wanglab/gogpt-training-data huggingface dataset:
Protein: Sec-independent protein translocase protein TatC (P69423)
Organism: Escherichia coli (strain K12)
Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00902, ECO:0000269|PubMed:11591389, ECO:0000269|PubMed:15225613, ECO:0000269|PubMed:20169075}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00902, ECO:0000269|PubMed:11591389, ECO:0000269|PubMed:15225613, ECO:0000269|PubMed:20169075}. Note=Localizes at the cell poles.
Interaction partners:
- Sec-independent protein translocase protein TatA
- Sec-independent protein translocase protein TatB
- Sec-independent protein translocase protein TatE
- Cell division protein FtsP
- 3'-5' ssDNA/RNA exonuclease TatD
- Trimethylamine-N-oxide reductase 1
- Protein translocase subunit SecA
- Membrane protein insertase YidC
- Multicopper oxidase CueO
- Flagellar regulator flk
Sequence:
MSVEDTQPLITHLIELRKRLLNCIIAVIVIFLCLVYFANDIYHLVSAPLIKQLPQGSTMIATDVASPFFTPIKLTFMVSLILSAPVILYQVWAFIAPALYKHERRLVVPLLVSSSLLFYIGMAFAYFVVFPLAFGFLANTAPEGVQVSTDIASYLSFVMALFMAFGVSFEVPVAIVLLCWMGITSPEDLRKKRPYVLVGAFVVGMLLTPPDVFSQTLLAIPMYCLFEIGVFFSRFYVGKGRNREEENDAEAESEKTEE
Protein: Taste receptor type 2 (H0ZSM0)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004424}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004424}.
Interaction partners:
Sequence:
MEACHSSQQSNVTSYGVMSLAIISLEVFASVWINAFLVCVLCIAWVKKKTLNSNEKILLLLGCSRISFLCFSWVNYFLSIIYPNCLYVCPIFQVLASSSTFFNYSSLWVSACLCCFYCIKIANFRNRFFIYLKVKIDRMVPWLLLGSGILALASCIVIYDITETLQSSNFTFTFQENFWEARITMDKHFFSSFFLAGFGYAASFTAVIFSAVFLLFSLWRHKHKMQTNSMKDLSMDAHIRAMKSILSFLVMYSINFVCLILSIIYSMMNENTTILISIYLCAFPGIHSLILIFSNPKLEKALLKILSYVKCKFFTK
Protein: Peroxisome biogenesis factor 2 (EC 2.3.2.27) (EC 2.3.2.36) (Peroxin-2) (Peroxisomal membrane protein 3) (Peroxisome assembly factor 1) (PAF-1) (P55098)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (By similarity). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane (By similarity). PEX2 also regulates peroxisome organization by acting as a E3 ubiquitin-protein ligase (By similarity). PEX2 ubiquitinates PEX5 during its passage through the retrotranslocation channel: catalyzes monoubiquitination of PEX5 at 'Cys-11', a modification that acts as a signal for PEX5 extraction into the cytosol (By similarity). Required for pexophagy in response to starvation by mediating ubiquitination of peroxisomal proteins, such as PEX5 and ABCD3/PMP70 (By similarity). Also involved in the response to reactive oxygen species (ROS) by mediating 'Lys-48'-linked polyubiquitination and subsequent degradation of PNPLA2/ATGL, thereby regulating lipolysis.
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:P28328}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Peroxisome assembly protein 12
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PEX14
- Peroxisomal biogenesis factor 19
- Peroxisomal targeting signal 1 receptor
- Peroxisomal targeting signal 2 receptor
- ATP-binding cassette sub-family D member 3
- Peroxisomal membrane protein 11B
- Peroxisomal ATPase PEX6
Sequence:
MAAREESTQSANRVLRISQLDALELNKALEQLVWSQFTQCFHGFKPGLLARFEPEVKAFLWLFLWRFTIYSKNATVGQSVLNIQHKNDSSPNPVYQPPSKNQKLLYAVCTIGGRWLEERCYDLFRNRHLASFGKAKQCMNFVVGLLKLGELMNFLIFLQKGKFATLTERLLGIHSVFCKPQNMREVGFEYMNRELLWHGFAEFLIFLLPLINIQKLKAKLSSWCTLCTGAAGHDSTLGSSGKECALCGEWPTMPHTIGCEHVFCYYCVKSSFLFDIYFTCPKCGTEVHSVQPLKAGIQMSEVNAL
Protein: Major heat shock 70 kDa protein Ab (Heat shock protein 70Ab) (HSP70-87A7) (P02825)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPAIGIDLGTTYSCVGVYQHGKVEIIANDQGNRTTPSYVAFTDSERLIGDPAKNQVAMNPRNTVFDAKRLIGRKYDDPKIAEDMKHWPFKVVSDGGKPKIGVEYKGESKRFAPEEISSMVLTKMKETAEAYLGESITDAVITVPAYFNDSQRQATKDAGHIAGLNVLRIINEPTAAALAYGLDKNLKGERNVLIFDLGGGTFDVSILTIDEGSLFEVRSTAGDTHLGGEDFDNRLVTHLADEFKRKYKKDLRSNPRALRRLRTAAERAKRTLSSSTEATIEIDALFEGQDFYTKVSRARFEELCADLFRNTLQPVEKALNDAKMDKGQIHDIVLVGGSTRIPKVQSLLQDFFHGKNLNLSINPDEAVAYGAAVQAAILSGDQSGKIQDVLLVDVAPLSLGIETAGGVMTKLIERNCRIPCKQTKTFSTYADNQPGVSIQVYEGERAMTKDNNALGTFDLSGIPPAPRGVPQIEVTFDLDANGILNVSAKEMSTGKAKNITIKNDKGRLSQAEIDRMVNEAEKYADEDEKHRQRITSRNALESYVFNVKQAVEQAPAGKLDEADKNSVLDKCNDTIRWLDSNTTAEKEEFDHKLEELTRHCSPIMTKMHQQGAGAGAGGPGANCGQQAGGFGGYSGPTVEEVD
Protein: Uncharacterized protein (Q57ZB3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSTGAELLSKALQLQHTRCETYRLWDAKFHCALGGALSASDFETAVNNSIIAAFRCVSLSFRELQCLCRDSTDDACRFLCVWIDELQELEQRHYNISVQFAQLVVQHCTALPLHSSTSQTDMCQTAANEEAENSGVENGSKEVQGTADVSENEKSTVANGERNNSSEVICASLHDRQLCELQRIIPLQAQSVLNYVTCRDDFFPSSSDDECEGDQTGGDGCTSNGADSEPGDLLVPFHHKSGVVATYSPGEVKKRCATFNAAVMPLWRSKLRLRQQLQEKMDELQEEITSASSVFP
Protein: Dynactin subunit 1 (E2JKZ0)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}.
Interaction partners:
- Probable dynactin subunit 2
- Dynactin subunit 5
- Actin-related protein 10
- Dynactin subunit 4
- Actin
- Dynactin subunit 6
- Dynein heavy chain, cytoplasmic
- WD_REPEATS_REGION domain-containing protein
- F-actin-capping protein subunit beta
- F-actin-capping protein subunit alpha
Sequence:
MSFEIGTRVKTSSGNGRVVFCGQTQFAEGDWVGVILDTATGKNNGTVQNVQYFECEPNFGVFVKSSAVELEDASKRSGLKAPAASAIRKDSSVMSRSAGSKASPGSSPGMSPAASSEKLTGRQTGMGPRSMSKLADPNEKKRSTTPQKARSPAPPMTKKNSESTSRMVREFSNLSQSSVASSRASASASKPRPQFTAPDPRRQSLAPPKKASTTTAPVSKPSLSKPRQSLAPSKPAEVTPQKPVPAAQASEAGDPPNELPLPTMTESGTELPKESVLSRAKKIDDTGPAAPMSPLSTTAAARPRTTSVSSSAQESSTEIEYLRNQVKELTEKLEAARVKRKEDHTKVMELDRVSFELRSSEEVRSRLIQKITELEKQIGDERIAKEQLQAWQDENKVLLSDHQDTMEMATIEKELAEERADSLQNDVLTLTEKLESMETELEILKEEMANGGGAAQVGNSVQMKQIEIQNDKLKDALIKLRDLNAQATLDRQKAVDEAERLKTENSELIRVAENLKRQTEIAESKIAGFQEQIDAAMGAEAMVTQLTDKNFNMEERIMQLEETIEDMEEARDLDEQLAEVQKQQVKDLMKEIEQLKIHIHELNGRIRDEQKHAVDLSQTILKFRERMANLNSQIQDQKDQVLSLEEQLHGHISVDNDRASMVNQLQISANRNFAEDVERQVNAIEVEFARRQAGYLKAFLPDNFSRVGGENDSILLVVMLPRLAAKTKLFASLAAQCFPQVPGGMRREHVTKSHKGEQWAHVARVNYLANSINAALGKLESAIGETTVEVLIKLTETYGEMSTHEKTVDQYLELLKKSRFDENTSLDSFVRPLVYFQNMFSLHIGGDGFNAAHWVSEICASLSAGLAYCRVNTQRISYFLQESITAGEVYNMLQTLNDEFAACESVILKAYRLLPGNVSGSEQKILKLESEFTEDLLNSVVQLDKMVSILQEVCANGALSFGGISETEGFDEKRVKEMINAVLGKQDGYIAIDKTFDPIRALIKSLRDSLEKVNSTLESAKMEHSAPEKKSFPPLLDRAHHRKQAAQEAEGLRWQMEKKDNEMLELRKQMKARIEDVSNYKLRLDMAESRLNSTDKAEGDKVKHLEEKINQMVADHRRKQIEYDESMDALQREMKEVESDNLELKQRANKISKEALWKNIQSMETRSSGSPSVPMSTSIDEGGASRGEVVFLENQLNKQTNARKRAELEVRKLKGELAQAGSKRFSAVPGLISGPITLESQTRQDLLLKLIDNLHDESLRLRREEVNHQAYVPSNPKISTEKMVEEMEIFNVKREQFFDKLNSVNRRLRRVWFDAWGEEYPFEIAAKSRPIVAVPEPKKFEEISAKWGIVW
Protein: Calcium channel, voltage-dependent, beta 4b subunit (Voltage-dependent L-type calcium channel subunit beta-4b isoform 2) (Voltage-gated calcium channel beta-4 subunit variant 2) (B0F0D1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Calcium channel, voltage-dependent, P/Q type, alpha 1A subunit, b.
- Calcium channel, voltage-dependent, alpha2/delta subunit 3
- Calcium voltage-gated channel auxiliary subunit alpha2delta 3.
- Voltage-dependent N-type calcium channel subunit alpha
- Potassium voltage-gated channel, shaker-related subfamily, beta member 2 a.
- Calcium channel, voltage-dependent, alpha 2/delta subunit 2a
- Voltage-dependent calcium channel gamma-1 subunit
- Voltage-dependent calcium channel gamma-1 subunit
- Calcium channel, voltage-dependent, alpha 2/delta subunit 1a
- Si:dkey-266j7.2.
Sequence:
MSRHIYIRNKIGEGIQAPIFQVNRGTYSRRSRLKRSDGSTTSTSFILRQGSADSYTSRPSDSDVSLEEERPEGGSQGRQEREQQAQLQLERAKAKAVAFAVKTNVSYCGALDEDVPVPGTAISFDAKDFLHIKEKFNNDWWIGRLVKEGCEIGFIPSPLKLENIRAQLEQKKSRVQGKSSGSSSSSLGDVMSSGKQKQKVTEHVAPYDVVPSMRPVVLVGPSLKGYEVTDMMQKALFDFLKHRFDGRITITRVTADISLAKRSVLNNPSKRAIIERSNTRSSLAEVQSEIERIFELARSLQLVVLDADTINHPAQLMKTSLAPIIVHVKVSSPKVLQRLIKSRGKSQSKHLNVQLVAADKLAQCPPEMFDIILDENQLEDACEHLAEYLEAYWKATHTSSSTPLNPLLGRNLGPAALAPYTTSAISGLQNQQGQKTRHANHTGDHSTPNERRNLMTSDENYHNERAHKGRNRGSSGSQHGGSGRDHHYMEEQQGYQDPYQDTYKPHRNRSSPGSYSQDSRHRL
Protein: Glutathione S-transferase (EC 2.5.1.18) (A0A140VKE3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSMTLGYWDIRGLAHAIRLLLEYTDSSYEEKKYTMGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILCYIARKHNLCGETEEEKIRVDILENQAMDVSNQLARVCYSPDFEKLKPEYLEELPTMMQHFSQFLGKRPWFVGDKITFVDFLAYDVLDLHRIFEPNCLDAFPNLKDFISRFEGLEKISAYMKSSRFLPKPLYTRVAVWGNK
Protein: Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 4 (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase 4) (NDST-4) (N-heparan sulfate sulfotransferase 4) (N-HSST 4) [Includes: Heparan sulfate N-deacetylase 4 (EC 3.-.-.-); Heparan sulfate N-sulfotransferase 4 (EC 2.8.2.-)] (Q9EQW8)
Organism: Mus musculus (Mouse)
Function: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Has low deacetylase activity but high sulfotransferase activity.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Heparan sulfate 2-O-sulfotransferase 1
- D-glucuronyl C5-epimerase
- Heparan-sulfate 6-O-sulfotransferase 3
Sequence:
MNLILKFRRSFRTLIVLLATFCLVSILISAYFLYSGYKQEMTLIETTAEAECADIKDLPYRSIELRTIKPIDTSKTDPTVLLFVESQYSQLGQDIIAILESSRFQYQMVIAPGKGDIPPLTDSGKGKYTLIIYENILKYVSMDSWNRELLEKYCIEYSVSIIGFHKANENSLPTTQLKGFPLNLFNNVALKDCSVNPQSPLLHITKGPKVEKGPLPGEDWTIFQYNHSTYQPVLLTELQSEKSLSFLSSQTLYATIIQDLGLHDGIQRVLFGNNLNFWLHKLIFIDAISFLSGKRLTLSLDRYILVDIDDIFVGKEGTRMNVKDVKALLETQNLLRTQVANFTFNLGFSGKFYHTGTEEEDEGDDLLLRSVDEFWWFPHMWSHMQPHLFHNESSLVEQMILNKEFALEHGIPINLGYAVAPHHSGVYPVHIQLYAAWKKVWGIQVTSTEEYPHLKPARYRKGFIHNSIMVLPRQTCGLFTHTIFYKEYPGGPQELDKSIKGGELFLTILLNPISIFMTHLSNYGNDRLGLYTFVNLANFVHSWTNLKLQTLPPVQLAHKYFELFPEQKDPLWQNPCDDKRHKDIWSREKTCDHLPKFLVIGPQKTGTTALYLFLLMHPSIISNLPSPKTFEEVQFFNGNNYHKGIEWYMDFFPTPSNITSDFLFEKSANYFHSEEAPKRAASLVPKAKIITILIDPSDRAYSWYQHQRSHEDPAALRFNFYEVITTGHWAPPDLKTLQRRCLVPGWYAVHIERWLAYFSTSQLLIIDGQQLRSDPATVMDEVQKFLGVTPHYNYSEALTFDPQKGFWCQLLEGGKTKCLGKSKGRKYPPMDSESRTFLSSYYRDHNVELSKLLHRLGQPLPSWLRQELQKVR
Protein: ABC multidrug transporter SNQ2 (Q6FQN3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: ABC multidrug transporter involved in the response to azoles such as fluconazole, itraconazole, ketoconazole and voriconazole and contributes to the development of PDR1-dependent azole resistance. Plays a role in biofilm tolerance to fluconazole. Confers also resistance to 4-nitroquinoline-N-oxide (4-NQO).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome G complete sequence
- Transcription factor PDR1
- Lanosterol 14-alpha demethylase
Sequence:
MSSSSEISVAGSDVSFEGRLTQHGRHEETPADQLTKILSGRSHEDADGDDAHSDNRSILSRSRRSSTAELSPEMVGRVQSLADVLSRHTSRSGGNIDLSQLSESDRFDAERIIGSFVRDADEQGIHLRKAGVTLEHVSARGADSTAMEGATFGNVLCLPYTIYKAIRDKSGSKMRTILNDVSGLARAGEMVLVLGRPGAGCSSMLKVTAGEIDQFAGGVEGEIMYDGIPQKEMMKRYKPDVIYNGEQDVHFPHLTVQQTLDFAIACKTPSKRVNDVSREEYIASTRDLHATIFGLRHTYHTKVGNDFVRGVSGGERKRVSIAEALVTKGSIYCWDNATRGLDASTALEYAKAIRITTNLLGSTAFVTIYQASENIYETFDKVTVLYTGRQIYFGPIDEAKDYFYRMGYECPPRQVTAEFLTALTDVNGYHKIRPGYENKVPRTAEEFERYWQESPEYRQLLIDIDQYKKEIDTEKTKEIYDQSMQQEKSKHARKKSYYTVSFWEQIRLCTKRGFQRIYGDKAYTVITICSAIIQSLVSGSLYYNTPSSTSGAFSRGGVLYFCLLYYSLMGLANLSFEHRPILQKHKIYSLYHPAAEALGSTIANFPFRMIGMTCFLIIIYFLSGLNRTASSFFRVYLFLTMCSESINALFELIAAGCDNISQANSISGIVMMSISLYSTYMIQLPSMRPWFKWISYILPIRYAFESMLLAEFHGRHMGCGGTLVPSGPGYENIASENQVCAFVGSKPGQSWVLGDDYLRLQFEYEYKHEWRNFGIMWCFLLGYIALKALITEIKRPVKGGGDALIFKKGTRKYHMKLDEEDGELHEIDTKEKFSSRSGSSTTSEDEIFEELESKGIFIWRNVCYTIPYDGGMRQLLDNVSGFCKPGTLTALMGESGAGKTTLLNTLAQRNVGIITGDMLVNGKPIDISFERRTGYVQQQDIHISELTVRESLQFSARMRRAQNVPEEEKMEHVERIIKVLDMEEYADALVGDVGRGLNVEQRKKLSIGVELVAKPDLLLFLDEPTSGLDSQSSWAIVQLLKKLAKAGQSILCTIHQPSATLFEEFDRLLLLKKGGQTVYFGDIGDNSKTLLSYFERNGARKCSPSENPAEYILEAIGAGATASVTEDWHQIWKNSDEFISTEKEVDHLIDQLSNQKTESEFGDAPTKYATSYAYQFKWVLIRTSMSLWRNLDYIMSKMMLMTVGGLYIGFTFYDPGDSYTGLQNTLFAAFISIILSAPAMNQIQARAIAARELFEVRESKSNMFHWSLLLITQYLSEIPYHFLFSAIFFVSSYFPLRTHFQASASAVYYLNYSIMFQLYYIGFGLCVLYMAPNLQSANVILGLCLSFLIAFCGVVQPVSLMPGFWTFMWKTSPYTYFVQNMVGILLHNKPVICRKKELSIFDPPAGQTCQEFTQAFLDKRGGYIANPNATTACEYCIYEVGDDYLKHISASYSYLWRNFGLYWAYIGFNICAMVAIYYIFHVRGVSFKFDRVFKLFSRITRRGKKSN
Protein: Receptor for retinol uptake STRA6 (Retinol-binding protein receptor STRA6) (Stimulated by retinoic acid gene 6 protein homolog) (Q4QR83)
Organism: Rattus norvegicus (Rat)
Function: Functions as retinol transporter. Accepts all-trans retinol from the extracellular retinol-binding protein RBP4, facilitates retinol transport across the cell membrane, and then transfers retinol to the cytoplasmic retinol-binding protein RBP1. Retinol uptake is enhanced by LRAT, an enzyme that converts retinol to all-trans retinyl esters, the storage forms of vitamin A. Contributes to the activation of a signaling cascade that depends on retinol transport and LRAT-dependent generation of retinol metabolites that then trigger activation of JAK2 and its target STAT5, and ultimately increase the expression of SOCS3 and inhibit cellular responses to insulin. Important for the homeostasis of vitamin A and its derivatives, such as retinoic acid. STRA6-mediated transport is particularly important in the eye, and under conditions of dietary vitamin A deficiency. Does not transport retinoic acid.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q0V8E7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q0V8E7}. Note=In the retinal pigment epithelium localizes to the basolateral membrane. {ECO:0000250|UniProtKB:Q0V8E7}.
Interaction partners:
- Retinol-binding protein 1
- Retinol-binding protein 4
- Transthyretin
- Lecithin retinol acyltransferase
- Cytochrome P450 26A1
- Retinol dehydrogenase 10
- Cytochrome P450 26B1
- Retinaldehyde dehydrogenase 3
Sequence:
MESQASENGSQTSSGVTDDYSSWYIEEPLGAEEVQPEGVNPLCQPTVPPALHHACLASLSLLALLLLALLVRRRRLWPHCAHCRPGLPSPVDFLAGNRSWTVPTAVFVALFSNLCLLLPDENPLPFLNRTAASSPDGEPETSRGPWKLLALLYYPALYYPLAACATAGHRAAYLLGTVLSWVHVSVQVWQRAECPQDPKIYKHYSLLASLPLLLSLGFLSLWYPVQVVQSIRHRTGAGSQGLQTSYSEKYLRALLCPKKLDSCSHPASKRSLLSRAWAFSQHSIYTPEPGFCLPLKLVISATLTGTATYQVALLLLVSVVPTVQKVRAGITTDVSYLLAGFGIVLSEDRQEVVELVKHHLWAVEACYISALVLSCSLTFLLLIRSLRTHRANLKALHRGAALDLGPPLQSTHPSRQAIVCWMSFSAYQTAFSCLGLLVQQVIFFLGTTILAFLVFVPLLHGRNLLLLRSLESTWPFWLTLVLAVILQNIAANWVFLESHHGYPELTNRRMLCVATFLLFPINMLVGAIMAIWRVLLSSLYNTVHLGQMDLSLLPQRAASLDPGYHTYRNFLRIEASQSHPGVIAFCALLLHVPSPQPQPPLAPQDSLRPAAEEEGMQLLQTKDLMAKGAGPKGSRSRARWGLAYTLLHNPSLQAFRKAALTSAKANGTQP
Protein: Large ribosomal subunit protein eL6 (60S ribosomal protein L6) (P47991)
Organism: Caenorhabditis elegans
Function: Component of the large ribosomal subunit.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q02878}. Cytoplasm {ECO:0000250|UniProtKB:Q02878}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q2YGT9}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q02878, ECO:0000250|UniProtKB:Q2YGT9}.
Interaction partners:
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein eL33
- Large ribosomal subunit protein eL28
- Small ribosomal subunit protein eS6
- 60S ribosomal protein L32
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein eS28
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL14
Sequence:
MVGKRNLPVISRNFDLSPGVLRFSASRLRLKKGEKKPKFTKDTSAKLPKLQRNGTKFALGHSKTVTLRKTLTPGTVLIVLAGRHKGKRVVFLKQLPQSGLLLVTGPHKINGFPLRRIGQAFVIATSLKVNVSGVKIPEHINDEYFKRKSTAQKTGKNIFASGKTEYTVSEQRKKDIKTVDAPILAAIKKHPEHKFLFGYLGTRFSLGKNQYPHKMQF
Protein: 14-3-3-like protein GF14 phi (General regulatory factor 4) (P46077)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P48349}. Cytoplasm {ECO:0000250|UniProtKB:P48349}. Note=Translocates from the cytosol to the nucleus when phosphorylated. {ECO:0000250|UniProtKB:P48349}.
Interaction partners:
- ATPase 2, plasma membrane-type
- DEAD-box ATP-dependent RNA helicase 28
- Glutathione S-transferase U9
- AT3g15090/K15M2_24
- Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH9
- Shaggy-related protein kinase epsilon
- Dual specificity phosphatase Cdc25
Sequence:
MAAPPASSSAREEFVYLAKLAEQAERYEEMVEFMEKVAEAVDKDELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEESRGNDDHVTTIRDYRSKIESELSKICDGILKLLDTRLVPASANGDSKVFYLKMKGDYHRYLAEFKTGQERKDAAEHTLTAYKAAQDIANAELAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAIAELDTLGEESYKDSTLIMQLLRDNLTLWTSDMQDESPEEIKEAAAPKPAEEQKEI
Protein: TCDD-inducible poly(ADP-ribose) polymerase (D3ZMH5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDMETTDPEPDCVVQPPSPPDDFSCQMRISEKITPLKTCFKKKQEQKRLGTGTLRSLRPILNTLLESGSLDGVFRARDQNGDESSLHEHIVKKPLDINPACPPAENSMPVLIPDGTNVEGQLPEAHPSTDAPEQVVPIQDHSFPPETINGTVADSTTGHFQTDLLHPVSGDVPTSPDCIDKVMDYVPGAFQDNSFTIQYILDTSDKLSTELFQDKSEEASLDLVFELVNQLQYHTHQETGIEICMDFLQGTCIYGRDCLKHHTVLPYHWQIKRTTTQKWQSVSNDSQEHLERFYCNPENDRMRMKYGGQDFWADLNAMTVFETTEFDQLRRLSTPPCSSTNSIYHTFWKFFCRDHFGWREYPESVVRLIEEANSRGLKEVRFMMWNNHYILHNSFFRREIKRRPLFRSCFILIPYLQTLGGVPTQASLPLEATSSQIICPDGVTSANFYPETWVYMHPSQDFIQVPVSAEDKSYRIIYNLFHKTVPEFKYRILQILRVQNQFLWEKYKRKKEYMNRKMSGRDRIINERHLFHGTSQDVVDGICKHNFDPRVCGKHATMFGQGSYFAKKASYSHNFSKKSSKGVHFMFLAKVLTGRYTMGSHGMRRPPPVNPGSVTSDLYDSCVDNFFEPQIFVIFNDDQSYPYFVIQYEEVSNTVSI
Protein: Beta-microseminoprotein E1 (msp-E1) (O97935)
Organism: Saguinus oedipus (Cotton-top tamarin)
Subcellular location: Secreted {ECO:0000250}. Note=Sperm surface. {ECO:0000250}.
Interaction partners:
Sequence:
MNVLLGGLVIFATFVTLCNGSCYVIRHKIVPGETIKECTDLKGNKHPLDSRWRTEDCELCACRDIEISCCSLVSTPVGYDRHNCRKIFNKETCKISVVEKTDPNRPCGVSGWIS
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (F8W2B2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Cell division cycle 14Aa.
- Dual specificity protein phosphatase CDC14AB
- Fizzy-related protein homolog
- Fizzy/cell division cycle 20-related 1b.
- Cyclosome subunit 8
- Cell division cycle 16 homolog
- Importin-5
- M-phase inducer phosphatase
- Anaphase-promoting complex subunit 1
Sequence:
MKRKSERRCGSRKRICASLRDRSDIQLHITDQLYFALLHQKVRSTPDRHCFCIDEELSYENFYADFGPLNLAMLYRFCCKLKKKLKSCAHAKKKIVFYTYGDRKKQANAAYLIGSYAVMHLQKTPEEAYSLLVSQNAPYLPFRDASFGACMYNLNILDCLRAVHKALQFGWLDFTQFNVEEYEHYERAENGDFNWILPGKFLAFSSPHPKSKIENGYPLHAPEAYFPYFRKHNVTTIIRLNKKMYDSKRFTDVGFKHHDLFFVDGSTPNDSIVSRFLHICENADGVIAVHCKAGLGRTGTLIGCYLMKHFRLTAAEAIAWIRICRPGSVIGPQQNFVDEMQSSLWAEGELYRQKINEQENGSAKTAVAGILSGVEDISINGTNKSTSQRKTASQNHTEEEEEDCAGLTQGDKLRALKSKRQSRASTGSISLEENTVHTKSTSKSLSSEKRKRTRASLGSNRASSNSISKARAPLLR
Protein: Extradiol ring-cleavage dioxygenase class III enzyme subunit B domain-containing protein (Q38B29)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTVYPSLFVCHGGGPLPLLRDEGHKMLVDALKSHRKLLENRFGLPKAIVVISAHYETNTPKVGGAERPSLLFDYYGFPEESYKFRYPVPGNAPLAAAIVNALTVGGFHAEMEPERLLDHGVFVPLMIMFPEANIPVVPLSVLRSGDPAEHIRMGKALRPLRSDAVMFIGSGSTMHHFAHFNREGAGRKFGDALTSILCKNEVATLPEDRLKAMERVKTMEGFTEAQPLREHEHLMPLLTLVGAANGNIAEEVASISFGRANVRNYLFTE
Protein: Coatomer subunit beta-1 (Beta-coat protein 1) (Beta-COP 1) (Q9SV21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit beta'-1
- Coatomer subunit delta
- Coatomer subunit alpha-2
- Coatomer subunit beta'-2
- Coatomer subunit alpha-1
- Coatomer subunit beta'-3
- Coatomer subunit epsilon-1
- Coatomer subunit gamma
- Coatomer subunit epsilon-2
- Structural molecule
Sequence:
MDKSSTMLVHYDKGTPAVANEIKEALEGNDVEAKVDAMKKAIMLLLNGETIPQLFITIIRYVLPSEDHTIQKLLLLYLELIEKTDSKGKVLPEMILICQNLRNNLQHPNEYIRGVTLRFLCRMKETEIVEPLTPSVLQNLEHRHPFVRRNAILAIMSIYKLPQGDQLFVDAPEMIEKVLSTEQDPSAKRNAFLMLFTCAEERAVNYLLSNVDKVSDWNESLQMVVLELIRSVCKTKPAEKGKYIKIIISLLSATSSAVIYECAGTLVSLSSAPTAIRAAANTYCQLLLSQSDNNVKLILLDRLYELKTLHRDIMVELIIDVLRALSSPNLDIRRKTLDISLDLITHHNINEVVQMLKKEVVKTQSGELEKNGEYRQMLIQAIHACAVKFPEVASTVVHLLMDFLGDSNVASALDVVVFVREIIETNPKLRVSIITRLLDTFYQIRAGKVCPCALWIIGEYCLSLSEVESGISTITQCLGELPFYSVSEESEPTETSKKIQPTSSAMVSSRKPVILADGTYATQSAASETTFSSPTVVQGSLTSGNLRALLLTGDFFLGAVVACTLTKLVLRLEEVQSSKTEVNKTVTQALLIMVSMLQLGQSPVSPHPIDNDSYERIVLCIKLLCHRNDEMKKIWLESCRQSFVKMISEKQLREMEELKAKTQTTHAQPDDLIDFFHLKSRKGMSQLELEDQVQDDLKRATGEFTKDENDANKLNRILQLTGFSDPVYAEAYVTVHHYDIALEVTVINRTKETLQNLCLELATMGDLKLVERPQNYSLAPERSMQIKANIKVSSTETGVIFGNIVYETSNVMERNVVVLNDIHIDIMDYISPAVCSEVAFRTMWAEFEWENKVAVNTTIQNEREFLDHIIKSTNMKCLTAPSAIEGECGFLAANLYAKSVFGEDALVNVSIEKQTDGALSGYIRIRSKTQGIALSLGDKITLKQKGSS
Protein: Small ribosomal subunit protein uS3c (30S ribosomal protein S3, chloroplastic) (P56798)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Large ribosomal subunit protein uL22c
- Small ribosomal subunit protein uS11c
- Small ribosomal subunit protein uS8c
- Large ribosomal subunit protein uL14c
- DNA-directed RNA polymerase subunit alpha
- Small ribosomal subunit protein uS2c
- Large ribosomal subunit protein uL16c
- Small ribosomal subunit protein uS14c
- Large ribosomal subunit protein uL3c
- Translation elongation factor EF1B/ribosomal protein S6 family protein
Sequence:
MGQKINPLGFRLGTTQSHHSLWFAQPKKYSEGLEEDKKIRDCIKNYVQKNIRISSGMEGIARIEIQKRIDLIQIIIYMGFPKLLIEDKPRRVEELQMNVQKELNCVNRKLNIAITRISNPYGDPNILAEFIAGQLKNRVSFRKAMKKAIELTEQANTKGIQVQIAGRIDGKEIARVEWIREGRVPLQTIEAKIDYCSYTVRTIYGVLGIKIWIFVDEE