wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein Rv2206 (P9WLI5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase
- Adenosylcobinamide-GDP ribazoletransferase
- Uncharacterized protein Rv2205c
- dUTPase
- RNA polymerase-binding protein RbpA
- Protein Rv2204c
Sequence:
MKLLGHRKSHGHQRADASPDAGSKDGCRPDSGRTSGSDTSRGSQTTGPKGRPTPKRNQSRRHTKKGPVAPAPMTAAQARARRKSLAGPKLSREERRAEKAANRARMTERRERMMAGEEAYLLPRDRGPVRRYVRDVVDSRRNLLGLFMPSALTLLFVMFAVPQVQFYLSPAMLILLALMTIDAIILGRKVGRLVDTKFPSNTESRWRLGLYAAGRASQIRRLRAPRPQVERGGDVG
Protein: Polypeptide N-acetylgalactosaminyltransferase 3 (EC 2.4.1.41) (H0ZAB5)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Glycosylates FGF23.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q14435}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q14435}. Note=Resides preferentially in the trans and medial parts of the Golgi stack. {ECO:0000250|UniProtKB:Q14435}.
Interaction partners:
- Glucosaminyl
- alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase
- Fibroblast growth factor 23
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
Sequence:
MALKKAPKLFKTFFHWKLWKFSIIVFVFLVFLFLLQREVGVQDFKDEAGIEPVVGKKSHVLGLVLNAMNNIKGAKPKMQIKAPIRQTKVPGERHCLPGHYTPVELKPFLDRPLQDPNAPGASGKAFKTINLNSEEQKEKQAGEEKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKRCPPLPTTSIIIVFHNEAWSTLLRTVHSVMYTSPAILLKEIILVDDASVDEYLHDKLDEYVKQFQIVKVVRQKERKGLITARLLGASVATGETLTFLDAHCECFYGWLEPLLARIAENPVAVVSPDIASIDLNTFEFSKPSPYGHSHNRGNFDWSLSFGWESLPKHENKRRKDETYPIRTPTFAGGLFSISKDYFEYIGSYDEEMEIWGGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSKSPHTFPKGTQVITRNQVRLAEVWMDEYKEIFYRRNTEAAKIVKQKTFGDISKRIDLRQRLQCKNFTWYLSNVYPEAYVPDLNPLFSGYLKNIGNRMCLDVGENNHGGKPLIMYSCHGLGGNQKELCLHASKGPVQLRECTYKGQKTFAVGEEQWLHQKDQTLYNEALHMCLTGNGEHPSLASCNPSDPFQKWIFGQND
Protein: Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta (Q5SWA0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRPWSSPAQLVAGAQPAGRGDPLGPRPIPPPRFRRASSQREPPYPRPAEPALELAGSKCQPDTPAASLCPADSPSQHRVMPPGPASWANVGSRPHTVANGHELFEVSEERDEEVAAFCHMLDILRSGSDIQDYFLTGYVWSAVTPSPEHLGDEVNLKVTVLCDRLQEALTFTC
Protein: Ras-related protein RABH1c (AtRABH1c) (Q9SMR4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000305|PubMed:19454595}; Lipid-anchor {ECO:0000305|PubMed:19454595}. Cytoplasm, cytosol {ECO:0000269|PubMed:19454595}.
Interaction partners:
- Guanosine nucleotide diphosphate dissociation inhibitor 1
- Vacuolar protein-sorting-associated protein 33 homolog
- Golgin candidate 5
- Guanosine nucleotide diphosphate dissociation inhibitor 2
- Guanosine nucleotide diphosphate dissociation inhibitor At5g09550
- Glutamate receptor 2.3
- Conserved oligomeric Golgi complex subunit 6
- Vacuolar protein sorting-associated protein 52 A
- At5g52210
- Vacuolar protein sorting-associated protein 54, chloroplastic
Sequence:
MASVSPLAKFKLVFLGDQSVGKTSIITRFMYDKFDTTYQPTIGIDFLSKTMYLEDRTVRLQLWDTAGQERFRSLIPSYIRDSSVAIVVYDVSNRQTFLNTSKWIEDVHRERGQSNVIIVLVGNKTDLVEKRQVSISEGEDKGKEYGVMFIETSAKENFNIKALFRKIAAALPGVDSYSLATKSDDMVDVNLKTTSNSSQGEQQGGAGGGGGCSC
Protein: DNA-directed DNA polymerase (EC 2.7.7.7) (EC 3.1.11.-) (Gp43) (Q38087)
Organism: Escherichia phage RB69 (Bacteriophage RB69)
Function: Replicates the viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction for proofreading purpose.
Interaction partners:
Sequence:
MKEFYLTVEQIGDSIFERYIDSNGRERTREVEYKPSLFAHCPESQATKYFDIYGKPCTRKLFANMRDASQWIKRMEDIGLEALGMDDFKLAYLSDTYNYEIKYDHTKIRVANFDIEVTSPDGFPEPSQAKHPIDAITHYDSIDDRFYVFDLLNSPYGNVEEWSIEIAAKLQEQGGDEVPSEIIDKIIYMPFDNEKELLMEYLNFWQQKTPVILTGWNVESFDIPYVYNRIKNIFGESTAKRLSPHRKTRVKVIENMYGSREIITLFGISVLDYIDLYKKFSFTNQPSYSLDYISEFELNVGKLKYDGPISKLRESNHQRYISYNIIDVYRVLQIDAKRQFINLSLDMGYYAKIQIQSVFSPIKTWDAIIFNSLKEQNKVIPQGRSHPVQPYPGAFVKEPIPNRYKYVMSFDLTSLYPSIIRQVNISPETIAGTFKVAPLHDYINAVAERPSDVYSCSPNGMMYYKDRDGVVPTEITKVFNQRKEHKGYMLAAQRNGEIIKEALHNPNLSVDEPLDVDYRFDFSDEIKEKIKKLSAKSLNEMLFRAQRTEVAGMTAQINRKLLINSLYGALGNVWFRYYDLRNATAITTFGQMALQWIERKVNEYLNEVCGTEGEAFVLYGDTDSIYVSADKIIDKVGESKFRDTNHWVDFLDKFARERMEPAIDRGFREMCEYMNNKQHLMFMDREAIAGPPLGSKGIGGFWTGKKRYALNVWDMEGTRYAEPKLKIMGLETQKSSTPKAVQKALKECIRRMLQEGEESLQEYFKEFEKEFRQLNYISIASVSSANNIAKYDVGGFPGPKCPFHIRGILTYNRAIKGNIDAPQVVEGEKVYVLPLREGNPFGDKCIAWPSGTEITDLIKDDVLHWMDYTVLLEKTFIKPLEGFTSAAKLDYEKKASLFDMFDF
Protein: Nuclear factor related to kappaB binding protein (E9PQ59)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDSLDHMLTDPLELGPCGDGHGTRIMEDCLLGGTRVSLPEDLLEDPEIFFDVVSLSTWQEVLSDSQREHLQQFLPQFPEDSAEQQNELILALFSGENFRFGNPLHIAQKLFRDGHFNPEVVKYRQLCFKSQYKRYLNSQQQYFHRLLKQILASRSDLLEMARRSGPALPFRQKRPSPSRTPEEREWRTQQRYLKVLREVKEECGDTALSSDEEATLDLQEQFSFEDLSSWLPSSPARSPSPAVPLRVVPTLSTTDMKTADKVELGDSDLKIMLKKHHEKRKHQPDHPDLLTGDLTLNDIMTRVNAGRKGSLAALYDLAVLKKKVKEKEEKKKKKIKTIKSEAEDLAEPLSSTEGVAPLSQAPSPLAIPAIKEEPLEDLKPCLGINEISSSFFSLLLEILLLESQASLPMLEERVLDWQSSPASSLNSWFSAAPNWAELVLPALQYLAGESRAVPSSFSPFVEFKEKTQQWKLLGQSQDNEKELAALFQLWLETKDQAFCKKMKTAQMPQHLSLGRTDYVVRPSTGEEKRVFQEQERYRYSQPHKAFTFRMHGFESVVGPVKGVFDKETSLNKAREHSLLRSDRPAYVTILSLVRDAAARLPNGEGTRAEICELLKDSQFLAPDVTSTQVNTVVSGALDRLHYEKDPCVKYDIGRKLWIYLHRDRSEEEFERIHQAQAAAAKARKALQQKPKPPSKVKSSSKESSIKVLSSGPSEQSQMSLSDSSMPPTPVTPVTPTTPALPAIPISPPPVSAVNKSGPSTVSEPAKSSSGVLLVSSPTMPHLGTMLSPASSQTAPSSQAAARVVSHSGSAGLSQVRVVAQPSLPAVPQQSGGPAQTLPQMPAGPQIRVPATATQTKVVPQTVMATVPVKAQTTAATVQRPGPGQTGLTVTSLPATASPVSKPATSSPGTSAPSASTAAVIQNVTGQNIIKQVAITGQLGVKPQTGNSIPLTATNFRIQGKDVLRLPPSSITTDAKGQTVLRITPDMM
Protein: ABC transporter B family member 21 (ABC transporter ABCB.21) (AtABCB21) (Multidrug resistance protein 17) (P-glycoprotein 21) (Q9M1Q9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255|PROSITE-ProRule:PRU00441}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase FKBP42
- Cytochrome P450, family 71, subfamily B, polypeptide 32
- Cytochrome P450 like protein
- Cytochrome P450, family 94, subfamily B, polypeptide 2
- At3g62160
Sequence:
MDSVIESEEGLKVDSPNRADAETSNSKIHEEDEKELKTESDLKEEKKKTEKNKQEEDEKTKTVPFHKLFAFADSFDIILMILGTIGAVGNGLGFPIMTILFGDVIDVFGQNQNSSDVSDKIAKVALKFVYLGLGTLVAALLQVSGWMISGERQAGRIRSLYLQTILRQDIAFFDVETNTGEVVGRMSGDTVLIQDAMGEKVGKAIQLVSTFIGGFVIAFTEGWLLTLVMVSSIPLLVMSGAALAIVISKMASRGQTSYAKAAVVVEQTVGSIRTVASFTGEKQAISNYNKHLVSAYRAGVFEGASTGLGLGTLNIVIFCTYALAVWYGGKMILEKGYTGGQVLIIIFAVLTGSMSLGQASPCLSAFAAGQAAAYKMFEAIKRKPEIDASDTTGKVLDDIRGDIELNNVNFSYPARPEEQIFRGFSLSISSGSTVALVGQSGSGKSTVVSLIERFYDPQSGEVRIDGINLKEFQLKWIRSKIGLVSQEPVLFTSSIKENIAYGKENATVEEIRKATELANASKFIDKLPQGLDTMVGEHGTQLSGGQKQRIAVARAILKDPRILLLDEATSALDAESERIVQEALDRIMVNRTTVVVAHRLSTVRNADMIAVIHQGKIVEKGSHSELLRDPEGAYSQLIRLQEDTKQTEDSTDEQKLSMESMKRSSLRKSSLSRSLSKRSSSFSMFGFPAGIDTNNEAIPEKDIKVSTPIKEKKVSFFRVAALNKPEIPMLILGSIAAVLNGVILPIFGILISSVIKAFFKPPEQLKSDTRFWAIIFMLLGVASMVVFPAQTIFFSIAGCKLVQRIRSMCFEKVVRMEVGWFDETENSSGAIGARLSADAATVRGLVGDALAQTVQNLASVTAGLVIAFVASWQLAFIVLAMLPLIGLNGYIYMKFMVGFSADAKRMYEEASQVANDAVGSIRTVASFCAEEKVMKMYKKKCEGPMRTGIRQGIVSGIGFGVSFFVLFSSYAASFYAGARLVDDGKTTFDSVFRVFFALTMAAVAISQSSSLSPDSSKASNAAASIFAVIDRESKIDPSDESGRVLDNVKGDIELRHISFKYPSRPDVQIFQDLCLSIRAGKTIALVGESGSGKSTVIALLQRFYDPDSGQITLDGVEIKTLQLKWLRQQTGLVSQEPVLFNETIRANIAYGKGGDATETEIVSAAELSNAHGFISGLQQGYDTMVGERGVQLSGGQKQRVAIARAIVKDPKVLLLDEATSALDAESERVVQDALDRVMVNRTTVVVAHRLSTIKNADVIAVVKNGVIVEKGKHETLINIKDGVYASLVQLHLSAST
Protein: Fer3-like protein (Basic helix-loop-helix protein N-twist) (Class A basic helix-loop-helix protein 31) (bHLHa31) (Nephew of atonal 3) (Neuronal twist) (Q96RJ6)
Organism: Homo sapiens (Human)
Function: Transcription factor that binds to the E-box and functions as inhibitor of transcription. DNA binding requires dimerization with an E protein. Inhibits transcription activation by ASCL1/MASH1 by sequestering E proteins (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor 12
- Transcription factor 4
- Protein HEXIM2
Sequence:
MAAYPESCVDTTVLDFVADLSLASPRRPLLCDFAPGVSLGDPALALREGRPRRMARFEEGDPEEEECEVDQGDGEEEEEEERGRGVSLLGRPKRKRVITYAQRQAANIRERKRMFNLNEAFDQLRRKVPTFAYEKRLSRIETLRLAIVYISFMTELLESCEKKESG
Protein: Mitotic interactor and substrate of PLK1 (Mitotic spindle positioning protein) (Q8IVT2)
Organism: Homo sapiens (Human)
Function: Plays a role in mitotic spindle orientation and mitotic progression. Regulates the distribution of dynactin at the cell cortex in a PLK1-dependent manner, thus stabilizing cortical and astral microtubule attachments required for proper mitotic spindle positioning. May link microtubules to the actin cytospkeleton and focal adhesions. May be required for directed cell migration and centrosome orientation. May also be necessary for proper stacking of the Golgi apparatus.
Subcellular location: Cell junction, focal adhesion. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Note=Predominantly localizes to cortical actin structures during interphase and mitosis. Present in retraction fibers, which are formed at former adhesion sites during mitosis, and at spicular membrane protrusions in re-attaching cytokinetic cells. Partially colocalizes with cytoplasmic F-actin. Not detected at microtubules at interphase, nor at spindle during mitosis.
Interaction partners:
- Tubby-related protein 4
- MBL associated serine protease 1
Sequence:
MDRVTRYPILGIPQAHRGTGLVLDGDTSYTYHLVCMGPEASGWGQDEPQTWPTDHRAQQGVQRQGVSYSVHAYTGQPSPRGLHSENREDEGWQVYRLGARDAHQGRPTWALRPEDGEDKEMKTYRLDAGDADPRRLCDLERERWAVIQGQAVRKSSTVATLQGTPDHGDPRTPGPPRSTPLEENVVDREQIDFLAARQQFLSLEQANKGAPHSSPARGTPAGTTPGASQAPKAFNKPHLANGHVVPIKPQVKGVVREENKVRAVPTWASVQVVDDPGSLASVESPGTPKETPIEREIRLAQEREADLREQRGLRQATDHQELVEIPTRPLLTKLSLITAPRRERGRPSLYVQRDIVQETQREEDHRREGLHVGRASTPDWVSEGPQPGLRRALSSDSILSPAPDARAADPAPEVRKVNRIPPDAYQPYLSPGTPQLEFSAFGAFGKPSSLSTAEAKAATSPKATMSPRHLSESSGKPLSTKQEASKPPRGCPQANRGVVRWEYFRLRPLRFRAPDEPQQAQVPHVWGWEVAGAPALRLQKSQSSDLLERERESVLRREQEVAEERRNALFPEVFSPTPDENSDQNSRSSSQASGITGSYSVSESPFFSPIHLHSNVAWTVEDPVDSAPPGQRKKEQWYAGINPSDGINSEVLEAIRVTRHKNAMAERWESRIYASEEDD
Protein: Geraniol 8-hydroxylase (EC 1.14.14.83) (Cytochrome P450 76B10) (Geraniol 10-hydroxylase) (SmG10H) (D1MI46)
Organism: Swertia mussotii (Felwort)
Function: Hydroxylase involved in the biosynthesis of hydroxygeraniol, a precursor of the iridoid monoterpenoid swertiamarin.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDFDFLTIAIGFLFTITLYQALNFFSRKSKNLPPGPSPLPLIGNLHLLGDQPHKSLAKLAKKHGPIMGLQLGQVTTIVVTSSGMAKEVLQKQDLAFSSRSIPNAIHAHDQYKYSVIWLPVASRWRGLRKALNSNMFSGNRLDANQHLRSRKVQELIAYCRKSSQTGDAIDVGRAAFRTSLNLLSNTMFSKDLTDPYSDSAKEFKDLVWNVMVEAGKPNLVDYFPLLDKVDPQGIRKRMTIHFGKILELFGGLIDERLQQKKAKGVNDDVLDVLLTTSEESPEEIDRTHIQRMCLDLFVAGTDTTSSTLEWAMSEMLKNPEKMKAAQAELAQVIGKGKAVEEADLARLPYLRCAIKETLRIHPPVPLLIPRRTEQEVEVCGYTVPKNSQVLVNVWAISRDDAIWKDPLSFKPERFLESELEMRGKDFELIPFGAGRRICPGLPLAVRMVPVMLGSLLNSFDWKLEGGIAPKDLDMEEKFGITLQKAHPLRAVATPL
Protein: Protein FATTY ACID EXPORT 2, chloroplastic (At-FAX2) (Q94A32)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in free fatty acids export from the plastids.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein FATTY ACID EXPORT 4, chloroplastic
- Protein FATTY ACID EXPORT 1, chloroplastic
- Protein FATTY ACID EXPORT 3, chloroplastic
- ABC transporter A family member 9
- Mitochondrial pyruvate carrier 1
- Protein TRIGALACTOSYLDIACYLGLYCEROL 4, chloroplastic
- La protein 2
- Protein TRIGALACTOSYLDIACYLGLYCEROL 1, chloroplastic
- Protein TRIGALACTOSYLDIACYLGLYCEROL 2, chloroplastic
Sequence:
MADLILSSSSAQSSLLHVRPNHYLLNTSTASPIRSVRFQNSNGFHPLAFASGHRRLPLGAVVPSDSTKTITSTITANCVDSGVKAVEVEPTIDYGGGGGIGGDKFGGGGGGGDGNDDGGEDDKEESDGKKSTPLSMSQKLTLGYAFLVGVGGLMGYLKSGSQKSLLAGGLSAAVLLYVFSQLPTKPVLASTVGVVMAGALMYVMGTRYMRSKKIFPAGVVSIMSFIMTGGYIHGIMRSLH
Protein: Zinc finger MYND-type containing 11 (E7ENI9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MARLTKRRQADTKAIQHLWAAIEIIRNQKQIANIDRITKYMSRVHGMHPKETTRQLSLAVKDGLIVETLTVGCKGSKAGIEQEGYWLPGDEIDWETENHDWYCFECHLPGEVLICDLCFRVYHSKCLSDEFRLRDSSSPWQCPVCRSIKKKNTNKQEMGTYLRFIVSRMKERKVNEGKYRSYEEFKADAQLLLHNTVIFYGADSEQADIARMLYKDTCHELDELQLCKNCFYLSNARPDNWFCYPCIPNHELVWAKMKGFGFWPAKVMQKEDNQVDVRFFGHHHQRAWIPSENIQDITVNIHRLHVKRSMGWKKACDELELHQRFLREGRFWKSKNEDRGEEEAESSISSTSNEQLKVTQEPRAKKGRRNQSVEPKKEEPEPETEAVSSSQEIPTMPQPIEKVSVSTQTKKLSASSPRMLHRSTQTTNDGVCQSMCHDKYTKIFNDFKDRMKSDHKRETERVVREALEKLRSEMEEEKRQAVNKAVANMQGEMDRKCKQVKEKCKEEFVEEIKKLATQHKQLISQTKKKQWCYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRRKR
Protein: Probable 3-deoxy-manno-octulosonic acid transferase (Kdo transferase) (EC 2.4.99.15) (Lipopolysaccharide core biosynthesis protein WaaZ) (P27241)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12591884}. Note=When overexpressed, a significant amount is also located in the membrane fraction. {ECO:0000269|PubMed:12591884}.
Interaction partners:
- Lipopolysaccharide core biosynthesis protein WaaS
- Putative lipopolysaccharide heptosyltransferase 4
- Lipopolysaccharide core heptose
- Lipopolysaccharide 1,2-glucosyltransferase
- Lipopolysaccharide 1,6-galactosyltransferase
- Lipopolysaccharide glucosyltransferase WaaO
- Lipopolysaccharide core heptose
- Lipopolysaccharide glucosyltransferase WaaG
- Lipopolysaccharide heptosyltransferase 3
- O-antigen ligase
Sequence:
MKNIRYIDKKDVENLIENKISDDVIIFLSGPTSQKTPLSVLRTKDIIAVNGSAQYLLSNNIVPFIYVLTDVRFLHQRRDDFYKFSQRSRYTIVNVDVYEHASKEDKLYILQNCLVLRSFYRREKGGFIKKIKFNILRQIHKELLISVPLSKKGRLVGFCKDISLGYCSCHTIAFAAIQIAYSLKYARIICSGLDLTGSCSRFYDENKNPMPSELSRDLFKILPFFRFMHDNVKDINIYNLSDDTAISYDVIPFIKLQDISAEESKDMTRKKMQYRTSTDSYAN
Protein: Autophagy-related protein 8f (Autophagy-related ubiquitin-like modifier ATG8f) (AtAPG8f) (Protein autophagy 8f) (Q8VYK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin-like modifier involved in autophagosomes formation. May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:16157655}; Lipid-anchor {ECO:0000269|PubMed:16157655}. Vacuole membrane {ECO:0000269|PubMed:16157655}; Lipid-anchor {ECO:0000269|PubMed:16157655}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q8LEM4}.
Interaction partners:
- Protein NBR1 homolog
- Ubiquitin-like modifier-activating enzyme atg7
- Autophagy-related protein 3
- Cysteine protease ATG4a
- Cysteine protease ATG4b
- ATG8-interacting protein 1
- Serine/threonine-protein kinase ATG1c
- Serine/threonine-protein kinase ATG1b
- Ubiquitin-like protein ATG12A
- Beclin-1-like protein
Sequence:
MAKSSFKQEHDLEKRRAEAARIREKYPDRIPVIVEKAEKSDIPTIDKKKYLVPADLTVGQFVYVIRKRIKLSAEKAIFIFVDNVLPPAGALMSSVYEEKKDDDGFLYVTYSGENTFGFGSP
Protein: Tubulin alpha-2 chain (EC 3.6.5.-) (P24634)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin beta-1 chain
- Tubulin beta-2 chain
- Acid phosphatase, putative
- Dynein heavy chain, cytoplasmic
- Tubulin alpha-1 chain
- RNase H type-1 domain-containing protein
- Calponin-homology domain protein
- Cytoplasmic dynein intermediate chain
- Mis6 domain protein
- Kinesin-like protein bimC
Sequence:
MRGEVCHIHIGQAGTQLGNSAWELYLLEHGLGADGRLDPEKGEDINAGGSFETFFTETGSGKYVPRSIFVDLDPSPIDEIRTGPYRQLFHPEQLISGKEDAANNYARGHYTVGKELVDTVVDRVRRLSDNCSSLQGFLVFHSFGGGTGSGFGALLLERLSTEYGKKSKLEFAVYPSPRVSTAVVEPYNAVLSTHSTIENSDCTFLVDNEAVYDICRRNLDIPRPSFEHLNRLIAQVVSSITSSLRFDGALNVDLNEFQTNLVPFPRIHYPLISYAPVISSNRSSHESFKVQDLTLQCAEPNNQMVVCDPRNGKYMAVALLYRGDCVPRDCTQAIASLKAKASFNLVEWCPTGFKVGINYQKPARVPGSELAPVDRSVSMLSNTTAISEAWSRLDHKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVAGDSLDMEGEEAEY
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q380W1)
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:
MLPFSGEQQRLSAHTVTLLTLCFTTILRLAKPSTNGFNEAKITQLCGTAMAIQDTAAVAIGRLQKLHRQEQAAAEARNKLLLAALVVPTVNDTILFTAAARAAENCRVDATTKAAGNVAAGVTAAANGAHVAGRLTELVAILQATTKSDTARKCITQANTRTTKLTSPAEFGCPTTITDEYAPKLNLDSSEITNKGLAKYSGPTQLQDATGNNVCAFMLGSNADNTALWQYSGSATPATVGADLITVSPHTGSGATATIAVANALGTDYQAPDSATAAKKLFTAIGKVMKLPESTCPETTEKAISEALTTTTIKAEVKDLLIKLGKVTNTMADQAARSLIGQAVKDDNAASTARVNQVNKLKVKKIDGGKPKEVKIETLTDPPEITTALLIAIPELKAKADRTVASEPAKDCSTNGGIQEENKECSKKTGDDCKDGCKLTGEGENKKCVKDTYFVKKEVEGGEKDSKTGTTNTTGSNSFVIHKVPLLLAFLLDFINL
Protein: WbcM protein (Q56916)
Organism: Yersinia enterocolitica
Interaction partners:
Sequence:
MKKIAFFGGDISHTGGTERVSITLANYLVKNGYQVVIISLSGNKPPKFPVDESIKLVSLFDEKRRFSLAYFSVVVRLRRILVDESIDILIDVDTMLALFSTTALLGTKIKHISWEHFNYKSNLNIKSRKLARKIAAKYSDAVVTLQRRSWLLARRKQISRKNNIYIQPFAFWNPKIKLTKRNSQIVLALGRLTNIKGFDLLLDIWVKVEEQSSNWKLIIAGDGEDKNLLLDKIKEFNLKNVELLPSTLHVSDLYDQSAIYAMTSRFEGFPMVLLEAKASGLPIIAYDCDTGPSELIINNEDGLLIPFSDSNAFARQLILLMNDDDLRESMSLRSLKNAEKYKIEVAIGDKWKSLIEKI
Protein: Smad anchor for receptor activation-like Smad-binding domain-containing protein (Q3UXU9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSVNEEQRYLSNIVKVLMSIFCNPFTLIVSVFALAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGTEGRGSCAVLSFSSPCSSERC
Protein: GA-binding protein subunit beta-1 (GABP subunit beta-1) (GABPB-1) (GABP subunit beta-2) (GABPB-2) (Q00420)
Organism: Mus musculus (Mouse)
Function: Transcription factor capable of interacting with purine rich repeats (GA repeats). Acts as a a master regulator of nuclear-encoded mitochondrial genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q06547}.
Interaction partners:
- GA-binding protein alpha chain
- Caspase-2
- Tumor protein 63
- Cathepsin B
Sequence:
MSLVDLGKKLLEAARAGQDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNPESPDTVTIHAATPQFIIGPGGVVNLTDETGVSAVQFGNSSTSVLATLAALAEASAPLSNSSETPVVATEEVVTAESVDGAIQQVVSSGGQQVITIVTDGIQLGNLHSIPTSGMGQPIIVTMPDGQQVLTVPATDIAEETVISEEPPAKRQCMEIIESRVECAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTRIQTNKEAV
Protein: Transcription initiation factor TFIID subunit 5 (TAFII-90) (TBP-associated factor 5) (TBP-associated factor 90 kDa) (P38129)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the DNA-binding general transcription factor complex TFIID and the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, chromatin modification (histone acetylation by TAF1), facilitation of DNA opening and initiation of transcription. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SAGA complex subunit SGF29
- SAGA complex subunit SPT8
- Transcription initiation factor TFIID subunit 2
- SAGA complex subunit HFI1
- SAGA complex/transcription factor TFIID complex subunit TAF6
- Transcription initiation factor TFIID subunit 8
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 3
- SAGA complex subunit NGG1
- SAGA complex subunit SPT20
Sequence:
MSQKQSTNQNQNGTHQPQPVKNQRTNNAAGANSGQQPQQQSQGQSQQQGRSNGPFSASDLNRIVLEYLNKKGYHRTEAMLRAESGRTLTPQNKQSPANTKTGKFPEQSSIPPNPGKTAKPISNPTNLSSKRDAEGGIVSSGRLEGLNAPENYIRAYSMLKNWVDSSLEIYKPELSYIMYPIFIYLFLNLVAKNPVYARRFFDRFSPDFKDFHGSEINRLFSVNSIDHIKENEVASAFQSHKYRITMSKTTLNLLLYFLNENESIGGSLIISVINQHLDPNIVESVTAREKLADGIKVLSDSENGNGKQNLEMNSVPVKLGPFPKDEEFVKEIETELKIKDDQEKQLNQQTAGDNYSGANNRTLLQEYKAMNNEKFKDNTGDDDKDKIKDKIAKDEEKKESELKVDGEKKDSNLSSPARDILPLPPKTALDLKLEIQKVKESRDAIKLDNLQLALPSVCMYTFQNTNKDMSCLDFSDDCRIAAAGFQDSYIKIWSLDGSSLNNPNIALNNNDKDEDPTCKTLVGHSGTVYSTSFSPDNKYLLSGSEDKTVRLWSMDTHTALVSYKGHNHPVWDVSFSPLGHYFATASHDQTARLWSCDHIYPLRIFAGHLNDVDCVSFHPNGCYVFTGSSDKTCRMWDVSTGDSVRLFLGHTAPVISIAVCPDGRWLSTGSEDGIINVWDIGTGKRLKQMRGHGKNAIYSLSYSKEGNVLISGGADHTVRVWDLKKATTEPSAEPDEPFIGYLGDVTASINQDIKEYGRRRTVIPTSDLVASFYTKKTPVFKVKFSRSNLALAGGAFRP
Protein: 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component (3-ketosteroid-9-alpha-hydroxylase, ferredoxin reductase component) (KSH) (Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase) (EC 1.14.15.30) (Rieske-type oxygenase) (RO) (B6V6V6)
Organism: Rhodococcus rhodochrous
Function: Probably involved in the degradation of cholesterol. In vitro, catalyzes the introduction of a 9alpha-hydroxyl moiety into the ring B of 3-ketosteroid substrates such as 1,4-androstadiene-3,17-dione (ADD), 4-androstene-3,17-dione (AD), 4-androstene-17beta-ol-3-one (testosterone), 4-pregnene-3,20-dione (progesterone), 19-nor-4-androstene-3,17-dione (nordion), 1-(5alpha)-androstene-3,17-dione, 5alpha-androstane-3,17-dione and 5beta-androstane-3,17-dione. KSH has the highest activity with 3-keto-Delta4 steroid substrates.
Interaction partners:
- 3-ketosteroid-9-alpha-monooxygenase, oxygenase component
- 3-ketosteroid-9-alpha-monooxygenase, oxygenase component
- 3-ketosteroid-9-alpha-monooxygenase, oxygenase component
- Unannotated protein.
- Unannotated protein
- Unannotated protein.
- Unannotated protein
- Unannotated protein.
- Unannotated protein.
- Unannotated protein.
Sequence:
MTTVEVPHGSRSVILTVSAVVEETADTRSIVFAVPDELRDKFAYRPGQFLTLRIPSDRTGSVARCYSLASSPFTDDAPKVTVKRTSDGYGSNWLCDNIATGQTLEVLPPAGVFTPKSLDHDFLLFGAGSGITPVISILKSALTQGGGKVVLVYANRDEKSVIFAEELRALAEKYPTRLTVVHWLESVQGLPTADQLAAIAAPYESYEAFMCGPGPFMDTVHQALNTVGMPRARVHAEVFNSLSGDPFADQAPVEVSDEDAADAATVEVELDGEVHKLSWPRKQTLVDIMLAKGIDVPYSCQEGECGSCACTVLEGKVEMENCDVLDPEDIEAGYILGCQARPVTDHLKIEF