wanglab/gogpt-training-data huggingface dataset:
Protein: Oxygen-independent coproporphyrinogen III oxidase (CPO) (EC 1.3.98.3) (Coproporphyrinogen III dehydrogenase) (CPDH) (O34162)
Organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha)
Function: Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P32131}.
Interaction partners:
- Uroporphyrinogen decarboxylase
- Oxygen-dependent coproporphyrinogen-III oxidase
- Protoporphyrinogen IX oxidase
- FAD-dependent oxidoreductase
- cytochrome-c oxidase
- Cbb3-type cytochrome oxidase, monoheme subunit II
- Polyferredoxin
- OmpW family protein
- Cbb3-type cytochrome c oxidase subunit
- OmpW family protein
Sequence:
MIPSAITSPAPDRRALSDFRALAGRIDGNGPRYTSYPTADRFHNGPDLSLYHDALAACRADAPAPLSLYLHIPFCENICYYCGCNKIITRDHGRSARYVNYLGREMALVADRLGPRRQVLQSHWGGGTPTFLDPGEMRRVMALLHEHFELAAEGEHSIEIDPRRVDHARMALLAELGFNRVSLGVQDFDPEVQQAIHRIQPFEETRAVVDAARTLGFRSVSLDLIYGLPHQTAARFGRTIDQVLALRPDRLSVYSYAHLPHVFKPQRRIDENALPPAGEKLDILVSTIERLSAEGYVYIGMDHFALPDDDLAVAQREGRLQRNFQGYSTHAGYDQVGLGISAIGAIAGRYVQNARTLDEYYGALDHGRLPLARGVAMSADDHLRREIIGALMCNGVLDIPALEARHGIRFGTAFAPELADLAALGADGLVQCAPDRITVTPLGRLLVRRVAMVFDRYLREDAARPASTGAQAVAANDGAQPVRFVPRARYSRVV
Protein: CBFA2/RUNX1 partner transcriptional co-repressor 3 (H3BSI4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPDSPAEVKTQPRSTPPSMPPPPPAASQGATRPPSFTPHTHREDGPATLPHGRFHGCLKWSMVCLLMNGSSHSPTAINGAPCTPNGFSNGPATSSTASLSTQHLPPACGARQLSKLKRFLTTLQQFGSDISP
Protein: Zinc finger protein 776 (Q68DI1)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAAAALRPPAQGTVTFEDVAVNFSQEEWSLLSEAQRCLYHDVMLENLTLISSLGCWYGAKDETPSKQTLSIQQESPLRTHWTGVCTKKVHLWGMCGPLLGDILHQGTQHNQKLNGFGAYEKKLDDDANHHQDQKQHIGEKSYRSNAKGTSFVKNCKFHMSHEPFIFHEVGKDFLSSLRLLQQEDIHTSGKSNFETKHGIPLQGGKTHYICGESTIPFSNKHSLVLHQRLLPREGPYVCSDSGKFTSKSNSFNNHQGVRTGKRPYQCGQCDESFWYKAHLTEHQRVHTGERPYECGECDKSFSHKHSLVDHQRVHTGERPYECDECGKSFSHKRSLVHHQRVHTGERPYQCGECGKSFNHKCNLIQHQRVHTGERPFECTACGKLFRSNSHLKEHQRVHTGERPYECKECRKSFRYKSHLTEHQRVHTGERPYECRECGKCFHQKGSLIQHQQIHSGERPHECGECGKCFHQKGSLIRHQQIHSGERPHECGECGKCFRQKGNLIKHQRVHTGERHHEC
Protein: Aftiphilin b (Aftiphilin isoform X1) (F1QB98)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Synergin, gamma.
Sequence:
MEPDVVRLYSSSPPPLDETGEEEEEDEFGEFGGFDGGGVSSSFSLSELDTPTTYDQSNALEDSPPDLIIKCTQNIIVSENNGWTNEKERETESISSFGIAEKESSGILTNGMTSSDLQVELSDRSDQNSPSMGSDVQNSSTGDEHSLSNGYSESCSNSDLDQSLHNCLQSTHIEVNYGRDASIADVLDRSRITDKLPDSNNHSSCTEACELRDTEAGLEICGNSQFLSSCRDAQEVEGEQDQSENCFAADCLDESMDHVDKAEAETVSSVDADLISDMQLSGDTIEIHGSFANSEVGIDAEVETSADPTADEDFCDFRDATQGFTDFSRTESMTQEGLPEFVTAMSRCSTDDDFGDTDTLKDFKEEDELAEEMTGEEGGFCSELPPSDSFADFSSAPFEGAAGGEDDGWAAFAPRESPKGDQDSWATFGEEQSTYAGKEEQDVETSSAPSREDIQSSTVDFSCKIQHLFKTAFPLDVHAEVSEVTEVLPLHKFLPAQDPQEQRDPSSSFFAQENALVMWRHLQDILGSHGLKFKWAGSHSNRILLNCLGIRNILFTGDKNQPLIVPMFAAGLGMLEPTKESQKSPASPALCPSAPLESGNILCTQVAPSLAISIDAQDEGISKLNLDYFGPVDECSSDSETDTPLPGVDPEIYELTTAKMENNTTGRNIADAFTKLMESIEKTKPTVRKPETDEEMSEEAAKVISLLPDLSFMKARVLMFPSILTPAANHT
Protein: Myogenesis-regulating glycosidase (EC 3.2.1.-) (Nuclear envelope transmembrane protein 37) (Uncharacterized family 31 glucosidase KIAA1161) (Q69ZQ1)
Organism: Mus musculus (Mouse)
Function: Putative glycosidase. Promotes myogenesis by activating AKT signaling through the maturation and secretion of IGF2.
Subcellular location: Nucleus membrane {ECO:0000269|PubMed:17062158, ECO:0000269|PubMed:19706595}; Single-pass type II membrane protein {ECO:0000269|PubMed:19706595}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19706595}; Single-pass type II membrane protein {ECO:0000269|PubMed:19706595}. Note=Only a minor fraction is present in the peripheral endoplasmic reticulum (PubMed:19706595). {ECO:0000269|PubMed:19706595}.
Interaction partners:
- Sodium-dependent phosphate transporter 2
- Solute carrier family 53 member 1
Sequence:
MSQNLQETSQAYPRHRPGSHAGPKSLKVTPRATMYTFLPDNFSPAKPKPTKELRPLLCSAVLGLLLVLAAVVAWCYYSASLRKAERLRAELLDLNRGGFSIRNQKGEQVFRLAFRSGALDLDSCSRDGALLGCSRAADGRPLHFFIQTVRPKDTVMCYRVRWEEAVPGRAVEHAMFLGDAAAHWYGGAEMRTQHWPIRLDGQQEPQPFVTSDVYSSDAAFGGILERYWLSSRAAAIKVNDSVPFHLGWNSTERSMRLQARYHDTSYKPPAGRTAAPELSYRVCVGSDVTSIHKYMVRRYFNKPSRVPASEAFRDPIWSTWALHGRAVDQNKVLQFAQQIRQHRFNSSHLEIDDMYTPAYGDFNFDEGKFPNASDMFRRLRDAGFRVTLWVHPFVNYNSSSFGEGVERELFVREPTGRLPALVRWWNGIGAVLDFTHPEAREWFQGHLRRLRLRYNVTSFKFDAGEVSYLPRDFSTYRPLSDPSVWSRRYTEMAEPFFSLAEVRVGYQSQNISCFFRLVDRDSVWGYDLGLRSLIPAVLTVSMLGYPFILPDMIGGNAVPERTAGRQDGPGPERELYVRWLEVAAFMPAMQFSIPPWQYDAEVVAIAHKFAALRASLVAPLLLELAGEITDTGDPIVRPLWWIAPGDETAHRIDSQFLIGDTLLVAPVLEPGKQERDVYLPAGKWRSYKGELFDKTPVLLTDYPVDLDEVAYFTWAS
Protein: Bud site selection protein 4 (P47136)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for establishment of the axial budding pattern in haploid cells. Cooperates with other bud site selection proteins to recognize a spatial landmark during mitosis and they subsequently become a landmark for downstream polarity establishment factors that coordinate axial budding and cytokinesis. Involved in the septin organization at the bud neck.
Subcellular location: Bud neck {ECO:0000269|PubMed:12221111, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8707826}. Note=Localizes to two distinct rings on either side of the mother-bud neck. The rings stay present in cells after cytokinesis and disappear before the next bud emergence. Requires IQG1 for proper localization.
Interaction partners:
- Bud site selection protein 3
- Axial budding pattern protein 2
- Putative protease AXL1
- Seventh homolog of septin 1
- Cell division control protein 10
- Cell division control protein 12
- Bud site selection protein 5
- Cell division control protein 11
- Riboflavin synthase
- Inhibitory regulator protein BUD2/CLA2
Sequence:
MHDAESTVDSLLKEIDNEMEQTKSNITQNGSEDTPHNWKLPLQEIGDDTMEMLVKHNTRSNATENSRGRSPSKMSTISNESLNLGLLRVNSELEESPAAVHQERIKNSVANGALGHANSPKVLNNLKNMAQDIDKLARDEEKPVKLSSSPLKFTLKSTQPLLSYPESPIHRSSIEIETNYDDEDEEEEDAYTCLTQSPQILHSPSRIPITNAVSINKLNLDFTLNPNESDKSLVSDTSVDSTGRELDTKTIPELPFCMSSTPEMTPVDEKCNLPSKLLNTSNNSHSDSRSPTASVEDLNISTNLPGADSSQNNPVTTDADALIENDVVRDLQQNMEHIDDAFDEKKVLDEGCSNEPVTFLGENDTRSIVYSNKGTNANVQEFSQEDSLAHSEPKFKDLNATSDDVWNEDKETDANISTSTKSEESYIADYKVTRQEDWDTKKLHQESEHANEQPAIIPQKDSSEETFTELNNESEFQRNFKDGEEYRIVQHEESLYGQRTKSPEENIINGSEIGVDHGEAAEVNEPLAKTSAEEHDLSSSCEDQSVSEARNKDRIEEKEVETKDENIETEKDESEYHKVEENEEPEHVPLLPPLPRWEEIQFNEPFIDENDTSNDSIDLTRSMKPSDYISIWHIQEEEIKSNSPESIANSQFSQQSSITTASTVDSKKDNGSTSFKFKPRIVSRSRIYNPKSRVSSLNYYDNEDYILSNSEWNALDPMRRNTLISKRIQDNIRTQKGHAPLIRPSIMKLNGEDSGFQNHFLEVEQPQEHENIPLSTHLSEQDITTNVGLDEQKLPTNTQDEAEISIREIESAGDITFNRGDLLSLSFDEELGQDFANFLDALDHDSTSFNHGPDDSSSFQRDSSKKSFNSLWESSYELKPPPSIRKQPIAPDVLQKLLESDTKDDADLEKIREERITEPRTGLGIGMLKTPVKDVSIALAASIKGYEASFSDTDSRPEGMNNSDAITLNMFDDFEEDKMTPSTPVRSISPIKRHVSSPFKVVKAGNKQENNEINIKAEEEIEPMTQQETDGLKQDIPPLLAQTKDNVEAKEETITQLEEPQDVEQEFPDMGTLYLSIKAISTLALYGTKSHRATYAIVFDNGENVVQTPWESLPYDGNIRINKEFELPIDFKGKAETSSASSERDSYKKCVITLKCKYEKPRHELVEIVDKVPVGKSFFGKTKYKFEKKYVQKKPKQDEWDYLFAQDGSFARCEIEINEEFLKNVAFNTSHMHYNMINKWSRIADKIHGSKRLYELPRKAPHKVASLDVEACFLERTSAFEQFPKQFSLVNKIVSKYKLQQNIYKEGYLLQDGGDLKGKIENRFFKLHGSQLSGYHEISRKAKIDINLLKVTKVLRNEDIQADNGGQRNFTDWVLFNECFQLVFDDGERITFNAECSNEEKSDWYNKLQEVVELNVFHQPWVKKYCEKLAEEEKTRTTGHNLKQDFN
Protein: GEO09701p1 (Limostatin, isoform A) (RH62559p) (Q6NPB2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFAYTWQLAPLILVILATTMTTTMAAPQQQEVPHALLDIETPNQFNYSPSPLAQPDSLRSKPYFDFLSTLYAHDTAKSNLFRPYSVRQRRDADVQKLSRPRRAIVFRPLFVYKQQEIRKQEIRDRNAQRRHDLNRLQRV
Protein: AP-1 complex subunit beta-1 (Adaptor protein complex AP-1 subunit beta-1) (Adaptor-related protein complex 1 subunit beta-1) (Beta-1-adaptin) (Beta-adaptin 1) (Clathrin assembly protein complex 1 beta large chain) (Golgi adaptor HA1/AP1 adaptin beta subunit) (P52303)
Organism: Rattus norvegicus (Rat)
Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules.
Subcellular location: Golgi apparatus. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.
Interaction partners:
- AP-1 complex subunit gamma
- AP-1 complex subunit mu-2
- AP-1 complex subunit mu-1
- AP complex subunit sigma
- AP complex subunit sigma
- AP complex subunit sigma
- Clathrin heavy chain 1
- AP-2 complex subunit mu
- AP-2 complex subunit alpha
- AP-2 complex subunit sigma
Sequence:
MTDSKYFTTTKKGEIFELKAELNSDKKEKKKEAVKKVIASMTVGKDVSALFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNTFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQLVEDQGFLDTLKDLISDSNPMVVANRVAALSEIAESHPSSNLLDLKAQSINKLLTALNECTEWAQIFILDCLGNYMPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFMEMLSKDLDYYATLLKKLAPPLVTLLSAEPEPQYVPLRNINLIVQKRPEILKHEMKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIKDIFRKYPNKYESVIATLCENLDSLDEPEARAAMIWIVGEYAERIDNADELLESFLDGFHDESTQVQLQLLTAIVKLFLKKPTETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVAAKEVVLAEKPLISEETDLIEPTLLDELICYIGTLASVYHKPPNAFVEGGRGVVHKSLPPRTASSESTESPEAAPAGAPASDQPDVIPAQGDLLGDLLNLDLGPPVSGPPLAASSVQMGAVDLLGGGLDSLMGDEPEGIGDSNFGAPPASVAAAAPARLGAPVSSGLSDLFDLTSGVGTLSGSYVAPKAVWLPAMKAKGLEISGTFTRQVGSISMDLQLTNKALQVMTDFAIQFNRNSFGLAPAAPLQVHAPLSPNQTVEISLPLNTVGSVMKMEPLNNLQVAVKNNIDVFYFSTLYPLHVLFVEDGKMDRQMFLATWKDIPNENEAQFQIRDCPLNTEAASSKLQSSNIFTVAKRTVEGQDMLYQSLKLTNGIWVLAELRIQPGNPSFTLSLKCRAPEVSQHDIQAYETILKN
Protein: Glutathione S-transferase Z2 (AtGSTZ2) (EC 2.5.1.18) (GST class-zeta member 2) (Q9ZVQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- Fumarylacetoacetase
- Homogentisate 1,2-dioxygenase
- Glutathione S-transferase Z1
- Glutathione S-transferase L3
- Elongation factor 1-beta 1
- Elongation factor 1-delta 2
- Elongation factor 1-beta 2
- Glutathione S-transferase U25
- Glutathione S-transferase L2, chloroplastic
- Probable elongation factor 1-gamma 1
Sequence:
MSYVTDFYQAKLKLYSYWRSSCAHRVRIALTLKGLDYEYIPVNLLKGDQSDSDFKKINPMGTVPALVDGDVVINDSFAIIMYLDDKYPEPPLLPSDYHKRAVNYQATSIVMSGIQPHQNMALFRYLEDKINAEEKTAWITNAITKGFTALEKLLVSCAGKYATGDEVYLADLFLAPQIHAAFNRFHINMEPFPTLARFYESYNELPAFQNAVPEKQPDTPSTI
Protein: Ubiquitin carboxyl-terminal hydrolase calypso (EC 3.4.19.12) (BRCA1-associated protein 1 homolog) (BAP1 homolog) (Polycomb group protein calypso) (Q7K5N4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Polycomb group (PcG) protein. Catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-118' (H2AK118ub1). Does not deubiquitinate monoubiquitinated histone H2B. Required to maintain the transcriptionally repressive state of homeotic genes throughout development. The PR-DUB complex has weak or no activity toward 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains.
Subcellular location: Nucleus {ECO:0000269|PubMed:20436459}. Note=Localizes to PcG response elements (PREs). {ECO:0000269|PubMed:20436459}.
Interaction partners:
- Polycomb group protein Asx
- Host cell factor
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome non-ATPase regulatory subunit 14
- Ubiquitin carboxyl-terminal hydrolase
- 26S proteasome non-ATPase regulatory subunit 7
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Polycomb protein PHO
- Chromatin assembly factor 1 p55 subunit
- Histone-lysine N-methyltransferase E
Sequence:
MNAAGGGSGAQAAAVAAGNNSLSHNALLSTASGATTMPMAQLADGWLELESDPGLFTLLLKDFGCHDVQVEEVYDLQKPIESPYGFIFLFRWIEERRARRKIVETTAEIFVKDEEAISSIFFAQQVVPNSCATHALLSVLLNCNENNLQLGDTLSRLKTHTKGMSPENKGLAIGNTPELACAHNSHAMPQARRRLERTGAGVSSCRFTGEAFHFVSFVPINGQLFELDGLKPYPMNHGGWEDSEDWTDKFRRVMAERLGIATGEQDIRFNLMAVVPDRRIAITHKLKMLRTNQAIVSGTLQKLLKADEQGESGNGDSQRPDTPTTLLEPSAFTARDLQSLLKNLDTEIAINEQHLADENDRRHMFKVDASRRTHNYDKFICTFLSMLAHQGVLGELVSQHLLPSKKVSGQGAANRISKQSTTASAGGSTAAGTASTPKTQQQQAAAAKNGKSPSKTPGRRRKGRNKCRKRK
Protein: Small COPII coat GTPase sar1 (EC 3.6.5.-) (Q01475)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Small GTPase component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. Sar1 controls the coat assembly in a stepwise manner. Activated sar1-GTP binds to membranes first and recruits the SEC23/24 complex. These sec23/24-sar1 prebudding intermediates are then collected by the sec13/31 complex as subunits polymerize to form coated transport vesicles. Conversion to sar1-GDP triggers coat release and recycles COPII subunits (By similarity).
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
Interaction partners:
- Membrane glycoprotein spo14
- Protein transport protein sec31
- Protein transport protein sec13
- Protein transport protein sec24
- Protein transport protein sec23-1
- Protein transport protein sec23-2
- COPII coat assembly protein sec16
- Triacylglycerol lipase ptl2
- Probable coatomer subunit gamma
- Uncharacterized protein C4.03c
Sequence:
MFIINWFYDALAMLGLVNKHAKMLFLGLDNAGKTTLLHMLKNDRLAVMQPTLHPTSEELAIGNVRFTTFDLGGHQQARRLWRDYFPEVNGIVYLVDCCDFERLSESKAELDALLAMEELARVPFLILGNKIDAPGAISEDELKAALGLYQTTGKGVSKPVPGIRPIEVFMCSVVLRQGYGEGFKWLAQYV
Protein: C-terminal binding protein 1 (H0Y8W7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XLEKFKALRIIVRIGSGFDNIDIKSAGDLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYRYPPGVVGVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL
Protein: Metal-binding activator 1 (P35192)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulatory protein involved in Cu/Fe utilization and stress resistance. Involved in basal level transcription of FRE1 and H(2)O(2)-induced transcription of CTT1. Regulates the transcription of CTR1 and CTR3 via the copper ion responsive elements in their promoters. Required for degradation of CTR1.
Subcellular location: Nucleus.
Interaction partners:
- Copper transport protein CTR3
- Ferric/cupric reductase transmembrane component 1
- Copper transport protein CTR2
- Ferric/cupric reductase transmembrane component 7
- Ferric/cupric reductase transmembrane component 2
- Iron-regulated transcriptional activator AFT1
- Iron transport multicopper oxidase FET3
Sequence:
MIIFNGNKYACASCIRGHRSSTCRHSHRMLIKVRTRGRPSPMAIRDAILVDSTSQSTEYENGAQIEGDCCSAMNQQPILFVRASAVRKARMINGKLHILMEEGFTAHEPKDISTFTDDGNKYITETEFLRKHSPKAPATGTISPDSTKSSSSSEKKERSRLQQEPIRHFSNCCKKDKSQNPASNGKTNKAPSDDIFTPYGSLESTSAFNDILQENYNSSVPGAHDSSETLTPQSTTTIAAPHSSDVASKVEVLTHKGIFLSTQCSCEDESCPCVNCLIHRSEEELNSYIQQSGVPLTNIGEAQITDKMMDYLDDCKCTDKECICPPDNCTCDGCFSHSTNIIPFEKFFFYGILNARLTRKTQIKFKGKLVPSKYWWDFLKLQVPLMTDAQLELLDIHAWFQKLVSNYAPHLSDATTS
Protein: Syntaxin-124 (AtSYP124) (O64791)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Vesicle trafficking protein that functions in the secretory pathway.
Subcellular location: Membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- UPF0235 protein At5g63440
- VAMP-like protein YKT62
- 25.3 kDa vesicle transport protein SEC22-1
- Putative SNAP25 homologous protein SNAP30
- Putative syntaxin-24
- VAMP-like protein YKT61
- SNAP25 homologous protein SNAP33
- Tlg2p-like protein a
- SNAP25 homologous protein SNAP29
- Syntaxin-31
Sequence:
MNDLFSSSFKKYTDLKQQAQMDDIESGKETMNLDKFFEDVENVKDNMKGVETLYKSLQDSNEECKTVHNAKKVKELRAKMDGDVAQVLKRVKMIKQKLEALEKANANSRNVSGCGPGSSTDRTRTSVVSGLGKKLKDLMDSFQGLRARMNAEYKETVERRYFTITGEQADEQTIENLISSGESENFLQKAIQEQGRGQILDTISEIQERHDAVKEIEKNLIELHQVFLDMAALVESQGQQLNDIESHVSKASSFVRRGTDQLQDAREYQKSSRKWTCYAILLFIVVFALLLIPALPHIMLMLK
Protein: Transketolase 1 (TK 1) (EC 2.2.1.1) (P23254)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Interaction partners:
- Transaldolase NQM1
- Transketolase 2
- Ribulose-phosphate 3-epimerase
- Transaldolase
- Glucose-6-phosphate isomerase
- Ribose-5-phosphate isomerase
- Fructose-bisphosphate aldolase
- Fructose-1,6-bisphosphatase
- Glucose-6-phosphate 1-dehydrogenase
- 6-phosphogluconate dehydrogenase, decarboxylating 1
Sequence:
MTQFTDIDKLAVSTIRILAVDTVSKANSGHPGAPLGMAPAAHVLWSQMRMNPTNPDWINRDRFVLSNGHAVALLYSMLHLTGYDLSIEDLKQFRQLGSRTPGHPEFELPGVEVTTGPLGQGISNAVGMAMAQANLAATYNKPGFTLSDNYTYVFLGDGCLQEGISSEASSLAGHLKLGNLIAIYDDNKITIDGATSISFDEDVAKRYEAYGWEVLYVENGNEDLAGIAKAIAQAKLSKDKPTLIKMTTTIGYGSLHAGSHSVHGAPLKADDVKQLKSKFGFNPDKSFVVPQEVYDHYQKTILKPGVEANNKWNKLFSEYQKKFPELGAELARRLSGQLPANWESKLPTYTAKDSAVATRKLSETVLEDVYNQLPELIGGSADLTPSNLTRWKEALDFQPPSSGSGNYSGRYIRYGIREHAMGAIMNGISAFGANYKPYGGTFLNFVSYAAGAVRLSALSGHPVIWVATHDSIGVGEDGPTHQPIETLAHFRSLPNIQVWRPADGNEVSAAYKNSLESKHTPSIIALSRQNLPQLEGSSIESASKGGYVLQDVANPDIILVATGSEVSLSVEAAKTLAAKNIKARVVSLPDFFTFDKQPLEYRLSVLPDNVPIMSVEVLATTCWGKYAHQSFGIDRFGASGKAPEVFKFFGFTPEGVAERAQKTIAFYKGDKLISPLKKAF
Protein: Coiled-coil domain-containing protein 6 (Papillary thyroid carcinoma-encoded protein) (Protein H4) (Q16204)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000305}. Note=May be a cytoskeletal protein.
Interaction partners:
- Nuclear receptor coactivator 4
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Serine/threonine-protein phosphatase 4 catalytic subunit
- 3-mercaptopyruvate sulfurtransferase
- Tropomyosin alpha-3 chain
- Serine/threonine-protein phosphatase 4 regulatory subunit 1
- Protein patched homolog 1
- E3 ubiquitin-protein ligase TRIM33
- Sodium-dependent phosphate transport protein 2B
- Proto-oncogene tyrosine-protein kinase ROS
Sequence:
MADSASESDTDGAGGNSSSSAAMQSSCSSTSGGGGGGGGGGGGGKSGGIVISPFRLEELTNRLASLQQENKVLKIELETYKLKCKALQEENRDLRKASVTIQARAEQEEEFISNTLFKKIQALQKEKETLAVNYEKEEEFLTNELSRKLMQLQHEKAELEQHLEQEQEFQVNKLMKKIKKLENDTISKQLTLEQLRREKIDLENTLEQEQEALVNRLWKRMDKLEAEKRILQEKLDQPVSAPPSPRDISMEIDSPENMMRHIRFLKNEVERLKKQLRAAQLQHSEKMAQYLEEERHMREENLRLQRKLQREMERREALCRQLSESESSLEMDDERYFNEMSAQGLRPRTVSSPIPYTPSPSSSRPISPGLSYASHTVGFTPPTSLTRAGMSYYNSPGLHVQHMGTSHGITRPSPRRSNSPDKFKRPTPPPSPNTQTPVQPPPPPPPPPMQPTVPSAATSQPTPSQHSAHPSSQP
Protein: Cytochrome P450 (EC 1.14.14.1) (Q9WV19)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU368053}. Microsome membrane {ECO:0000256|RuleBase:RU368053}.
Interaction partners:
Sequence:
MMLGGAFSIFMALCLSCLLILIAWKRTSKGGKLPPGPTPIPFLGNFLQVRTDATFQSFQKLQKKYGSVFTVYFGPRPVVVLCGHEAVKEALVDQADDFSGRGEMPTLEKNFQGYGLALSNGERWKILRRFSLTVLRNFGMGKRSIEERIQEEAGYLLEELHKVKGAPIDPTLYLSRTVSNVICSVVFGKRFDYQDQRFQSLMRMINESFVEMSKPWAQLYDMYWKVMQYFPGRHNYLYNLIEDLKDFIASRVKINEASFDPSNPRDFIDCFLIKMHQDKSDPHTEFNLKNLVLTTLNLFFAGTETVSSTLRYGFLLLLKYPEVEAKIHEEINQVIGTHRTPRVDDRAKMPYTDAVIHEIQRLTDIVPLGVPHNVTRDTHFRGYLLPKGTDVYPLFGSVLKDPKYFRYPDAFYPQHFLDEQGRFKKNDAFVVFSSGKRICVGEALARMELFLYFTSILQRFSLRSLVPPADIDIAHKISGFGNIPPVYELCFMAR
Protein: Alanine racemase N-terminal domain-containing protein (Q9HTM9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable oxidoreductase
- Probable cytochrome c
- Lipoprotein
- Neutral ceramidase
- Probable transcriptional regulator
- Low specificity L-threonine aldolase
- Low specificity L-threonine aldolase
Sequence:
MRPADRGGPYDDYFRALNRELKANGPMCPVLLIDLDRLDHNIDVVMRSVRRGGKHLRLVEKSLPSPGLLAYIARRAGTRRLMSFHQPFLNHDAVAFADADILLGKPLPVRSAELFYREHKGAFDPARQLQWLIDTPQRLRQYLALAQGLGTRMRVNIELDVGLHRGGVADQAALGELLALIAAHPQYLEFAGFMGYDPFVGMGVPGILGSPEELFAKVMALYQGHVDFARQRFAALWTPQLTLNTAGSPSYRMHEKETLSSEVSVGTAMLKPSHYDLASLAEHVPAVYIATPVLKSTGAVQIPALDGKSRLFSWWDPNQRGTFFIYGGNWMADFASPEGLRSNGIYGRSSNQEMVNGSPSVGLEVDDQVFLRPTQSESVLLQFGDLLALRGGRIVERWPVYA
Protein: Meis homeobox 2 (A0A8I6AHY1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MFLYDELPHYGGMDGVGVPASMYGDPHAPRPIPPVHHLNHGPPLHATQHYGAHAPHPNVMPASMGSAVNDALKRDKDAIYGHPLFPLLALVFEKCELATCTPREPGVAGGDVCSSDSFNEDIAVFAKQVRAEKPLFSSNPELDNLMIQAIQVLRFHLLELEKVHELCDNFCHRYISCLKGKMPIDLVIDERDGSSKSDHEELSGSSTNLADHNPSSWRDHDDATSTHSAGTPGPSSGGHASQSGDNSSEQGDGLDNSVASPGTGDDDDPDKDKKRQKKRGIFPKVATNIMRAWLFQHLTHPYPSEEQKKQLAQDTGLTILQVNNWFINARRRIVQPMIDQSNRAGFLLDPSVSQGAAYSPEGQPMGSFVLDGQQHMGIRPAGPMSGMGMNMGMDGQWHYM
Protein: Adrenocortical dysplasia protein homolog (POT1 and TIN2-interacting protein) (Q96AP0)
Organism: Homo sapiens (Human)
Function: Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded TTAGGG repeats added by telomerase and protects chromosome ends. Without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Promotes binding of POT1 to single-stranded telomeric DNA. Modulates the inhibitory effects of POT1 on telomere elongation. The ACD-POT1 heterodimer enhances telomere elongation by recruiting telomerase to telomeres and increasing its processivity. May play a role in organogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:15181449, ECO:0000269|PubMed:25205116, ECO:0000269|PubMed:25233904}. Chromosome, telomere {ECO:0000269|PubMed:15181449, ECO:0000269|PubMed:25205116, ECO:0000269|PubMed:25233904}.
Interaction partners:
- Telomeric repeat-binding factor 1
- Telomeric repeat-binding factor 2-interacting protein 1
- TERF1-interacting nuclear factor 2
- Telomeric repeat-binding factor 2
- Protection of telomeres protein 1
- Telomerase reverse transcriptase
- CST complex subunit STN1
- CST complex subunit CTC1
- CST complex subunit TEN1
- Histone H2B type 2-F
Sequence:
MAGSGRLVLRPWIRELILGSETPSSPRAGQLLEVLQDAEAAVAGPSHAPDTSDVGATLLVSDGTHSVRCLVTREALDTSDWEEKEFGFRGTEGRLLLLQDCGVHVQVAEGGAPAEFYLQVDRFSLLPTEQPRLRVPGCNQDLDVQKKLYDCLEEHLSESTSSNAGLSLSQLLDEMREDQEHQGALVCLAESCLTLEGPCTAPPVTHWAASRCKATGEAVYTVPSSMLCISENDQLILSSLGPCQRTQGPELPPPDPALQDLSLTLIASPPSSPSSSGTPALPGHMSSEESGTSISLLPALSLAAPDPGQRSSSQPSPAICSAPATLTPRSPHASRTPSSPLQSCTPSLSPRSHVPSPHQALVTRPQKPSLEFKEFVGLPCKNRPPFPRTGATRGAQEPCSVWEPPKRHRDGSAFQYEYEPPCTSLCARVQAVRLPPQLMAWALHFLMDAQPGSEPTPM