTSDm protein (Q70HU3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00649}.
Interaction partners:
Sequence:
MPRIVPLQLLRCLRVLLDNNGGILSAVEVKRISGLMAKYSKKLVSKCVYVQILKSTKTELLGDFMAVGGWSLVYTWLNDAIRAMNWPLVQEILELLLLSPVDVNRLKINSAPILVKGLCKDGGNEGVRILAKRLVEQWLKIVTENTSMTIQGAAPHIAATTASQVPASVSGAGSASVPDSASSSDSTDSAGAPVTYTITSAANSSNSNSITIKWKPLLDNPDGGDETDSGTQSKDNEVEHLEKGSSATHLLADASLGKKSGLDDSSSAAEVKSGEDVDNKKHKSSKSDKSKRSEKEREKDRKKESSSHRSSSSSHKSSSSSSSSSSKSSSSKSSSSSSSSHRSSSDKYRDKDKARSSSGSSSSSKDRERSSGSSSSSSNKHKSSKSSSSSSSSSSSSSGSSSSKDRKSSSSTSSSSSSSRQDKDKDNKLMPPPAVAASNAAGTSPTASAKESDAQKPRSIPIMSRKASISIEIRRDTEKTATVKTYQSKFRSHGLTEEAPPPPSRKGLKKPTSSAVAASPALMAVPSSLKRPSPPPRDLSTDKKAKIDINNVAGHVERPGAAKLIAPKKIQTLVETNLFSDALAASIEPKKVVKRKRTSATSPTDKDAPLAPLKFYQDTLDESKSEEKSDDSSKENDDARSSSPGKDTDADDDDIPLKRVKEDIEQKVQKAKAAAGGEGGEAGNTSDNAEDLPEEPKKPGPGCGPDGPPGVLTLHRRKGPKKKLTWQSEEKLTQIRYFEVDRSERVNVMKQTFLEMKNMERFSERDALTIARRGFDDTMEPQMEWRPLLEVDNVPDHPNGNLSKQRQVQMDREATTLRALYFSPDMIPDSPAEAELEPHFAHDIPVIPMDDLTGNPDAVNDYSALAWPEPKKYAPSSGVGANISGSDMGFNDNMLTGLGAGPNLMQNPFDPFMGGMPAPTGMPPGPNMMPNQVPNGTPQIWQNQMGPGGGPPGVPPMMNGPGGPGMDMSNMNMNNMPPQNFMGNQFGSPVSPFGSGPPPGFNQYPPMMMNGPGPGPVMGPNGPVMGPNGPMMNGPPNGPMMNGPPNGMGPGLMMGGPRNNNNNNNRNKNNGGGIWRSGGNNFQENSGGNWRSAGSGPNRGGGGGNGNTGVCKQFMRGHCNMGKNCKYVHPQKKRL
Protein: ATPase-like fidgetin (Protein sur2) (O43078)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDSDLDRILPIASRALLCEGNRDWAGAYVSYCKVLEEMKKSSAARDRMGLGPLTGAEACSWNGLYDNCLSKASKLRKTILESEMERQNYQLAAKLSKKAPVDLHPLRPVRSQTPAYTPMTTRMMYRQTRGAQSEVNLSTPKQIYSKHSPPSTSTSSIVSSSYGDAPSYLAPSKPNRSPPLKPEDPFASFNSSASAIAAASKSAAASASALSSDTGRSATMNSTTFPTAMKSQSTTKPTLSNSVSSPSIQVSNNQNANNSTPLSFHAPIPPLHVPAVPLTSASHSSSDGKSRKHPSPYKPYLNSSHDTLGSSTRPSSADTAGSPATSPPATADSKTIVSKTISASTTQQTEPLQQTTPSSDFEYAIMNEIISNHEPVYWSDIAGLDDAKNSLKEAVIYPFLRPELFQGLREPVQGMLLFGPPGTGKTMLARAVATEAKATFFSISASSLTSKYLGDSEKLVRALFEVAKRQTCSVIFVDEIDSILSARNDSGNEHESSRRLKTEFLIQWSSLTNAAPDKQTGHSPRVLVLAATNLPWCIDEAARRRFVKRTYIPLPEKETRYKHLSHLLHNQVHCLTEEDLEELVNLTEGYSGSDITALAKDAAMGPLRNLGDALLTTSAEMIPPISLNHFKASLRTIRPSVSQEGIHRYEEWNKQFGSQR
Protein: Large ribosomal subunit protein uL5 (60S ribosomal protein L11) (Q6IQI6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Large ribosomal subunit protein eL34
- Mitochondrial ribosomal protein S16.
- Ribosomal protein S3
- Large ribosomal subunit protein eL21
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein eS4
- Large ribosomal subunit protein uL18
- 40S ribosomal protein S6
- 40S ribosomal protein S15
Sequence:
MADQSEKKENPMRELRIRKLCLNICVGESGDRLTRAAKVLEQLTGQTPVFSKARYTVRSFGIRRNEKIAVHCTVRGAKAEEILEKGLKVREYELRKNNFSDTGNFGFGIQEHIDLGIKYDPSIGIYGLDFYVVLGRPGFSIADKKRKTGRIGAKHRIRKEEAMRWFQQKYDGIILPGK
Protein: Splicing factor SF3a60 homolog (Protein ATROPOS) (Splicing factor ATO) (Q9FG01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Splicing factor homolog to SF3a60 that may be involved in pre-spliceosome formation. Is necessary for gametic cell fate determination.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130}.
Interaction partners:
- At2g32600/T26B15.16
- Nuclear protein-like
- Uncharacterized protein At3g23325
- U2 small nuclear ribonucleoprotein A'
- Cell division cycle 5-like protein
- Small nuclear ribonucleoprotein Sm D2
- Protein STABILIZED1
- Probable splicing factor 3A subunit 1
- SWAP
- 110 kDa U5 small nuclear ribonucleoprotein component CLO
Sequence:
MSSTLLEQTRSNHEEVERLERLVVEDLQKEPPSSKDRLVQGHRVRHMIESIMLTTEKLVETYEDKDGAWDDEIAALGGQTATGTNVFSEFYDRLKEIREYHKRHPSGRLVDANEDYEARLKEEPIIAFSGEEGNGRYLDLHDMYNQYINSKFGERVEYSAYLDVFSQPEKIPRKLKLSRQYMKYMEALLEYLVYFFQRTEPLQDLDRILSKVCSDFEEQYADGIVEGLDNELIPSQHTVIDLDYYSTVEELVDVGPEKLKEALGALGLKVGGTPQQRAERLFLTKHTPLEKLDKKHFARPPHNGKQNGDAKSTHESENAKEIALTEAKVKKLCNLLDETIERTKQNIVKKQSLTYEEMEGEREGEEANTELESDDEDGLIYNPLKLPIGWDGKPIPYWLYKLHGLGQEFKCEICGNYSYWGRRAFERHFKEWRHQHGMRCLGIPNTKNFNEITSIEEAKELWKRIQERQGVNKWRPELEEEYEDREGNIYNKKTYSDLQRQGLI
Protein: Small ribosomal subunit protein uS11y (40S ribosomal protein S14-2) (Q9CAX6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm.
Interaction partners:
- Small ribosomal subunit protein eS28z/eS28y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein uL1z
- U3 small nucleolar ribonucleoprotein protein IMP3
- Small ribosomal subunit protein eS10z
- Small ribosomal subunit protein eS8y
- Large ribosomal subunit protein eL15z
- Small ribosomal subunit protein uS7z
- Small ribosomal subunit protein uS8mz
- Small ribosomal subunit protein eS28x
Sequence:
MSKRKTKEPKVETVTLGPSVREGEQVFGVVHIFASFNDTFIHVTDLSGRETLVRITGGMKVKADRDESSPYAAMLAAQDVAQRCKELGITAMHVKLRATGGNKTKTPGPGAQSALRALARSGMKIGRIEDVTPIPTDSTRRKGGRRGRRL
Protein: Spore coat protein SP87 (Protein PL3) (P54643)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May contribute to the structure of the coat at the interface between the middle, cellulosic layer and the outer, electron-dense, proteinaceous layer.
Subcellular location: Cytoplasmic vesicle, secretory vesicle. Spore coat. Note=Accumulates specifically in regulated secretory vesicles of prespore cells (prespore vesicles). The protein later accumulates extracellularly in the spore coat.
Interaction partners:
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein uL14
Sequence:
MLFLKNIGVFFMIFLVSKSYATDCNKITNEEECHKSSECIVINYTPCCGEQKWACSKGTFDTCTYENSCYRNSSNNQVVEVSNKCFNLDGFIKITTPTEYSCSDAKIKECALLGKSCSFQKNSCSNPTSCCPGESICEGLSSGSSTSGGGSSGGTSGGSSSGGTSGGSSSGGTSGSSSSGSSSGGVSSCSTTHCPEGYHCSMVNDVATCLASTTGGTGLPGTSSSTAGVSSCLTTLCPIGHICVEDSNGVNCVPNGGGTSGGSSSTGTSGGHPDPCRDVDCPDGFHCECKDGKTAKCVPSPTTGSSSTSGGHPDPCKDVTCPDGFHCECKDGKTAKCVPSPTTGSSSTSGGNTNPCSNVNCPDGFYCECKDGKTAKCVPSGPTQPPKPPVCSLRCPPNHECRFNDQGHQCCVKVHHDRCSLRCPHGHECKVDHNGKECCVRSHRPPPPEVCSLRCPPKHECKFDDHGKKCCVKIHCDEVCDLDCGRGFECKIRHDGSKCCVRSERPHPPQHEKCNKRCPPGHECKVDQHGKECCVVAHRPPPKCSLRCPPRHECRVNHFGEECCVKVHHDKCSLRCPPGHECKVDQHGKECCVVAHRPPPKCSLRCPPKHECRINHFGEECCVKSRNDCLTCEDLNCERKGLHCAMKTVPIDKENCCEKVPVCYSTNPLLDGGHGFI
Protein: Small ribosomal subunit protein uS15m (37S ribosomal protein S28, mitochondrial) (O13602)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential component of the small mitochondrial ribosomal subunit.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS17m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS14m
Sequence:
MRLFEGAFQPWKLASTNLMQQCLLLNKKSQFHTTCILQGLKKQKANQRRKQNLKRREELRKQNLDTLADPIIGHSSEWIARLLKPYEILVERKKPNFPIRSIKFPASMETINLIVEKFEKIRASATEETKDFIKLNEVNEFPSSDTSLESNQDGFERLHPLAERLERMSQLSDLRKESIHRIFNIENSNSKTLRLNNKQLAVESFARNERDTGSPEVQAAVYTSRILALSDHCKNHKKDQTGKRMLRYYVHQRQRMLKYLRKVNFDRYVHCIKNLGLTDELVLREVTQ
Protein: Ras-related protein Rab-20 (P35295)
Organism: Mus musculus (Mouse)
Function: Plays a role in apical endocytosis/recycling. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium. Plays a role in the fusion of phagosomes with lysosomes (By similarity).
Subcellular location: Cytoplasmic vesicle, phagosome {ECO:0000250|UniProtKB:Q9NX57}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus {ECO:0000250|UniProtKB:Q9NX57}. Note=Recruited to phagosomes containing S.aureus or Mycobacterium (By similarity). Highly enriched on apical endocytic structures in polarized epithelial cells of kidney proximal tubules (PubMed:7706395). {ECO:0000250|UniProtKB:Q9NX57, ECO:0000269|PubMed:7706395}.
Interaction partners:
- Rab5 GDP/GTP exchange factor
Sequence:
MRKPDGKIVLLGDMNVGKTSLLQRYMERRFPDTVSTVGGAFYLKQWRSFNISIWDTAGREQFHGLGSLYCRGAAAIILTYDVNHPQSLFELEDRFLGLTETANNDCLFAIVGNKVDLTSERDTEGGEKEGPASGKVGSCVSTKVPKQVQPEDAVALYKKILKYKMLDEREMPAAEQMCFETSAKTGYNVDLLFETLFDLVVPMIMRQRAEESDQTVDIASCKTPKQTRSGCCA
Protein: ATPase protein 9 (ATPase subunit c) (Q6NN09)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- ATP synthase F
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit alpha, mitochondrial
- ATP synthase subunit a
- ATP synthase F
- ATP synthase subunit b, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit g
- Putative ATP synthase subunit f
- ATP synthase subunit O, mitochondrial
Sequence:
MFVSTVSRIAPVARSAFLANSKQYLRPLSSAIISQSQTLAAQNTTPVALLPQIRSFQTSPVTRDIDSAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMMAFLLLFAF
Protein: Small GTPase, putative (Q38AY2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- SH3 domain protein, conserved
- 14-3-3-like protein, putative
- 14-3-3-like protein, putative
- Uncharacterized protein
- Protein farnesyltransferase subunit beta
- Serine/threonine-protein kinase, putative
- BTB domain-containing protein
- Ras-family member, GTP-binding protein, putative
- Raptor N-terminal CASPase-like domain-containing protein
- Raptor N-terminal CASPase-like domain-containing protein
Sequence:
MNLRGDGSAQKYASVPTLYNVVVLGCERVGKSTFIDQVMKGTFRSDYVPTTLETFIHRTTVDGRNYVLHLCDSSGSEAFVRHRLLYLARADGVLLFYSTTDKESLASVVGWVKELREARHNIGVKAAMPILLVGTKRDDRRSRVVTMPEAEAVARSCLSALSLKMQHMNRKKVVEAEGFAKLVRDAISSTLPVVEVSALRTNEVLHALRIMILMISNFSKRRLPAPVTLTSSIEFATPPSLTPCFTSFDERPGSAFFRMRSPIRALGERSNIAVGGTTSPSAVVVKRTPSLVGVAVASRRNSAARRNTVDAVRGPTECEDGSAPWCSDVVLVGGTEPEPFSALHENGYCVSEGPPNQTETQSTLLRSLSHDGEVHACGLERQKKRELSGRRREVGCTGSCVIM
Protein: LD15989p (Q86NX9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
ASRDGRLRMNDQLLSVNGVSLRGQNNAEAMETLRRAMVNTPGKHPGTITLLVGRKILRSASSSDILDHSNSHSHSHSNSSGGSNSNGSGNNNNSSSNASDNSGATVIYLSPEKREQRCNGGGGGGSAGNEMNRWSNPVLDRLTGGICSSNSAQPSSQQSHQQQPHPSQQQQQQRRLPAAPVCSSAALRNESYYMATNDNWSPAQMHLMTAHGNTALLIEDDAEPMSPTLPARPHDGQHCNTSSANPSQNLAVGNQGPPINTVPGTPSTSSNFDATYSSQLSLETNSGVEHFSRDALGRRSISEKHHAALDARETGTYQRNKKLREERERERRIQLTKSAVYGGSIESLTARIASANAQFSGYKHAKTASSIEQRETQQQLAAAEAEARDQLGDLGPSLGMKKSSSLESLQTMVQELQMSDEPRGHQALRAPRGRGREDSLRAAVVSEPDASKPRKTWLLEDGDHEGGFASQRNGPFQSSLNDGKHGCKSSRAKKPSILRGIGHMFRFGKNRKDGVVPVDNYAVNISPPTSVVSTATSPQLQQQQQQQLQQHQQQQQIPTAALAALERNGKPPAYQPPPPLPAPNGVGSNGIHQNDIFNHRYQHYANYEDLHQQHQQHQISRRHQHYHSQRSARSQDVSMHSTSSGSQPGSLAQPQAQSNGVRPMSSYYEYETVQQQRVGSIKHSHSSSATSSSSSPINVPHWKAAAMNGYSPASLNSSARSRGPFVTQVTIREQSSGGIPAHLLQQHQQQQLQQQQPTYQTVQKMSGPSQYGSAAGSQPHASKV
Protein: Vitamin D 25-hydroxylase (EC 1.14.14.24) (Cytochrome P450 2R1) (Q6VVW9)
Organism: Mus musculus (Mouse)
Function: A cytochrome P450 monooxygenase involved in activation of vitamin D precursors. Catalyzes hydroxylation at C-25 of both forms of vitamin D, vitamin D(2) and D(3) (calciol). Can metabolize vitamin D analogs/prodrugs 1alpha-hydroxyvitamin D(2) (doxercalciferol) and 1alpha-hydroxyvitamin D(3) (alfacalcidol) forming 25-hydroxy derivatives. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6VVX0}; Peripheral membrane protein. Microsome membrane {ECO:0000250|UniProtKB:Q6VVX0}; Peripheral membrane protein.
Interaction partners:
- 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial
- 1,25-dihydroxyvitamin D
- Vitamin D-binding protein
- 7-dehydrocholesterol reductase
- Cytochrome P450 3A25
- Glutamine-dependent NAD
Sequence:
MLELPGARACAGALAGALLLLLFVLVVRQLLRQRRPAGFPPGPPRLPFVGNICSLALSADLPHVYMRKQSRVYGEIFSLDLGGISTVVLNGYDVVKECLVHQSEIFADRPCLPLFMKMTKMGGLLNSRYGRGWIDHRRLAVNSFHYFGSGQKSFESKILEETWSLIDAIETYKGGPFDLKQLITNAVSNITNLILFGERFTYEDTDFQHMIELFSENVELAASAPVFLYNAFPWIGILPFGKHQRLFRNADVVYDFLSRLIEKAAVNRKPHLPHHFVDAYLDEMDQGQNDPLSTFSKENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVHKEIDLIVGHNRRPSWEYKCKMPYTEAVLHEVLRFCNIVPLGIFHATSEDAVVRGYSIPKGTTVITNLYSVHFDEKYWKDPDMFYPERFLDSNGYFTKKEALIPFSLGRRHCLGEQLARMEMFLFFTSLLQQFHLHFPHELVPNLKPRLGMTLQPQPYLICAERR
Protein: MIF-like protein mif-3 (P90835)
Organism: Caenorhabditis elegans
Interaction partners:
- Macrophage migration inhibitory factor
- PWWP domain-containing protein
- L-dopachrome isomerase
- Bromo domain-containing protein
- Inverted formin-2
- Cleavage and polyadenylation specificity factor subunit 5
- IntraMembrane Protease
Sequence:
MPVIKVQTNVKKVSDGFEVRLAIHMAKVMKRPESQIFVSLDMNSRMTRGQLTDPLAVLDVTSSTVLTPILTEEYTVALCEFFSQELALDSDAVLINYRSLSPELIGFNGHILTENRPFISTDRARFIIGVLGIAFLAFLLQFLKYI
Protein: V-type proton ATPase subunit d 1 (V-ATPase subunit d 1) (32 kDa accessory protein) (V-ATPase 40 kDa accessory protein) (V-ATPase AC39 subunit) (p39) (Vacuolar proton pump subunit d 1) (P61421)
Organism: Homo sapiens (Human)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. May play a role in coupling of proton transport and ATP hydrolysis (By similarity). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity).
Subcellular location: Membrane {ECO:0000305|PubMed:21844891}; Peripheral membrane protein {ECO:0000305|PubMed:21844891}; Cytoplasmic side {ECO:0000305|PubMed:21844891}. Lysosome membrane {ECO:0000305|PubMed:30374053}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P61420}; Peripheral membrane protein {ECO:0000305}. Note=Localizes to centrosome and the base of the cilium. {ECO:0000250|UniProtKB:Q6PGV1}.
Interaction partners:
- V-type proton ATPase 116 kDa subunit a 2
- V-type proton ATPase subunit D
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase 16 kDa proteolipid subunit c
- V-type proton ATPase subunit G 1
- V-type proton ATPase subunit H
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit S1
Sequence:
MSFFPELYFNVDNGYLEGLVRGLKAGVLSQADYLNLVQCETLEDLKLHLQSTDYGNFLANEASPLTVSVIDDRLKEKMVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQRSIAELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGRLYPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF
Protein: Deferrochelatase (EC 4.98.1.1) (Peroxidase EfeB) (EC 1.11.1.-) (P31545)
Organism: Escherichia coli (strain K12)
Function: Involved in the recovery of exogenous heme iron. Extracts iron from heme while preserving the protoporphyrin ring intact. Also displays peroxidase activity on guaiacol in vitro.
Subcellular location: Periplasm {ECO:0000269|PubMed:16551627}.
Interaction partners:
- Iron uptake system component EfeO
- Dye-decolorizing peroxidase YfeX
Sequence:
MQYKDENGVNEPSRRRLLKVIGALALAGSCPVAHAQKTQSAPGTLSPDARNEKQPFYGEHQAGILTPQQAAMMLVAFDVLASDKADLERLFRLLTQRFAFLTQGGAAPETPNPRLPPLDSGILGGYIAPDNLTITLSVGHSLFDERFGLAPQMPKKLQKMTRFPNDSLDAALCHGDVLLQICANTQDTVIHALRDIIKHTPDLLSVRWKREGFISDHAARSKGKETPINLLGFKDGTANPDSQNDKLMQKVVWVTADQQEPAWTIGGSYQAVRLIQFRVEFWDRTPLKEQQTIFGRDKQTGAPLGMQHEHDVPDYASDPEGKVIALDSHIRLANPRTAESESSLMLRRGYSYSLGVTNSGQLDMGLLFVCYQHDLEKGFLTVQKRLNGEALEEYVKPIGGGYFFALPGVKDANDYFGSALLRV