wanglab/gogpt-training-data huggingface dataset:
Protein: tRNA threonylcarbamoyladenosine dehydratase (EC 6.1.-.-) (t(6)A37 dehydratase) (Q46927)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the ATP-dependent dehydration of threonylcarbamoyladenosine at position 37 (t(6)A37) to form cyclic t(6)A37 (ct(6)A37) in tRNAs that read codons beginning with adenine. TcdA is also part of a sulfur transfer pathway; is able to accept sulfur from CsdA directly in vitro, but CsdE might act as the sulfur donor in vivo.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sulfur acceptor protein CsdE
- Cysteine desulfurase CsdA
- Triosephosphate isomerase
- tRNA
Sequence:
MSVVISDAWRQRFGGTARLYGEKALQLFADAHICVVGIGGVGSWAAEALARTGIGAITLIDMDDVCVTNTNRQIHALRDNVGLAKAEVMAERIRQINPECRVTVVDDFVTPDNVAQYMSVGYSYVIDAIDSVRPKAALIAYCRRNKIPLVTTGGAGGQIDPTQIQVTDLAKTIQDPLAAKLRERLKSDFGVVKNSKGKLGVDCVFSTEALVYPQSDGTVCAMKATAEGPKRMDCASGFGAATMVTATFGFVAVSHALKKMMAKAARQG
Protein: Javelin-like, isoform D (A0A0B4K682)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Protein spindle-F
Sequence:
MPTTKTQTQTTTTCSEEEEAAIIRENCDTPMATPANATTANTTTAAPITTTTTTVNTRRQEEAAAVASTPSVTKTATTTNILAAAAGCHKPLFFSRRFQDKRNFSSLPLFVYATSPSTHAHSADGVGVAKEAAAFCHKNEGFEPATHGISKTDGSCISHHSQSNGNGIEGVNGGGIVGHHLGGVLRTTDLASGAMECLPMSSAAHHPHLMAGASAVGAVSASPTATVVVGATYPHHLHHHHLSHHTPYSNSYGSHHIHSEQTKSLQELQHEVGALLEFRDLVIETFPDLKHKMASMSATPSTPTSSVGAIGGSHSVGGGSSSLATSRREWEPGIRMKRKQSHKEPSTSSAAAAPSSGAEASSSSLTRSRSNSHSGKKEPKSGENNNGSVVQDSGFSTETSSSKEGHSASSTNGAMTVAIAANRLSCAESDDELLNLLDVIHRKSNRLREEVEHLQSYERQHGDAQKTGGEGQGASKEGMTAQQFREQVERLNREDIKQLRKERDRLLDKLAEMEAETLTGRIKAAKMSDQVEELVGVKKDLEEQLKLAMAQKLELSSRVQQLQQQQQSKSSSSGSQSDYSSQRNFLSSATTVLSNGSRPSSNVISNNTFQPVVLDQPAQEAFHQSPGSDIPLRKQQQQSLGRLDGIVSTPGTRNSKCRLTDSKRFAAILLETNVLELQRHLLTLTVQNQVLAQKLESSSKSKTLLAKRLDKNSEEFEHLRYQLEEKNIELEGTKAQLRLVESRLQASNSTSNSYLHSSQHDYETNRSSASTTLMLSRRGVSDSVDSTSTAMPAPPVTQISTPSMKAMVPLAMDELQQHSSSTESAHEHENQGLQTPNSTSSPLSKTIINASPCPVGSSTPSNIAARVMSISVGGVSPFEAMTPPPRQNAFRKFGSASKPSKIPLPGSKAAAYFSGKPPTGRPSTAGRSPPSANNSSSTSYGSKSSLSRSTGNLQSLRRAETSASNHSLSTNTSRSSTSSSIPLATTPYSSGSTGNRSQPTAATTPSPRVLQNSPLPKLKRDTISSRVRHLDSLSRAQQTPEGLKGTTTNSTSIAAQLSSTLRKDLQLSGNGTGAPYNQHHLNHRRSGHSPASNSSGSGVSRRYSSASTGGSGGRAIGRDQGEPTTPTSSYGGDSDSGKNLANTVEKPNFRLNNQNWQLWQTSSSSQGKIQMERYLPHELHDVSEETAYDSYYTEYTTPDSMDCGSANLLVTFDYGYCDSMEARANPAAPEDDDRCDGVDPDYGGDGCADEVDAIWFGTPPRDKKDEKLFEVHHVQHKLLDDSMQSLISYDVDDFEEELSEPDPDEEIFYDSIECV
Protein: Uncharacterized protein (Q389M8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKRHMHDRMRHASRDPRRQSTREAIMLSACTKKPKKRLFTYSQWCSLLRRRRRVALRRRPTTRRRLLRRIFALRYGKYQKPLCNCAMPNHGTILTGAVPGRTSILWLPSHWYMRRRFHYCVEKAKVSPCPNPEPDLAIVGGGSGRGTPSCTVTLRIAVPLKCQRKQHRILQRWVARLPTFVSSQMTSKVVRQHRGKLTAVPPPMCFVAERSHMCVWRLQQLNMERRFSPEELMNLLIMRTNENPPAMGYTKSFRLSKTTPDPTGGTWQTNGCSVYYGYVWSAAAKAAGYPFPQDACTVQSNPVVAVTLVLVRDGKVGRGDTYYLIAPCPVYFGPQARRHLSFCLISHWNPCPAVGFLSSMLEVWCCAGAAAQECGEKAVLPSHSWVRQRVDKAMMRWHSATAGKSESSEFLEAENSNVFLSTKSSSLTPTKRALGGVKVFTFPSFPPFTDIVDCTSFPIHQCVVTVLAVSVRRIRNADALGSSRTCNTWSYRACHFQLSRHLFSSVVSPVAATWRQWCDDSEEVAGTVGLCRSNGYAYSARAIGEEERETLQLLSGCYALFGRESARNVWRNSGVARLYHSPSNAHQRVLLKFSARGGRQHQEVGGALLLLKPKDQEESGATLCVTIPELTRIGTIATAPFFSMRFGCCLAYAWVWDHAGWKSLISDHCRRAVSGSRSSQRGDVVNEGSVEDPNSKNTECCFVCSNNGLLALLPYLREVPTSCKGGRTTVPGKTKRGKVTTAMKMKKWKEVQSKLCDIDVCTPVDIVRLTARS
Protein: Uncharacterized protein (Q582V8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MCSYPYVCETVILPLLLFLLLCFLFLFNVFFSSFTSLHLHGTAANIRLFFCFLPLLAFLALLFSFLFLRGVGVLLLLLLLLSLFIHCYLRFSRSDRLRCSYIFLLIVFISFLLMMMMMMFLICFVLFCFVLCPPAPHCQLFTLFRYLFFFAVQVSNNIKKYIRLY
Protein: Group 1 truncated hemoglobin GlbN (Truncated hemoglobin) (trHbN) (Hemoglobin-like protein HbN) (P9WN25)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Binds oxygen cooperatively with very high affinity (P(50) = 0.013 mmHg at 20 degrees Celsius) because of a fast combination (25 microM(-1).sec(-1)) and a slow dissociation (0.2 sec(-1)) rate.
Interaction partners:
- Group 2 truncated hemoglobin GlbO
- nitric oxide dioxygenase
- Probable conserved membrane protein
Sequence:
MGLLSRLRKREPISIYDKIGGHEAIEVVVEDFYVRVLADDQLSAFFSGTNMSRLKGKQVEFFAAALGGPEPYTGAPMKQVHQGRGITMHHFSLVAGHLADALTAAGVPSETITEILGVIAPLAVDVTSGESTTAPV
Protein: Carboxypeptidase N catalytic chain (CPN) (EC 3.4.17.3) (Anaphylatoxin inactivator) (Arginine carboxypeptidase) (Carboxypeptidase N polypeptide 1) (Carboxypeptidase N small subunit) (Kininase-1) (Lysine carboxypeptidase) (Plasma carboxypeptidase B) (Serum carboxypeptidase N) (SCPN) (P15169)
Organism: Homo sapiens (Human)
Function: Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Carboxypeptidase N subunit 2
- Carboxypeptidase B
- Carboxypeptidase B2
- Tubulin-specific chaperone E
- Tubulin-specific chaperone E
- Tubulin-specific chaperone D
- Kininogen-1
Sequence:
MSDLLSVFLHLLLLFKLVAPVTFRHHRYDDLVRTLYKVQNECPGITRVYSIGRSVEGRHLYVLEFSDHPGIHEPLEPEVKYVGNMHGNEALGRELMLQLSEFLCEEFRNRNQRIVQLIQDTRIHILPSMNPDGYEVAAAQGPNKPGYLVGRNNANGVDLNRNFPDLNTYIYYNEKYGGPNHHLPLPDNWKSQVEPETRAVIRWMHSFNFVLSANLHGGAVVANYPYDKSFEHRVRGVRRTASTPTPDDKLFQKLAKVYSYAHGWMFQGWNCGDYFPDGITNGASWYSLSKGMQDFNYLHTNCFEITLELSCDKFPPEEELQREWLGNREALIQFLEQVHQGIKGMVLDENYNNLANAVISVSGINHDVTSGDHGDYFRLLLPGIYTVSATAPGYDPETVTVTVGPAEPTLVNFHLKRSIPQVSPVRRAPSRRHGVRAKVQPQARKKEMEMRQLQRGPA
Protein: Uncharacterized protein (Q59T87)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Chromatin structure-remodeling complex subunit SFH1
- Npl6p
- Chromatin structure-remodeling complex protein RSC8
- Arp9p
- Chromatin structure-remodeling complex subunit RSC1
- Bromo domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Chromatin structure-remodeling complex protein RSC58
- Uncharacterized protein
Sequence:
MVKNTSYKKQKLSSRNRIINQEVPLFPPTKYEKSKATLKHFPSSIVNGVTAEGGLYSLTFKSINCASFVENNELMKTVFKVPKLELSKVTDNDDVDKLKNWKQTLENDINELKKSDSNVANTNIVSDLQNELQTDLENNGNNLATFGEKLADSFVVNINISDGNYKVIQDVIIPGLQVDTFEDVTNPDLSEYEKITLSDTQNEEKEETGNKQETEVGQEVESEQKDENKTEQTSQPTST
Protein: At4g18400 (Q8LEL5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- SWR1 complex subunit 6
- At3g51500
- Protein EIN6 ENHANCER
- Transcription initiation factor TFIID subunit 14b
- Phosphatidylinositol 3-and 4-kinase family protein with FAT domain-containing protein
- SWR1 complex subunit 2
- At4g30630
- At5g57910
- E3 ubiquitin-protein ligase JMJ24
- Phosphotransferases/inositol or phosphatidylinositol kinase
Sequence:
MAEEEKRTSPEPPLPSPPESSSQPEHPPPETSTPPATFDPSRMIGIIKRKALIKDLAAAYHVECLALCRELLELQKRKDEPFLDTKATEDLRKETLRSSSKRAKKKR
Protein: V-type proton ATPase subunit B, brain isoform (V-ATPase subunit B 2) (Endomembrane proton pump 58 kDa subunit) (Vacuolar proton pump subunit B 2) (P62814)
Organism: Mus musculus (Mouse)
Function: Non-catalytic subunit of the V1 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 (By similarity). In renal intercalated cells, can partially compensate the lack of ATP6V1B1 and mediate secretion of protons (H+) into the urine under base-line conditions but not in conditions of acid load.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:15013950, ECO:0000269|PubMed:16174750, ECO:0000269|PubMed:17898041, ECO:0000269|PubMed:29993276}. Melanosome {ECO:0000250|UniProtKB:P21281}. Cytoplasm {ECO:0000269|PubMed:15013950, ECO:0000269|PubMed:17898041}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:P62815}; Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250|UniProtKB:P62815}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit E 1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit d 1
- V-type proton ATPase subunit F
- V-type proton ATPase subunit H
- V-type proton ATPase subunit G 2
- V-type proton ATPase subunit C 1
- V-type proton ATPase 16 kDa proteolipid subunit c
Sequence:
MALRAMRGIVNGAAPELPVPTGGPMAGAREQALAVSRNYLSQPRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFEKNFITQGPYENRTVYETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH
Protein: Noggin-3 (Q9YHV3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May function as an inhibitor of bone morphogenetic proteins (BMP) signaling during later stages of development including late phases of dorsoventral patterning, to refine the early pattern set up by the interaction of chordino and BMP2/4. Not involved in organizer function or early phases of dorsoventral pattern formation.
Subcellular location: Secreted.
Interaction partners:
- Bone morphogenetic protein 4.
- Bone morphogenetic protein 7
- Bone morphogenetic protein 2
- Bone morphogenetic protein 2a.
- Bone morphogenetic protein 6.
- Chordin
- Bone morphogenetic protein 5.
- Growth differentiation factor 5
- Noggin-2
- Noggin-1
Sequence:
MDNIPYFLATVLIFSLGFRIEEGMCQHYYLLRPIPSDSLPIVELKEDPDPVLDPKERDLNETELRAILGSHFEQNFMSINPPEDKHAGQDELNESELMKQRPNGIMPKEIKAMEFDIQHGKKHKPSKKLRRRLQLWLWSYTFCPVVHTWQDLGNRFWPRYLKVGSCYNKRSCSVPEGMVCKPPKSSHLTVLRWRCVQRKGGLKCAWIPVQYPVISECKCSCPN
Protein: Myosin regulatory light chain 11 (Fast skeletal myosin light chain 2) (MLC2B) (Myosin light chain 11) (Myosin regulatory light chain 2, skeletal muscle isoform) (Q96A32)
Organism: Homo sapiens (Human)
Function: Myosin regulatory subunit that plays an essential role to maintain muscle integrity during early development (By similarity). Plays a role in muscle contraction (By similarity).
Interaction partners:
- Myosin light chain 1/3, skeletal muscle isoform
- Troponin C, skeletal muscle
- Myosin-7
- Myosin-2
- Myosin-1
- Myosin-3
- Troponin T, fast skeletal muscle
- Actin, cytoplasmic 2
- Actin, cytoplasmic 1
- Troponin I, fast skeletal muscle
Sequence:
MAPKRAKRRTVEGGSSSVFSMFDQTQIQEFKEAFTVIDQNRDGIIDKEDLRDTFAAMGRLNVKNEELDAMMKEASGPINFTVFLTMFGEKLKGADPEDVITGAFKVLDPEGKGTIKKKFLEELLTTQCDRFSQEEIKNMWAAFPPDVGGNVDYKNICYVITHGDAKDQE
Protein: Phosphatidylinositol mannoside acyltransferase (PIM acyltransferase) (EC 2.3.1.265) (A0QWG5)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the transfer of a palmitoyl moiety from palmitoyl-CoA to the 6-position of the mannose ring linked to the 2-position of myo-inositol in phosphatidyl-myo-inositol monomannoside (PIM1) or dimannoside (PIM2).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:12851411, ECO:0000269|PubMed:26965057, ECO:0000269|PubMed:29185694}; Peripheral membrane protein {ECO:0000269|PubMed:26965057, ECO:0000269|PubMed:29185694}; Cytoplasmic side {ECO:0000269|PubMed:26965057, ECO:0000269|PubMed:29185694}. Note=Permanently associated with the membrane. {ECO:0000305|PubMed:29185694}.
Interaction partners:
- Phosphatidyl-myo-inositol mannosyltransferase
- Phosphatidylinositol phosphate synthase
- Hydrolase, nudix family protein
- HIT family protein hydrolase
- GDP-mannose-dependent alpha-
- Threonine--tRNA ligase
- GDP-mannose-dependent alpha-mannosyltransferase
- O-acyl transferase
- Acyl-coenzyme A thioesterase THEM4
- Divalent metal cation transporter MntH
Sequence:
MTLSGRIPLGGQVTDLGYAAGWRLVRAMPEAMAQGVFGAGARYAARNGGPEQLRRNLARVVGKPPADVPDDLIRASLASYARYWREAFRLPAMDHGRLGEQLDVIDIDHLWSALDAGRGAVLALPHSGNWDMAGVWLVQNYGPFTTVAERLKPESLYRRFVEYRESLGFEVLPLTGGERPPFEVLAERLTDNRPICLMAERDLTRSGVQVDFFGEATRMPAGPAKLAIETGAALFPVHCWFEGDGWGMRVYPELDTSSGDVTAITQALADRFAANIATYPADWHMLQPQWIADLSDERRARLGT
Protein: Protein GID8 homolog (Q84WK5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22676313}. Note=Associates predominantly in the form of large cytoplasmic complexes. {ECO:0000269|PubMed:22676313}.
Interaction partners:
- Protein MAEA homolog
- Protein RMD5 homolog
- WD repeat-containing protein 26 homolog
- WD repeat-containing protein WDS homolog
- Ran-binding protein M homolog
- ARM repeat superfamily protein
- At4g09200
- SPla/RYanodine receptor
- Centromere protein O
- ENTH/VHS family protein
Sequence:
MSLFRIFINQLEEDDEDMATSKKMITREEWEKKLNAVKLRKEDMNTLVMNFLVTEGYVEAAEKFQRESGTKPEIDLATITDRMAVKKAVQNGNVEDAIEKVNDLNPEILDTNPELFFHLQQQRLIELIRQGKTEEALEFAQEELAPRGEENQAFLEELEKTVALLVFDDASTCPVKELLDLSHRLKTASEVNAAILTSQSHEKDPKLPSLLKMLIWAQTQLDEKAVYPHINDLSTGKLEDPSE
Protein: COBL-like 1, isoform CRA_d (Cordon-bleu WH2 repeat protein like 1) (A0A7P0TAB9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDGRTPRPQDAPARRKPKAKAPLPPAETKYTDVSSAADSVESTAFIMEQKENMIDKDVELSVVLPGDIIKSTTVHGRYAGVNEISGPPLLIPPLKVSVIYVLMFVL
Protein: T. brucei spp.-specific protein (Q38C65)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKTENFPRGQSAGPEGSLVEIPDHGERQQEVCHIGAPLQREIEAPAAEAGQSSDYKKPHAPHLLPVMEPVKPSSDPQLKDGRKEMPFTSALPIVVPDAPRLATQQRQVQKTKGNGSSAVPGEPDTCEGEPRAPSPGDPRPTQAFPAVEPFKRTASAKLSEARTDPRSPSASPDNESDGARVGSRQVDEEGSRPLCTLPAVELRKKPAGSTLQEEQAKELNTTHAFPVVEPDAVCTEARRSEELEDTRAGHAFPPVASGKQNTGA
Protein: Pivalyl-CoA mutase small subunit (PCM small subunit) (EC 5.4.99.-) (Pivalyl-CoA mutase, AdoCbl-binding subunit) (A7IQE6)
Organism: Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Function: Together with Xaut_5043, catalyzes the reversible isomerization between pivalyl-CoA and isovaleryl-CoA, using radical chemistry. Does not exhibit isobutyryl-CoA mutase (ICM) activity.
Interaction partners:
Sequence:
MIHAGTRPLRVLVTKIGLDGHDRGSRIVAAYLRDAGMEVIYTPPWQTIPGVVKLATEEDVDVIGISSLATDHLIVPKMMEALRAAGLGHVGVVVGGIVPEAEQSALAAAGVSRVFGPGAAREEIVECVTALGQKSRAERVDDYSEANP
Protein: Structural maintenance of chromosomes protein 4 (Cell untimely torn protein 3) (Chromosome segregation protein cut3) (P41004)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Subcellular location: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
Interaction partners:
- Condensin complex subunit 2
- Condensin complex subunit 1
- Condensin complex subunit 3
- Structural maintenance of chromosomes protein 2
- Cohesin subunit rad21
- DNA topoisomerase 2
- Sister chromatid cohesion protein pds5
- Separin
- Exosome complex protein C1739.07
- Sister chromatid cohesion protein mis4
Sequence:
MSDKGIFRTSSTPSIVDVTPDRGERPRKLVRSVLESPSQKDVASIVKIEQTPSRPFFNDFLKKRITDSLNERPNLLNKFMSAQDGTPSKSTGFNERSSQLVSEFTTTEDIENCEETTQVLPPRLVVYELRLTNFKSYAGTQIVGPFHPSFSSIVGPNGSGKSNVIDALLFVFGFRASKLRQSKASALIHKSATHPSLDSCDVEITFKEVNSDFTYVDGSELTVRRTAYKNNTSKYFVNGVESSFSAVSNLLKEKGIDLNHKRFLILQGEVESIAQMKPRAISEGDDGLLEYLEDIIGTSKYKPIIEENMQELSNSDDICAEKESRLKLVLSEKAKLEDSKNSVLSFLKDENELFMKQNQLYRTILYETRNKKTLVQNLLNSLEGKLQAHLEKFEQTERDISEKNEEVKSLREKAAKVKNDCTSEKKTRQSYEQQTVKIEEQLKFLLNKEKKLKKSIEALSFEKSEAENSLSSHDIDSQKLNSEIADLSLRLQQEELSLDDIRKSLQGKTEGISNAIEEKQKAMAPALEKINQLTSEKQILQVELDMLLNKENDLINDVESSQSSLDKLRNDAEENRNILSSKLKVLSDLKGEKKDVSKNIERKKETVHNTYRNLMSNRTKLEEMKASLSSSRSRGNVLESLQRLHESDNLNGFFGRLGDLATIDEAYDVAISTACPALNHIVVDNIETGQKCVAFLRSNNLGRASFIILKELAQKNLARIQTPENVPRLFDLLRFNDQKFAPAFYNVLQNTLVAKNLEQANRIAYGKTRWRVVTLSGQLIDKSGTMTGGGTRVKKGGMSSAITSDVSPASVETCDKQVQLEDTRYRQHLSELESLNQRFTEISERIPSAELEISKLQLDVSACDRLVAGEERRILQLKSDLKSIRNNNERKRNLQNKISNMDKEVEAININNEGLVTEIKTLQDKIMEIGGIRYRIQKSKVDDLHEQLKFVKDKLNKMSFKKKKNEQRSQSFQVELSNLTSEYDTTTESIATLKTELQSLNKYVDEHKSRLREFENALWDINSSIDELVKFIEFESKQMNSVKAERIELENQIQEQRTALSEVGNNENKYLKLMSNLKLHNLTEFCDQTTMDSTFPEYSEDELSSVDKSELVSNISVLKKKTEDREVDINVLSEYRRCNKEAEKRDSDYQSELQKRTDLKKVVTDLQSQRLDEFMYGFGIISMKLKEMYQIITMGGNAELELVDSLDPFSEGVLFSVMPPKKSWKNISNLSGGEKTLSSLALVFALHNYKPTPLYVMDEIDAALDFKNVSIVANYIKERTKNAQFIVISLRSNMFELSSRLVGIYKTANMTKSVTINNKEILTD
Protein: Potassium channel toxin alpha-KTx 11.1 (Parabutoxin-1) (PBTx1) (P60164)
Organism: Parabuthus villosus (Black hairy thick-tailed scorpion)
Function: Binds and inhibits voltage-sensitive potassium channels. Inhibits the vertebrate potassium channels Kv1.1/KCNA1, Kv1.2/KCNA2 and Kv1.3/KCNA3 with low affinity. Also weakly inhibits Kv7.1/KCNQ1 (10 uM of the toxin inhibits currents by 21.43%).
Subcellular location: Secreted {ECO:0000269|PubMed:10542442}.
Interaction partners:
Sequence:
DEEPKESCSDEMCVIYCKGEEYSTGVCDGPQKCKCSD
Protein: ATP sulfurylase 2 (EC 2.7.7.4) (Q43870)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: [Isoform 1]: Plastid, chloroplast {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
Interaction partners:
- Adenylyl-sulfate kinase 3
- Adenylyl-sulfate kinase 2, chloroplastic
- Adenylyl-sulfate kinase 4, chloroplastic
- Adenylyl-sulfate kinase 1, chloroplastic
- 5'-adenylylsulfate reductase 2, chloroplastic
- 5'-adenylylsulfate reductase 3, chloroplastic
- 5'-adenylylsulfate reductase 1, chloroplastic
- Bifunctional adenosine 5'-phosphosulfate phosphorylase/adenylylsulfatase HINT4
- Assimilatory sulfite reductase
- Sulfite oxidase
Sequence:
MSLMIRSSYVSHITLFQPRNSKPSSFTNQISFLSSSNNNPFLNLVYKRNLTMQSVSKMTVKSSLIDPDGGELVELIVPETEIGVKKAESETMPKVKLNQIDLEWVHVISEGWASPLKGFMREDEYLQSLHFNSLRLKNGTFVNMSLPIVLAIDDDTKEQIGSSENVALVCPQGDIIGSLRSVEIYKHNKEERIARTWGTTSPGLPYVEEYITPSGNWLIGGDLEVFEPIKYNDGLDHYRLSPKQLREEFDNRQADAVFAFQLRNPVHNGHALLMNDTRKRLLEMGYKNPVLLLHPLGGFTKADDVPLDVRMEQHSKVLEDGVLDPKTTIVSIFPSPMHYAGPTEVQWHAKARINAGANFYIVGRDPAGMGHPTEKRDLYDPDHGKRVLSMAPGLEKLNILPFRVAAYDTIEKKMAFFDPSRAKEFLFISGTKMRTYARTGENPPDGFMCPSGWNVLVKYYESLQESEAKQQAVVSA
Protein: Transmembrane protein 80 (Q9D3H0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell projection, cilium {ECO:0000269|PubMed:26982032}. Note=Localizes at the transition zone, a region between the basal body and the ciliary axoneme. {ECO:0000269|PubMed:26982032}.
Interaction partners:
- Transmembrane protein 231
- Transmembrane protein 17
- Transmembrane protein 237
- B9 domain-containing protein 1
- B9 domain-containing protein 2
Sequence:
MLFHLSGLYSALYFLATLLMIVYKSQVFSYPCNCLALDLVLLLLMGILKVAQLYLGTKGNLMEAEVPLAASLAFTAVGGLLSVHFLLWQTLVLWMDSVLSTVLLVLHGLEAGLQVVVIADFIR
Protein: V-type proton ATPase subunit a (Q6NLA3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGSLFRSEEMALCQLFLQSEAAYACVSELGELGLVQFRDLNPDVNAFQRKFVNEVRRCDEMERKLRYLEKEIKKDGIPMLDTGESPEAPQPREMIDLEATFEKLENELREVNQNAEALKRNFLELTELKHILRKTQVFFDEQEGGVNQTTESMTRALITDEARTAGASMGPVQLGYMEKSNEREDYLPCFVAGVILRERLPAFERMLWRACRGNVFLRQAMIETPLEDPTNGDQVHKSVFIIFFQGDQLKTRVKKICEGFRATLYPCPEAPADRREMAMGVMTRIEDLNTVLGQTQDHRHRVLVAAAKNLKNWFVKVRKIKAIYHTLNLFNLDVTQKCLIAECWVPLLDIETIQLALRRGTERSGSSVPPILNRMQTFENPPTYNRTNKFTKAFQALIDAYGVASYREMNPAPYTIITFPFLFAVMFGDLGHGAIMALFGLWMIRKEKGLAAQKTDNEIWNIFFGGRYIIFLMGVFSMYTGLIYNDIFSKSLNIFGSHWHLSYNKSTVMENKFLQLSPKGDYEGAPYPFGMDPIWQVAGANKIIFHNAYKMKISIIFGVIHMIFGVVMSWHNHTYFRNRISLLYEFIPQLVFLLLLFFYMVLLMFIKWIKFAATNDKPYSEACAPSILITFIDMVLFNTPKPPPENCETYMFMGQHFIQVLFVLVAVGCIPVMLLAKPLLIMQARKQANEEVQPIAGATSDAEAGGVSNSGSHGGGGGHEEEEELSEIFIHQSIHTIEYVLGSVSHTASYLRLWALSLAHAQLAEVLWTMVLSIGLKQEGPVGGIVLTCVFAFWAILTVGILVLMEGLSAFLHTLRLHWVEFQSKFYKGQGYAFQPFSFDAIIENGAAAAEE
Protein: COP-coated vesicle membrane protein erv25, putative (Q38AU2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- GOLD domain-containing protein
- GOLD domain-containing protein
- GOLD domain-containing protein
- Cytosolic coat protein, putative
- GOLD domain-containing protein
- Coatomer subunit delta
- Coatomer subunit beta'
- GPI inositol-deacylase
- Coatomer subunit gamma
- ER lumen protein-retaining receptor
Sequence:
MNTMQGIMRDLRMVMSPFLLVLVVAISTPASAARFLLQNTQPICFVEEVGEDTRFLTGVYTRSDSLPYPPTVKMTIKSPSGSVTWEGKVVAGTNSFSAPVSAGSIGKYQICVSVSTWGFRASDDGSSVVMDVNIDQKTTVISKTEVPMLKRQNVGGMEVFTFRDFGGQQKDILRPPEYFKRVEGALSKLLMQVKDVSSGIDHNIERFSRMFTTSENTHKRIWAFGVLTVLVTIATIWLQFRLLKSTLREKKLV
Protein: Cyclin-dependent protein kinase inhibitor SMR7 (Protein SIAMESE-RELATED 7) (Q9LVX6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable cyclin-dependent protein kinase (CDK) inhibitor that functions as a repressor of mitosis in the endoreduplication cell cycle. Acts as a potent cell cycle inhibitor, regulating a hydroxyurea-dependent checkpoint in leaves.
Interaction partners:
- Cyclin-dependent protein kinase inhibitor SMR5
- SUPPRESSOR OF GAMMA RESPONSE 1
- Cyclin-dependent protein kinase inhibitor SMR4
- Wee1-like protein kinase
- Transcription factor MYB3R-3
- NAC domain containing protein 85
- NAC domain containing protein 44
- Transcription factor MYB3R-5
- Cyclin-dependent kinase inhibitor 6
- Transcription factor MYB3R-4
Sequence:
MGISKKSQVSRELDTDGKKFIFAKTSIRASLKPVKTKLIKPERESEDGICITPTARGAKTPECPAAPRKRPPVLKCQNNIRIEYFVPPSDFELVFIQRR
Protein: Transcription elongation factor A protein-like 5 (TCEA-like protein 5) (Transcription elongation factor S-II protein-like 5) (Q5H9L2)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MEKLYKENEGKPENERNLESEGKPEDEGSTEDEGKSDEEEKPDMEGKTECEGKREDEGEPGDEGQLEDEGNQEKQGKSEGEDKPQSEGKPASQAKPESQPRAAEKRPAEDYVPRKAKRKTDRGTDDSPKDSQEDLQERHLSSEEMMRECGDVSRAQEELRKKQKMGGFHWMQRDVQDPFAPRGQRGVRGVRGGGRGQKDLEDVPYV