wanglab/gogpt-training-data huggingface dataset:
Protein: Microtubule-associated protein RP/EB family member 1B (APC-binding protein EB1B) (End-binding protein 1) (AtEB1) (End-binding protein 1B) (AtEB1B) (Protein ATEB1 homolog 2) (ATEB1H2) (Q9FJJ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. May be involved in anchoring microtubules to their nucleation sites and/or functioning as a reservoir for distribution to the growing end. In plants, microtubule minus ends are not necessarily severed from the nucleation site and transported to the plus end of a microtubule as part of the recycling process. May play a role in endomembrane organization during polarized growth of plant cells.
Subcellular location: Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, phragmoplast. Note=Localizes both to the plus ends of microtubules and to the sites of nucleation during division and interphase.
Interaction partners:
- Protein SPIRAL1
- CLIP-associated protein
- Tubulin beta-6 chain
- Tubulin alpha-6 chain
- Mitotic spindle checkpoint protein MAD2
- Protein MOR1
- Serine/threonine-protein kinase Aurora-2
- Mitotic checkpoint protein BUB3.2
- Kinesin-like protein KIN-14D
- Mitotic checkpoint protein BUB3.1
Sequence:
MATNIGMMDSAYFVGRNEILSWINDRLHLNLSRIEEAASGAVQCQMLDMTFPGVVPMHKVNFEAKNEYEMIQNYKVMQEVFTKLKITKPLEVNRLVKGRPLDNLEFLQWLKRFCDSINGGIMNENYNPVERRSRGGREKSVKGSSKISKSLQTNNMHHPPVATSNKPAGPKQAKSHGIGGGSNSSAEVQALSKEVEDLKVSVDLLEKERDFYFSKLRDIEILCQTPELDDLPIVVAVKKILYATDANESVLEEAQECLNQSLGLEGYEEEGKEEEEEEEEEEEEAAAAAETQT
Protein: Mannitol-1-phosphate 5-dehydrogenase (EC 1.1.1.17) (P09424)
Organism: Escherichia coli (strain K12)
Interaction partners:
- PTS system mannitol-specific EIICBA component
- PTS system mannitol-specific cryptic EIICB component
- Hexitol phosphatase B
- Mannitol operon repressor
- Hexitol phosphatase A
- Mannose-6-phosphate isomerase
- Sorbitol-6-phosphate 2-dehydrogenase
- Mannitol-specific cryptic phosphotransferase enzyme IIA component
- ATP-dependent 6-phosphofructokinase isozyme 1
- Fructokinase
Sequence:
MKALHFGAGNIGRGFIGKLLADAGIQLTFADVNQVVLDALNARHSYQVHVVGETEQVDTVSGVNAVSSIGDDVVDLIAQVDLVTTAVGPVVLERIAPAIAKGQVKRKEQGNESPLNIIACENMVRGTTQLKGHVMNALPEDAKAWVEEHVGFVDSAVDRIVPPSASATNDPLEVTVETFSEWIVDKTQFKGALPNIPGMELTDNLMAFVERKLFTLNTGHAITAYLGKLAGHQTIRDAILDEKIRAVVKGAMEESGAVLIKRYGFDADKHAAYIQKILGRFENPYLKDDVERVGRQPLRKLSAGDRLIKPLLGTLEYGLPHKNLIEGIAAAMHFRSEDDPQAQELAALIADKGPQAALAQISGLDANSEVVSEAVTAYKAMQ
Protein: Flagellar hook-basal body complex protein FlhO (P39752)
Organism: Bacillus subtilis (strain 168)
Function: Not required for motility.
Interaction partners:
- Flagellar basal-body rod protein FlgC
- Flagellar hook-basal body complex protein FlhP
- Flagellar motor switch phosphatase FliY
- Flagellar basal body rod protein FlgB
- Flagellar hook-basal body complex protein FliE
- FlaA locus uncharacterized protein YlxG
- Flagellar secretion chaperone FliS
- Flagellar M-ring protein
- Flagellar motor switch protein FliG
- Flagellar hook-associated protein 1
Sequence:
MLKGLYTATSAMIAQQRRTEMLSNNIANANTSGYKADQGSMRAFPEMLLSRIESKSPAGTSRTEIGSVNTGVYMQELKPLFTQGSLKSTDQPTDIALIENQVPMSAETNEKAALFYPVQTADGIRYSKSSTFSLNENNQLTINGRPILSTDRQPITVDNENFTVSENGTVTTNGRTAGQIDVRMAEDVRNLKRDGNDLYSTADGNDLPSAAGNNQVAYSLKQGVSELSNVDVTSAYTEMTEAYRSFEANQKVIQAYDKSMDKAANEIGKI
Protein: Kelch-like protein 31 (BTB and kelch domain-containing protein 6) (Kelch repeat and BTB domain-containing protein 1) (Kelch-like protein KLHL) (Q9H511)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor in MAPK/JNK signaling pathway to regulate cellular functions. Overexpression inhibits the transcriptional activities of both the TPA-response element (TRE) and serum response element (SRE).
Interaction partners:
- N-terminal Xaa-Pro-Lys N-methyltransferase 1
- Large ribosomal subunit protein uL23
- Cullin-3
Sequence:
MAPKKKIVKKNKGDINEMTIIVEDSPLNKLNALNGLLEGGNGLSCISSELTDASYGPNLLEGLSKMRQENFLCDLVIGTKTKSFDVHKSVMASCSEYFYNILKKDPSIQRVDLNDISPLGLATVIAYAYTGKLTLSLYTIGSIISAAVYLQIHTLVKMCSDFLIREMSVENCMYVVNIAETYSLKNAKAAAQKFIRDNFLEFAESDQFMKLTFEQINELLIDDDLQLPSEIVAFQIAMKWLEFDQKRVKYAADLLSNIRFGTISAQDLVNYVQSVPRMMQDADCHRLLVDAMNYHLLPYHQNTLQSRRTRIRGGCRVLVTVGGRPGLTEKSLSRDILYRDPENGWSKLTEMPAKSFNQCVAVMDGFLYVAGGEDQNDARNQAKHAVSNFCRYDPRFNTWIHLASMNQKRTHFSLSVFNGLVYAAGGRNAEGSLASLECYVPSTNQWQPKTPLEVARCCHASAVADGRVLVTGGYIANAYSRSVCAYDPASDSWQELPNLSTPRGWHCAVTLSDRVYVMGGSQLGPRGERVDVLTVECYSPATGQWSYAAPLQVGVSTAGVSALHGRAYLVGGWNEGEKKYKKCIQCFSPELNEWTEDDELPEATVGVSCCTLSMPNNVTRESRASSVSSVPVSI
Protein: REST corepressor 1 (Protein CoREST) (Q9UKL0)
Organism: Homo sapiens (Human)
Function: Essential component of the BHC complex, a corepressor complex that represses transcription of neuron-specific genes in non-neuronal cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts by deacetylating and demethylating specific sites on histones, thereby acting as a chromatin modifier. In the BHC complex, it serves as a molecular beacon for the recruitment of molecular machinery, including MeCP2 and SUV39H1, that imposes silencing across a chromosomal interval. Plays a central role in demethylation of Lys-4 of histone H3 by promoting demethylase activity of KDM1A on core histones and nucleosomal substrates. It also protects KDM1A from the proteasome. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development and controls hematopoietic differentiation.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:10734093, ECO:0000269|PubMed:15897453}. Note=Upon infection by HSV-1, it is partially translocated into the cytoplasm in an HSV-1-dependent manner.
Interaction partners:
- Histone deacetylase 1
- PHD finger protein 21A
- Paired amphipathic helix protein Sin3a
- C-terminal-binding protein 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1-related
- Histone deacetylase 2
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- RE1-silencing transcription factor
- Zinc finger protein 217
- Mediator of RNA polymerase II transcription subunit 12
Sequence:
MPAMVEKGPEVSGKRRGRNNAAASASAAAASAAASAACASPAATAASGAAASSASAAAASAAAAPNNGQNKSLAAAAPNGNSSSNSWEEGSSGSSSDEEHGGGGMRVGPQYQAVVPDFDPAKLARRSQERDNLGMLVWSPNQNLSEAKLDEYIAIAKEKHGYNMEQALGMLFWHKHNIEKSLADLPNFTPFPDEWTVEDKVLFEQAFSFHGKTFHRIQQMLPDKSIASLVKFYYSWKKTRTKTSVMDRHARKQKREREESEDELEEANGNNPIDIEVDQNKESKKEVPPTETVPQVKKEKHSTQAKNRAKRKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGIEPYRLPEVIQKCNARWTTEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRRFNIDEVLQEWEAEHGKEETNGPSNQKPVKSPDNSIKMPEEEDEAPVLDVRYASAS
Protein: Trifunctional enzyme subunit alpha, mitochondrial (78 kDa gastrin-binding protein) (Monolysocardiolipin acyltransferase) (MLCL AT) (EC 2.3.1.-) (TP-alpha) [Includes: Long-chain enoyl-CoA hydratase (EC 4.2.1.17); Long chain 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.211)] (P40939)
Organism: Homo sapiens (Human)
Function: Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through four consecutive reactions breaking down fatty acids into acetyl-CoA. Among the enzymes involved in this pathway, the trifunctional enzyme exhibits specificity for long-chain fatty acids. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA described here carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities while the trifunctional enzyme subunit beta/HADHB bears the 3-ketoacyl-CoA thiolase activity. Independently of the subunit beta, the trifunctional enzyme subunit alpha/HADHA also has a monolysocardiolipin acyltransferase activity. It acylates monolysocardiolipin into cardiolipin, a major mitochondrial membrane phospholipid which plays a key role in apoptosis and supports mitochondrial respiratory chain complexes in the generation of ATP. Allows the acylation of monolysocardiolipin with different acyl-CoA substrates including oleoyl-CoA for which it displays the highest activity.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:29915090}. Mitochondrion inner membrane {ECO:0000269|PubMed:29915090}. Note=Protein stability and association with mitochondrion inner membrane do not require HADHB. {ECO:0000269|PubMed:29915090}.
Interaction partners:
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 1
- Enoyl-CoA hydratase, mitochondrial
Sequence:
MVACRAIGILSRFSAFRILRSRGYICRNFTGSSALLTRTHINYGVKGDVAVVRINSPNSKVNTLSKELHSEFSEVMNEIWASDQIRSAVLISSKPGCFIAGADINMLAACKTLQEVTQLSQEAQRIVEKLEKSTKPIVAAINGSCLGGGLEVAISCQYRIATKDRKTVLGTPEVLLGALPGAGGTQRLPKMVGVPAALDMMLTGRSIRADRAKKMGLVDQLVEPLGPGLKPPEERTIEYLEEVAITFAKGLADKKISPKRDKGLVEKLTAYAMTIPFVRQQVYKKVEEKVRKQTKGLYPAPLKIIDVVKTGIEQGSDAGYLCESQKFGELVMTKESKALMGLYHGQVLCKKNKFGAPQKDVKHLAILGAGLMGAGIAQVSVDKGLKTILKDATLTALDRGQQQVFKGLNDKVKKKALTSFERDSIFSNLTGQLDYQGFEKADMVIEAVFEDLSLKHRVLKEVEAVIPDHCIFASNTSALPISEIAAVSKRPEKVIGMHYFSPVDKMQLLEIITTEKTSKDTSASAVAVGLKQGKVIIVVKDGPGFYTTRCLAPMMSEVIRILQEGVDPKKLDSLTTSFGFPVGAATLVDEVGVDVAKHVAEDLGKVFGERFGGGNPELLTQMVSKGFLGRKSGKGFYIYQEGVKRKDLNSDMDSILASLKLPPKSEVSSDEDIQFRLVTRFVNEAVMCLQEGILATPAEGDIGAVFGLGFPPCLGGPFRFVDLYGAQKIVDRLKKYEAAYGKQFTPCQLLADHANSPNKKFYQ
Protein: STE20/SPS1-related proline-alanine-rich protein kinase (Ste-20-related kinase) (EC 2.7.11.1) (DCHT) (Serine/threonine-protein kinase 39) (Q9UEW8)
Organism: Homo sapiens (Human)
Function: May act as a mediator of stress-activated signals. Mediates the inhibition of SLC4A4, SLC26A6 as well as CFTR activities by the WNK scaffolds, probably through phosphorylation. Phosphorylates RELT.
Subcellular location: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000305}. Note=Nucleus when caspase-cleaved. {ECO:0000305}.
Interaction partners:
- Solute carrier family 12 member 2
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Solute carrier family 12 member 6
- Solute carrier family 12 member 3
- Protein transport protein Sec61 subunit gamma
- Translocation protein SEC62
- Calcium-binding protein 39
- ATP-sensitive inward rectifier potassium channel 1
- Translocation protein SEC63 homolog
- Protein transport protein Sec61 subunit beta
Sequence:
MAEPSGSPVHVQLPQQAAPVTAAAAAAPAAATAAPAPAAPAAPAPAPAPAAQAVGWPICRDAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPNVVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGLDYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDKEMMKKYGKSFRKLLSLCLQKDPSKRPTAAELLKCKFFQKAKNREYLIEKLLTRTPDIAQRAKKVRRVPGSSGHLHKTEDGDWEWSDDEMDEKSEEGKAAFSQEKSRRVKEENPEIAVSASTIPEQIQSLSVHDSQGPPNANEDYREASSCAVNLVLRLRNSRKELNDIRFEFTPGRDTADGVSQELFSAGLVDGHDVVIVAANLQKIVDDPKALKTLTFKLASGCDGSEIPDEVKLIGFAQLSVS
Protein: Proline dehydrogenase, mitochondrial (EC 1.5.5.2) (Proline oxidase) (P09368)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Converts proline to delta-1-pyrroline-5-carboxylate.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Proline utilization trans-activator
- Pyrroline-5-carboxylate reductase
- Urea active transporter
- Arginase
- Glutamate 5-kinase
- 4-aminobutyrate aminotransferase
- Ornithine aminotransferase
- Gamma-glutamyl phosphate reductase
- Succinate-semialdehyde dehydrogenase [NADP
Sequence:
MIASKSSLLVTKSRIPSLCFPLIKRSYVSKTPTHSNTAANLMVETPAANANGNSVMAPPNSINFLQTLPKKELFQLGFIGIATLNSFFLNTIIKLFPYIPIPVIKFFVSSLYCGGENFKEVIECGKRLQKRGISNMMLSLTIENSEGTKSLSSTPVDQIVKETISSVHNILLPNIIGQLESKPINDIAPGYIALKPSALVDNPHEVLYNFSNPAYKAQRDQLIENCSKITKEIFELNQSLLKKYPERKAPFMVSTIDAEKYDLQENGVYELQRILFQKFNPTSSKLISCVGTWQLYLRDSGDHILHELKLAQENGYKLGLKLVRGAYIHSEKNRNQIIFGDKTGTDENYDRIITQVVNDLIINGEDSYFGHLVVASHNYQSQMLVTNLLKSTQDNSYAKSNIVLGQLLGMADNVTYDLITNHGAKNIIKYVPWGPPLETKDYLLRRLQENGDAVRSDNGWPLIKAIAKSIPKRVGL
Protein: Protein orai (Store-operated calcium channel) (Q09232)
Organism: Caenorhabditis elegans
Function: Ca(2+) release-activated Ca(2+)-like (CRAC-like) channel subunit which mediates Ca(2+) influx and increase in Ca(2+)-selective current by synergy with the Ca(2+) sensor, stim-1. Required for Ca(2+) and IP3-dependent contractile activity of sheath cells and the spermatheca. Affects brood size and somatic cell function.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Stromal interaction molecule 1
- Inositol 1,4,5-trisphosphate receptor itr-1
- START domain-containing protein
Sequence:
MPRSHDPSRVELLRKEGGLTEKRVSISVEDIRGAVANWKNSGGAGDPITPYPLPQFFLQPPSTAGGGSRNGVGSKEGSVTSLRMPLKKAGDDVDLGHRGELDLSEKYNYDLSRAQLKASSRTSALLAGFAMVCLVELQYDQSTPKPLLIVLGVVTSLLVSVHLLALMMSTCILPYMEATGCTQDSPHIKLKFYIDLSWLFSTCIGLLLFLVEIGVIFYVKFTAVGYPTAGYITTAMLVPVGVVFVVFSYLIHKNRVSHSLGRFKHKVDTMKQFLDVEANLQKSTLAPSTIRDI
Protein: Spectinomycin 9-adenylyltransferase (AAD(9)) (Q07448)
Organism: Enterococcus faecalis (Streptococcus faecalis)
Function: Mediates bacterial resistance to the antibiotic spectinomycin but not streptomycin.
Interaction partners:
Sequence:
MRRIYLNTYEQINKVKKILRKHLKNNLIGTYMFGSGVESGLKPNSDLDFLVVVSEPLTDQSKEILIQKIRPISKKIGDKSNLRYIELTIIIQQEMVPWNHPPKQEFIYGEWLQELYEQGYIPQKELNSDLTIMLYQAKRKNKRIYGNYDLEELLPDIPFSDVRRAIMDSSEELIDNYQDDETNSILTLCRMILTMDTGKIIPKDIAGNAVAESSPLEHRERILLAVRSYLGENIEWTNENVNLTINYLNNRLKKL
Protein: PAN2-PAN3 deadenylation complex subunit PAN3 (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 3) (PAN deadenylation complex subunit 3) (Q58A45)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. PAN3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit PAN2 to mRNA via its interaction with RNA and PABP, and to miRNA targets via its interaction with GW182 family proteins.
Subcellular location: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:14583602, ECO:0000269|PubMed:18625844}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus {ECO:0000269|PubMed:28559491}. Note=Shuttles between cytoplasm and nucleus. {ECO:0000269|PubMed:28559491}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|PubMed:28559491}.
Interaction partners:
- PAN2-PAN3 deadenylation complex catalytic subunit PAN2
- Polyadenylate-binding protein 1
- Trinucleotide repeat-containing gene 6C protein
- Nipped-B-like protein
Sequence:
MNSGGGLPPPSAAASPSSSSLAAAVAVVAPPGVGGVPGGAAVGVKLKYCRYYAKDKTCFYGEECQFLHEDPAAGAAPGLGLHSNSVPLALAGAPVAGFPPGAVAGGGAGPPPGPKKPDLGDPGTGAAAGGGGSSGGLDGPRLAIPGMDGGALTDTSLTDSYFSTSFIGVNGFGSPVETKYPLMQRMTNSSSSPSLLNDSAKPYSAHDPLTSPASSLFNDFGALNISQRRKPRKYRLGMLEERLVPMGSKARKAKNPIGCLADRCKSGVPINMVWWNRVTENNLQTPNPTASEFIPKGGSTSRLSNVSQSNMSAFSQVFSHPSMGSPATAGLAPGMSLSAGSSPLHSPKITPHTSPAPRRRSHTPNPASYMVPSSASTSVNNPVSQTPSSGQVIQKETVGGTTYFYTDTTPAPLTGMVFPNYHIYPPTAPHVAYMQPKANAPSFFMADELRQELINRHLITMAQIDQADMPAVPTEVDSYHSLFPLEPLPPPNRIQKSSNFGYITSCYKAVNSKDDLPYCLRRIHGFRLVNTKCMVLVDMWKKIQHSNIVTLREVFTTKAFAEPSLVFAYDFHAGGETMMSRHFNDPNADAYFTKRKWGQHEGPLPRQHAGLLPESLIWAYIVQLSSALRTIHTAGLACRVMDPTKILITGKTRLRVNCVGVFDVLTFDNSQNNNPLALMAQYQQADLISLGKVVLALACNSLAGIQRENLQKAMELVTINYSSDLKNLILYLLTDQNRMRSVNDIMPMIGARFYTQLDAAQMRNDVIEEDLAKEVQNGRLFRLLAKLGTINERPEFQKDPTWSETGDRYLLKLFRDHLFHQVTEAGAPWIDLSHIISCLNKLDAGVPEKISLISRDEKSVLVVTYSDLKRCFENTFQELIAAANGQL
Protein: Glutamine synthetase (EC 6.3.1.2) (A8WCU5)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSLLTDLVNLNLSDCTDKIIAEYIWIGGSGMDLRSKARTLSGPVSDPSKLPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRRGNNILVMCDAYTPAGEPIPTNKRCNAAKIFSHPDVAAEEPWYGIEQEYTLLQKDVKWPIGWPLGGYPGPQGPYYCGVGVDKAYGRDIVDSHYKACLYAGINISGINGEVMPGQWEFQVGPAVGISAGDELWVARYILERITEIAGVVLSFDPKPIQGDWNGAGAHTNYSTKSMRSDGGYEVIKKAIAKLGLRHKEHIAAYGEGNERRLTGRHETADINTFLWGVANRGASIRVGRDIEKAGKGYFEDRRPASNMDPYVVTSMIAETTILWKP
Protein: Dioxygenase for synthesis of lipid (H9L4A3)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Interaction partners:
- Lipid A acyltransferase PagP
- Phosphoethanolamine transferase EptA
- Lipid A biosynthesis acyltransferase
- Lipid A 1-diphosphate synthase
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Kdo
- Outer membrane protein
- Lipid A biosynthesis acyltransferase
- Virulence transcriptional regulatory protein PhoP
- Virulence sensor histidine kinase PhoQ
Sequence:
MFAAIIIGIFIISVIYAHSRGVEKQKLSRQLFDHSTFMAPINMFMTRFSTLPAKQPYFDTTAFPELQKLTENWQVIREEALQLQHHIKAAQANNDAGFNTFFKRGWKRFYLKWYSDAHPSAETLCPITTKLVNSIPSIKAAMFAELPPGAYLGKHRDPYAGSVRYHLGLSTPNDDRCFIEVDRQRHSWRDGKAVIFDETYVHWAENKTEQTRIILFCDIERPMKWRWAQSVNHWVGASLMSAASSPNDENDRTGAINRIFKYVHAARDAGQRLKKKNRTLYYALKYLVIAAIFAAIILFSLL
Protein: Calcitonin [Cleaved into: Calcitonin (CT); Katacalcin (Calcitonin carboxyl-terminal peptide) (CCP) (PDN-21)] (P01258)
Organism: Homo sapiens (Human)
Function: Calcitonin causes a rapid but short-lived drop in the level of calcium and phosphate in blood by promoting the incorporation of those ions in the bones.
Subcellular location: Secreted.
Interaction partners:
- Calcitonin gene-related peptide type 1 receptor
- Calcitonin receptor
- Receptor activity-modifying protein 1
- Receptor activity-modifying protein 2
- Islet amyloid polypeptide
- Receptor activity-modifying protein 3
- Pro-adrenomedullin
- Calcitonin gene-related peptide 2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MGFQKFSPFLALSILVLLQAGSLHAAPFRSALESSPADPATLSEDEARLLLAALVQDYVQMKASELEQEQEREGSSLDSPRSKRCGNLSTCMLGTYTQDFNKFHTFPQTAIGVGAPGKKRDMSSDLERDHRPHVSMPQNAN
Protein: Uncharacterized PPE family protein PPE63 (P9WHX5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MADFLTLSPEVNSARMYAGGGPGSLSAAAAAWDELAAELWLAAASFESVCSGLADRWWQGPSSRMMAAQAARHTGWLAAAATQAEGAASQAQTMALAYEAAFAATVHPALVAANRALVAWLAGSNVFGQNTPAIAAAEAIYEQMWAQDVVAMLNYHAVASAVGARLRPWQQLLHELPRRLGGEHSDSTNTELANPSSTTTRITVPGASPVHAATLLPFIGRLLAARYAELNTAIGTNWFPGTTPEVVSYPATIGVLSGSLGAVDANQSIAIGQQMLHNEILAATASGQPVTVAGLSMGSMVIDRELAYLAIDPNAPPSSALTFVELAGPERGLAQTYLPVGTTIPIAGYTVGNAPESQYNTSVVYSQYDIWADPPDRPWNLLAGANALMGAAYFHDLTAYAAPQQGIEIAAVTSSLGGTTTTYMIPSPTLPLLLPLKQIGVPDWIVGGLNNVLKPLVDAGYSQYAPTAGPYFSHGNLVW
Protein: Outer membrane protein Rv1973 (P9WJ77)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:18439872}.
Interaction partners:
- Probable conserved Mce associated membrane protein
- Mce-family protein Mce3C
- Possible Mce-family lipoprotein LprM
- Mce-family protein Mce3A
- Mce-family protein Mce3F
- SCP domain-containing protein
- Mce-family protein Mce3B
- Probable conserved membrane protein
- Mce-family protein Mce3D
- Uncharacterized protein Rv1351
Sequence:
MSWSRVIAYGLLPGLALALTCGAGLLKWQDGAVRDAAVARAESVRAATDGTTALLSYRPDTVQHDLESARSRLTGTFLDAYTQLTHDVVIPGAQQKQISAVATVAAAASVSTSADRAVVLLFVNQTITVGKDAPTTAASSVRVTLDNINGRWLISQFEPI
Protein: Zona pellucida sperm-binding protein 2 (75 kDa zona pellucida protein) (Zona pellucida glycoprotein 2) (Zp-2) (Zona pellucida protein A) [Cleaved into: Processed zona pellucida sperm-binding protein 2] (P48829)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP2 may act as a secondary sperm receptor.
Subcellular location: [Processed zona pellucida sperm-binding protein 2]: Zona pellucida {ECO:0000250|UniProtKB:P20239}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20239}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Zona pellucida sperm-binding protein 3
- Growth/differentiation factor 9
- Zona pellucida sperm-binding protein 1
- Factor in the germline alpha
- Bone morphotic protein 15
- Izumo sperm-egg fusion 1
- Zonadhesin
- NLR family pyrin domain containing 5
- NOBOX oogenesis homeobox
Sequence:
PGTVTCNENEIIVEFPSYVGTKTLHASVVDPLGVEMLNCTYILDPEKLTLRVPYKACTRAVHGGYQMSIRVMNNSAALRHTDVEYQFFCPVEQTLEFSKSAACTKDFMSLSFPHIPTGLGDSTMVNESQMGWMVQAGHGPGAQTLSLEEAKGQGFGVLIDDNKMTLSVLLNATGVTHYVEGTSHLHTMFLKLSLVSPGQKMPFPSRAICLSGPVTCNATHMTLTIPEFPGKLESVSIENRNITVSQLHDQGIDVEAINGLRLHFSKTVLKTKFSEKCLHDQLYISSLKLTFNLELDTVSTVINPECPCDSPASIVSGELCTQDGFMDFEVYTHQTKPALNLDTLRVGSSSCQPVFKAQSQGLVRFRIPLNGCGTRHKFEDEKVIYENEVHALWENLPPSKISRDSEFRMTVQCYYTRDDMLLNANIKSLPPPVASVKPGPLALSLQTYPDESYQQPYRVNEYPIVKYLRQPIYMEVRVLNRNDPNIKLALDDCWATSSMDPASLPKWSIVMDGCEYSLDNYQTNFHPVGSSVTHPEHYQRFDVKTFAFVSEAQARSSLVYFHCSALICNQHYPDSPLCSVTCPGSSRHRRATGNTEEERVTASLPGPILLLPNGSSFRGVGDSKEHGMAGDVTSKTMAAVAAVAGVVATLGFISYLCKKRTMMLSH
Protein: Probable UDP-arabinopyranose mutase 1 (EC 5.4.99.30) (Reversibly glycosylated polypeptide 1) (RGP1) (UDP-L-arabinose mutase 1) (UDP-glucose:protein transglucosylase) (UPTG) (O04300)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: Probable UDP-L-arabinose mutase involved in the biosynthesis of cell wall non-cellulosic polysaccharides (By similarity). Was initially shown to possess an autoglycosylating activity which is dependent on the presence of UDP-glucose and manganese.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:9207152}. Cell junction, plasmodesma {ECO:0000269|PubMed:9207152}. Golgi apparatus {ECO:0000269|PubMed:9207152}. Note=Cell wall-associated, with highest concentrations on plasmodesmata. Also located in the Golgi apparatus. {ECO:0000269|PubMed:9207152}.
Interaction partners:
Sequence:
MASLPKPTPLLKDELDIVIPTIRNLDFLEMWRPFFEQYHLIIVQDGDPSKVIKVPEGFDYELYNRNDINRILGPKASCISFKDSACRCFGYMVSKKKYIYTIDDDCFVAKDPTGHEINALEQHIKNLLSPSTPFFFNTLYDPYREGTDFVRGYPFSLREGVPTAVSHGLWLNIPDYDAPTQLVKPHERNTRFVDAVLTIPKGSLFPMCGMNLAFNRELIGPAMYFGLMGDGQPIGRYDDMWAGWCIKVICDHLGYGVKTGLPYIWHSKASNPFVNLKKEYKGIFWQEEIIPFFQAATLSKDCTSVQKCYIELSKQVKEKLGTIDPYFIKLADAMVTWVEAWDEINNNKSEETTSTKASEVAATK
Protein: Transcription factor Atoh7-a (Atonal bHLH transcription factor 7-A) (Helix-loop-helix protein xATH-5-A) (Protein atonal homolog 5-A) (xAth5-A) (Protein atonal homolog 7-A) (O13125)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that binds to DNA at the consensus sequence 5'-CAG[GC]TG-3' (By similarity). Positively regulates the determination of retinal ganglion cell fate and formation of the optic nerve and retino-hypothalamic tract. Required for retinal circadian rhythm photoentrainment (By similarity). Plays a role in brainstem auditory signaling and binaural processing (By similarity). Regulates the differentiation of olfactory receptor neurons. During retinal neurogenesis, activates the transcription of several genes such as brn3d, coe3, cbfa2t2, glis2, elrC and xgadd45-gamma.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8N100}. Perikaryon {ECO:0000250|UniProtKB:Q9Z2E5}. Cell projection, axon {ECO:0000250|UniProtKB:Q9Z2E5}.
Interaction partners:
Sequence:
MKSDSPVHRESHTGCQSPCPLRCLPARLEGSTKRRLAANARERRRMQGLNTAFDSLRKVVPQWGEDKQLSKYETLQMALSYIMALSRILSEAERYSRTDPEEWTNIQYDHIEEEQCLSYMEVRCPRDCDRYLPQTFSH