wanglab/gogpt-training-data huggingface dataset:
Protein: Polyubiquitin 12 [Cleaved into: Ubiquitin-related 1; Ubiquitin-related 2; Ubiquitin-related 3] (Q3E7K8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase UPL4
- Protein NBR1 homolog
- E3 ubiquitin-protein ligase PRT1
- BRAP2 RING ZnF UBP domain-containing protein 1
- E3 ubiquitin-protein ligase UPL3
- Cytochrome P450 72A14
- Cytochrome P450, family 72, subfamily A, polypeptide 9
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL18y
Sequence:
MQIFLKTLTGKTKVLEVESSDTIDNVKAKIQDIEGIPPDQHRLIFAGKQLEDGRTLADYNVQEDSTLHLLLRFRGGMQIFVKTLTGKTITLEVESSDTIDNLKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGISPDQQRLIFAGKQHEDGRTLADYNIQKESTLHLVLRLRGGSF
Protein: Sororin (Cell division cycle-associated protein 5) (p35) (Q96FF9)
Organism: Homo sapiens (Human)
Function: Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin. May antagonize the action of WAPL which stimulates cohesin dissociation from chromatin. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for efficient DNA double-stranded break repair.
Subcellular location: Nucleus {ECO:0000269|PubMed:15837422}. Chromosome {ECO:0000269|PubMed:15837422}. Cytoplasm {ECO:0000269|PubMed:15837422}. Note=Associates with nuclear chromatin from S phase until metaphase and is released in the cytoplasm upon nuclear envelope breakdown.
Interaction partners:
- Sister chromatid cohesion protein PDS5 homolog A
- Wings apart-like protein homolog
- Structural maintenance of chromosomes protein 3
- Sister chromatid cohesion protein PDS5 homolog B
- Double-strand-break repair protein rad21 homolog
- Cyclin-dependent kinase 1
- Cohesin subunit SA-2
- Cohesin subunit SA-1
- Structural maintenance of chromosomes protein 1A
- Nipped-B-like protein
Sequence:
MSGRRTRSGGAAQRSGPRAPSPTKPLRRSQRKSGSELPSILPEIWPKTPSAAAVRKPIVLKRIVAHAVEVPAVQSPRRSPRISFFLEKENEPPGRELTKEDLFKTHSVPATPTSTPVPNPEAESSSKEGELDARDLEMSKKVRRSYSRLETLGSASTSTPGRRSCFGFEGLLGAEDLSGVSPVVCSKLTEVPRVCAKPWAPDMTLPGISPPPEKQKRKKKKMPEILKTELDEWAAAMNAEFEAAEQFDLLVE
Protein: Vacuolar-sorting protein SNF8 (ELL-associated protein of 30 kDa) (ESCRT-II complex subunit VPS22) (hVps22) (Q96H20)
Organism: Homo sapiens (Human)
Function: Component of the endosomal sorting complex required for transport II (ESCRT-II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation by participating in derepression of transcription by RNA polymerase II, possibly via its interaction with ELL. Required for degradation of both endocytosed EGF and EGFR, but not for the EGFR ligand-mediated internalization. It is also required for the degradation of CXCR4. Required for the exosomal release of SDCBP, CD63 and syndecan.
Subcellular location: Cytoplasm. Endosome membrane. Nucleus {ECO:0000305}. Late endosome membrane. Note=Recruited to the endosome membrane to participate in vesicle formation.
Interaction partners:
- Vacuolar protein-sorting-associated protein 25
- Vacuolar protein-sorting-associated protein 36
- Charged multivesicular body protein 6
- Vacuolar protein sorting-associated protein 28 homolog
- Tumor susceptibility gene 101 protein
- Charged multivesicular body protein 2a
- Charged multivesicular body protein 3
- RNA polymerase II elongation factor ELL
- Vacuolar protein sorting-associated protein 37C
- Charged multivesicular body protein 4b
Sequence:
MHRRGVGAGAIAKKKLAEAKYKERGTVLAEDQLAQMSKQLDMFKTNLEEFASKHKQEIRKNPEFRVQFQDMCATIGVDPLASGKGFWSEMLGVGDFYYELGVQIIEVCLALKHRNGGLITLEELHQQVLKGRGKFAQDVSQDDLIRAIKKLKALGTGFGIIPVGGTYLIQSVPAELNMDHTVVLQLAEKNGYVTVSEIKASLKWETERARQVLEHLLKEGLAWLDLQAPGEAHYWLPALFTDLYSQEITAEEAREALP
Protein: Transforming growth factor beta (Q7ZZU7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MRLVCLVLTALCLVTGTGSMSTCKTLDLEVVRKKRIEAIRGQILSKLRMAKEPESGADDDGQKIPDSLLSLYNSTVELSEEMKTKIVPVQDEDEDYFGKEVHKFVFQQAQNNTKHQMFFNVSEMKRSIPDYRLLSQAELRLRIKNPTMDQEQRLELYRGVGDQARYLGTRFVSKDLSNRWLSFDVKQTMIEWLQGSEDEETLELRLYCDCKANQQSTDKFLFTISGLDKQRGDTAGLADMMVKPYILALSLPSNGNSLASVRKRRAVGTDETCDEKTETCCMRKLYIDFRKDLGWKWIHKPKGYFANYCMGSCTYIWNAENKYSQILALYKHHNPGASAQPCCVPAILDPLPILYYVGRQHKVEQLSNMVVRNCKCS
Protein: Protein CLASP-3 (Q03609)
Organism: Caenorhabditis elegans
Function: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Putative extracellular sulfatase Sulf-1 homolog
- HoloCentric chromosome binding Protein
- Calponin homology domain-containing protein
- HoloCentric chromosome binding Protein
Sequence:
MTSRMQPKSGVYSVSKADFTKIFEDVPKVPITSAVDLRNKFDAVRIILSNSSEDWNKRQTQLKTVRSLVIHGEKVVDRPTMIAHLVQLLGCFELAVKDLRSQVLREAAITCSFIVSKYGIETHSIGEDILVPAMSQVAVSTKIMATSASTLTEFIVEYVQTRQVFTILSSFSTSKDKSQRRQLAALLEIVISKWSDRIKKQIMRQICELIKSAINDADSETRAAGRRAFAKLDEMHSEEADALYLELDHSKQKMLRGGDAASSWASVNSEKGSIPIRSKLSAGSKAHMNISAKFLAQRSASAIDPKATKFAGPSRLVRPTSTKTMARQDTSPAGCKYSNFISMFFKTLLLSAKIPYPNRPGSRTRTSSITSTDSRDTSPTRRNSPLPPETQKARVKYGNGSFFAKLGMPDTTDDDEFLLPIRIRSPLKTPTIEAHDKVSQVLKECCSSSVSEKKEGIKKLLPIVADTSLNPIEIKNIGNCLNRLLSDASNTMVLEIYSIFVRTHSSRLSEWLRLALAKLFARKAAETLPNTKKQIGHTLNVILECFNAHHQLVTVCELMCDPIHLMVPKARVVLLEYLTSLLDEYTEPGASINAKELKTAIRKMLTWASDPRLSILLTPHVEKAICSMFCVNVADFSALISDLDSEQKNWIHQTLQRNGLENGISSNNIATNSGATASRETSNTSFQKESTSFGLPEFGARKGGTGVNLGSLNISNNLALSRLEEQSTSRLMEKVNLNSTVTLPPDTLEKIQNVQDLLQKMRSSENADEQESAISSIYMMICDGGFGVWEQCYAKLLLNLFEILSKSRSENNKKMCLRILGKMCTAQAAKLFDSTEMAVCKVLDAAVNTNDATTALAVEDCLRTLATHLPLSNIINIAKVILNQEPIDDERASLVLKMVTRLFEELPAEELNNIVDDITPTIIKAYQSTSSTVRKTVVYCLVAMVNRVGEQRMTPHFTKLPKAMTNLIQVYVNRAISTSLPRL
Protein: Serine protease inhibitor Kazal-type 1 (P12) (Prostatic secretory glycoprotein) (Serine protease inhibitor Kazal-type 3) (P09036)
Organism: Mus musculus (Mouse)
Function: Serine protease inhibitor which exhibits anti-trypsin activity. In the pancreas, protects against trypsin-catalyzed premature activation of zymogens.
Subcellular location: Secreted {ECO:0000269|PubMed:1929395}.
Interaction partners:
- trypsin
- trypsin
- Anionic trypsin-2
- Trypsin-5
- trypsin
- Trypsin-4
- trypsin
- trypsin
- trypsin
- Chymotrypsin-C
Sequence:
MKVAVIFLLSALALLSLAGNTFSAKVTGKEASCHDAVAGCPRIYDPVCGTDGITYANECVLCFENRKRIEPVLIRKGGPC
Protein: Delta-1-pyrroline-5-carboxylate synthase B (P5CS B) [Includes: Glutamate 5-kinase (GK) (EC 2.7.2.11) (Gamma-glutamyl kinase); Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase)] (P54888)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: P5CS plays a key role in proline biosynthesis, leading to osmoregulation in plants.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate synthase A
- Ornithine aminotransferase, mitochondrial
- Delta-1-pyrroline-5-carboxylate dehydrogenase 12A1, mitochondrial
- Pyrroline-5-carboxylate reductase
- Glutamate synthase 1, chloroplastic
- Glutamate dehydrogenase 2
- glutamate dehydrogenase
- Glutamate dehydrogenase 1
- Probable glutamate dehydrogenase 3
- Proline dehydrogenase 1, mitochondrial
Sequence:
MTEIDRSRAFAKDVKRIVVKVGTAVVTGKGGRLALGRLGAICEQLAELNSDGFEVILVSSGAVGLGRQRLRYRQLVNSSFADLQKPQMELDGKACAGVGQSSLMAYYETMFDQLDVTVAQMLVTDSSFRDKDFRKQLSETVKAMLRMRVIPVFNENDAISTRRAPYKDSTGIFWDNDSLAALLSLELKADLLILLSDVEGLYTGPPSDSTSKLIHTFIKEKHQDEITFGEKSKLGRGGMTAKVKAAVNAAYGGVPVIITSGYAAENISKVLRGLRVGTLFHQDAHLWAPVVDTTSRDMAVAARESSRKLQALSSEDRKQILHDIANALEVNEKTIKAENDLDVAAAQEAGYEESLVARLVMKPGKISSLAASVRQLAEMEDPIGRVLKKTQVADDLILEKTSSPIGVLLIVFESRPDALVQIASLAIRSGNGLLLKGGKEARRSNAILHKVITDAIPETVGGKLIGLVTSREEIPDLLKLDDVIDLVIPRGSNKLVSQIKNSTKIPVLGHADGICHVYVDKSGKLDMAKRIVSDAKLDYPAACNAMETLLVHKDLEQNGFLDDLIYVLQTKGVTLYGGPRASAKLNIPETKSFHHEYSSKACTVEIVEDVYGAIDHIHQHGSAHTDCIVTEDSEVAEIFLRQVDSAAVFHNASTRFSDGFRFGLGAEVGISTSRIHARGPVGVEGLLTTRWIMRGKGQVVDGDNGIVYTHKDLPVLQRTEAVENGI
Protein: Large neutral amino acids transporter small subunit 1 (4F2 light chain) (4F2 LC) (4F2LC) (L-type amino acid transporter 1) (LAT1) (Solute carrier family 7 member 5) (Q7YQK4)
Organism: Oryctolagus cuniculus (Rabbit)
Function: The heterodimer with SLC3A2 functions as sodium-independent, high-affinity transporter that mediates uptake of large neutral amino acids such as tyrosine, L-DOPA, leucine, histidine, methionine, valine, isoleucine and alanine (By similarity). The heterodimer with SLC3A2 mediates the uptake of phenylalanine and tryptophan. Functions as an amino acid exchanger (By similarity). May play a role in the transport of L-DOPA across the blood-brain barrier (By similarity). May act as the major transporter of tyrosine in fibroblasts (By similarity). May mediate blood-to-retina L-leucine transport across the inner blood-retinal barrier (By similarity). Can mediate the transport of thyroid hormones diiodothyronine (T2), triiodothyronine (T3) and thyroxine (T4) across the cell membrane. When associated with LAPTM4B, the heterodimer formed by SLC3A2 and SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation. Involved in the uptake of toxic methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the membrane (By similarity).
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q01650}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q01650}. Cell membrane {ECO:0000269|PubMed:12614332, ECO:0000269|PubMed:16125134}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q01650}. Lysosome membrane {ECO:0000250|UniProtKB:Q01650}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q01650}. Note=Located to the plasma membrane by SLC3A2/4F2hc. Localized to the apical membrane of placental syncytiotrophoblastic cells. Recruited to lysosomes by LAPTM4B (By similarity). Expressed in both luminal and abluminal membranes of brain capillary endothelial cells (By similarity). {ECO:0000250|UniProtKB:Q01650, ECO:0000250|UniProtKB:Q63016}.
Interaction partners:
Sequence:
MAGAGPKRRAAAAAAPEEERQAREKMLAARREAEAEGEGVALQRNITLLNGVAIIVGTIIGSGIFVTPTGVLKEAGSPGLSLVVWAVCGVFSIVGALCYAELGTTITKSGGDYAYMLEVYGSLPAFLKLWIELLIIRPSSQYIVALVFATYLLKPVFPTCPVPEEAAKLVACLCVLLLTAVNCYSVKAATRVQDAFAAAKLLALALIILLGFVQIGKGGVSNLDPKFSFEGTNWDVGNIVLALYSGLFAYGGWNYLNFVTEEMINPYRNLPLAIIISLPICTLVYVLTNLAYFTTLSPEQMLASEAVAVDFGNHHLGVMSWVIPVFVGLSCFGSVNGSLFTSSRLFFVGSREGHLPSVLSMIHPQLLTPVPSLVFTCAMTLLYAFSRDIFSVINFFSFFNWLCVALAIIGMMWLRYKKPELERPIKVNLALPVFFILACLFLIAVSFWKTPVECGIGFTIILSGLPVYFFGVWWKNKPKWLLQGIFSATALCQKLMQVVPQET
Protein: Arginine/ornithine antiporter (Arginine-ornithine exchanger) (P18275)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes electroneutral exchange between arginine and ornithine to allow high-efficiency energy conversion in the arginine deiminase pathway. Also mediates the proton motive force-driven uptake of arginine and ornithine, but the exchange is several orders of magnitude faster than the proton motive force-driven transport.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:1311296, ECO:0000269|PubMed:8449902}; Multi-pass membrane protein {ECO:0000269|PubMed:8449902}.
Interaction partners:
- Arginine deiminase
- Carbamate kinase
- Ornithine carbamoyltransferase, catabolic
- 2-oxo-hept-3-ene-1,7-dioate hydratase
- Cytochrome c551 peroxidase
- Outer membrane protein OprG
- UspA domain-containing protein
- UspA domain-containing protein
- UspA domain-containing protein
- alcohol dehydrogenase
Sequence:
MSQESSQKLRLGALTALVVGSMIGGGIFSLPQNMAASADVGAVLIGWAITAVGMLTLAFVFQTLANRKPELDGGVYAYAKAGFGDYMGFSSAWGYWISAWLGNVGYFVLLFSTLGYFFPIFGKGDTVAAIVCASVLLWALHFLVLRGIKEAAFINTVTTVAKVVPLFLFILICLFAFKLDIFTADIWGKSNPDLGSVMNQVRNMMLVTVWVFIGIEGASIFSSRAEKRSDVGKATVIGFITVLLLLVLVNVLSMGVMTQPELAKLQNPSMALVLEHVVGHWGAVLISVGLLISLLGALLSWVLLCAEIMFAAAKDHTMPEFLRRENANQVPANALWLTNICVQVFLVVVFFTSGDPDGMDPYTKMLLLATSMILIPYFWSAAYGLLLTLKGETYENDARERSKDLVIAGIAVAYAVWLLYAGGLKYLLLSALLYAPGAILFAKAKHEVGQPIFTGIEKLIFAAVVIGALVAAYGLYDGFLTL
Protein: FpvI (Q9I193)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- FpvR
- Ferripyoverdine receptor
- Anti-sigma factor FoxR
- Sigma factor regulator, VreR
- Probable transmembrane sensor
- Probable transmembrane sensor
- L-ornithine N
- Probable transmembrane sensor
- Probable transmembrane sensor
- Sigma factor regulator, FemR
Sequence:
MENHYRELLRFLSARLGDRHAAADVAHDAYLRVLERSSQAQIEHPKAFLYRTALNLAVDEHRRSRVRRAEPLEVLDDEEGLASPSPQTVVDQGQRLDNLQRALAELPAICRSSFLLRKLDGLSHSQIAEHLNISRSLVEKHIVNAMKHCRVRMREWEAD
Protein: FI23202p1 (Pebble) (Q9U7D8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEMETIEEQSKCEMSITTLPTRICLVGGVGQDADTLQAAESFGLPIVTSDTGLDILGESSDWRTFYVLDDFEGASFEAIHKQKECILGPPALKYAAEMKQTLGQNSRPIYNYAMRGVVTCFTGIRKKDELTKLVNLIHSMGGCIKKDLNTKTTHLICNHSGGEKYQYAKTFRLTVVRPAWVFAAWADRNSLEFDATQENFTKTHRLKAFEGQKICFFGFPVEEHQHMVDVLLENGGVCAELDDPECSHVVVDEHTTLTKPEPKNNHTHILKSDWFWYTIQNGYANEMDYLFGDYLDSITNTPNTDRRDSLPISFNKRKRKRFSQRIQLEGTPLGSGKRRSSVSDAGLLSVSNSLFDCTTSPDKLESDKLLHAEPEASDATPAKKSMRFNHFMDFYTTESNYVGILDTILNLFKNKLEELAETNDPLLNKSEIKTIFGNFLPIHEVHQSMLEHLRKLHANWREDCLIGDIIIQHRDELIKAYPPYVNFFEQMKEQLQYCDREYPRFHAFLKINQTKPECGRQGLQDLMIRPVQRLPSISLLLNDILKHTTSGNADHGRLEEALKAIKQVTLHINEDKRRTESRMAIFDIFNDIEGCPAHLVSSNRSFILKCEVNELSDSLSGRGDSLVLYLFSDSIELCKRRSKGFNTAKSPSTAKTHKHLKLISLNTIRLVIDISDSPRAFGLLLRGDKEKLYTFTISDEETDKSVYVKKLCNQIAAHTCRTDADKLLICRTSQELEVDISDVNVSTLSKAFKLAAKTRLKVGRAFSFNKTPNKLKRAVSTMMTSPFGSTNSLTPASQLAQMRLASCTNINEVDDEDCASMRSSSPSTQSEMLVVPPLSVQPTRKNKAVVGRI
Protein: UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase (EC 2.3.2.10) (Q9EY50)
Organism: Weissella viridescens (Lactobacillus viridescens)
Function: Involved in the synthesis of the bacterial cell wall. Catalyzes the addition of alanine into the interchain peptide bridge of peptidoglycan precursor using aminoacyl-tRNA(Ala) as amino acid donor. This alanine is added to the epsilon-amino group of the L-lysine of the peptidoglycan UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-L-lysyl-D-alanyl-D-alanine, in a ribosome-independent mechanism. Specific for UDP-N-acetyl-muramoyl-pentapeptide. Has no activity toward UDP-N-acetyl-muramoyl-tetrapeptide or UDP-N-acetyl-muramoyl-tripeptide. Also acts on L-seryl-tRNA(Ser).
Interaction partners:
- Aminoacyltransferase FemA
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Lipid II isoglutaminyl synthase subunit MurT
- Aminoacyltransferase FemA
Sequence:
MPVLNLNDPQAVERYEEFMRQSPYGQVTQDLGWAKVKNNWEPVDVYLEDDQGAIIAAMSMLLGDTPTDKKFAYASKGPVMDVTDVDLLDRLVDEAVKALDGRAYVLRFDPEVAYSDEFNTTLQDHGYVTRNRNVADAGMHATIQPRLNMVLDLTKFPDAKTTLDLYPSKTKSKIKRPFRDGVEVHSGNSATELDEFFKTYTTMAERHGITHRPIEYFQRMQAAFDADTMRIFVAEREGKLLSTGIALKYGRKIWYMYAGSMDGNTYYAPYAVQSEMIQWALDTNTDLYDLGGIESESTDDSLYVFKHVFVKDAPREYIGEIDKVLDPEVYAELVKD
Protein: Citrate synthase (Q2U9X4)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Aconitate hydratase, mitochondrial
- Aconitate hydratase, mitochondrial
- ATP citrate synthase
- Aconitate hydratase, mitochondrial
- ATP citrate synthase
- Malate dehydrogenase
- malate dehydrogenase
- Pyruvate carboxylase
- Acetyltransferase component of pyruvate dehydrogenase complex
- Malate synthase
Sequence:
MASSLRIGTSVLRSTSLAGKPVVQSVAFNGLRCYSTGKAKSLKETFADNLPGEIEKVKKLRKDYGNKVIGEVTLDQAYGGARGVKCLVWEGSVLDSEEGIRFRGYTIPECQKLLPKAPGGEEPLPEGLFWLLLTGEIPSEQQVRDLSAEWAARSDLPKFIEELIDRCPSTLHPMAQFSLAVTALEHESAFAKAYAKGINKKDYWNYTFEDSMDLIAKLPTIAAKIYRNVFKDGKVAPIQKDKDYSYNLANQLGFGNNNDFVELMRLYLTIHSDHEGGNVSAHTTHLVGSALSSPMLSLSAGLNGLAGPLHGLANQEVLNWLTKMKAAIGNDLSDQAIKDYLWSTLNAGQVVPGYGHAVLRKTDPRYVSQREFALRKLPDDQMFNLVSQVYKIAPGVLTEHGKTKNPFPNVDAHSGVLLQYYGLTEANYYTVLFGVSRALGVLPQLIIDRALGAPIERPKSFSTEAYAKLVGAKL
Protein: Endonuclease III (EC 4.2.99.18) (DNA-(apurinic or apyrimidinic site) lyase) (A0A0H2UQJ4)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Interaction partners:
Sequence:
MVLSKKRARKVLEEIIALFPDAKPSLDFTNHFELLVAVMLSAQTTDAAVNKATPGLFVAFPTPQAMSVATESEIASHISRLGLYRNKAKFLKKCAQQLLDDFDGQVPQTREELESLAGVGRKTANVVMSVGFGIPAFAVDTHVERICKHHDIVKKSATPLEVEKRVMDILPPEQWLAAHQAMIYFGRAICHPKNPECDQYPQLYDFSNL
Protein: Translation initiation factor IF-1 (P69222)
Organism: Escherichia coli (strain K12)
Function: One of the essential components for the initiation of protein synthesis. Binds in the vicinity of the A-site. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit, IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00075, ECO:0000269|PubMed:376343}.
Interaction partners:
- Small ribosomal subunit protein uS8
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS10
Sequence:
MAKEDNIEMQGTVLETLPNTMFRVELENGHVVTAHISGKMRKNYIRILTGDKVTVELTPYDLSKGRIVFRSR
Protein: Segment polarity protein dishevelled homolog DVL-2 (Dishevelled-2) (DSH homolog 2) (O14641)
Organism: Homo sapiens (Human)
Function: Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Participates both in canonical and non-canonical Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Promotes internalization and degradation of frizzled proteins upon Wnt signaling.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q60838}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q60838}; Cytoplasmic side {ECO:0000250|UniProtKB:Q60838}. Cytoplasm, cytosol {ECO:0000269|PubMed:24616100}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q60838}. Nucleus {ECO:0000269|PubMed:25805136}. Note=Localizes at the cell membrane upon interaction with frizzled family members and promotes their internalization. Localizes to cytoplasmic puncta (By similarity). Interaction with FOXK1 and FOXK2 induces nuclear translocation (PubMed:25805136). {ECO:0000250|UniProtKB:Q60838, ECO:0000269|PubMed:24616100, ECO:0000269|PubMed:25805136}.
Interaction partners:
- Axin-1
- Vang-like protein 1
- Vang-like protein 2
- Low-density lipoprotein receptor-related protein 6
- Dapper homolog 1
- Segment polarity protein dishevelled homolog DVL-1
- Segment polarity protein dishevelled homolog DVL-3
- Frizzled-4
- Beta-arrestin-2
- Prickle-like protein 1
Sequence:
MAGSSTGGGGVGETKVIYHLDEEETPYLVKIPVPAERITLGDFKSVLQRPAGAKYFFKSMDQDFGVVKEEISDDNARLPCFNGRVVSWLVSSDNPQPEMAPPVHEPRAELAPPAPPLPPLPPERTSGIGDSRPPSFHPNVSSSHENLEPETETESVVSLRRERPRRRDSSEHGAGGHRTGGPSRLERHLAGYESSSTLMTSELESTSLGDSDEEDTMSRFSSSTEQSSASRLLKRHRRRRKQRPPRLERTSSFSSVTDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDMNFENMSNDDAVRVLRDIVHKPGPIVLTVAKCWDPSPQAYFTLPRNEPIQPIDPAAWVSHSAALTGTFPAYPGSSSMSTITSGSSLPDGCEGRGLSVHTDMASVTKAMAAPESGLEVRDRMWLKITIPNAFLGSDVVDWLYHHVEGFPERREARKYASGLLKAGLIRHTVNKITFSEQCYYVFGDLSGGCESYLVNLSLNDNDGSSGASDQDTLAPLPGATPWPLLPTFSYQYPAPHPYSPQPPPYHELSSYTYGGGSASSQHSEGSRSSGSTRSDGGAGRTGRPEERAPESKSGSGSESEPSSRGGSLRRGGEASGTSDGGPPPSRGSTGGAPNLRAHPGLHPYGPPPGMALPYNPMMVVMMPPPPPPVPPAVQPPGAPPVRDLGSVPPELTASRQSFHMAMGNPSEFFVDVM
Protein: Leucokinin (DLK) (P81829)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts through intracellular calcium in Malpighian tubule stellate cells to raise chloride conductance.
Subcellular location: Secreted.
Interaction partners:
- Diuretic hormone 44, isoform A
- Cardioactive peptide
- Allatostatin-A
- Short neuropeptide F
- Neuropeptide F
- Protein hugin
- Leucokinin receptor
- Diuretic hormone class 2
- Adipokinetic hormone
- Cardio acceleratory peptide 2b
Sequence:
MAKIVLCMVLLAFGRQVYGASLVPAPISEQDPELATCELQLSKYRRFILQAILSFEDVCDAYSSRPGGQDSDSEGWPFRHYAPPPTSQRGEIWAFFRLLMAQFGDKEFSPIIRDAVIERCRIKSQLQRDEKRNSVVLGKKQRFHSWGGKRSPEPPILPDY
Protein: Epithelial membrane protein 1 (EMP-1) (CL-20) (Protein B4B) (Tumor-associated membrane protein) (P54849)
Organism: Homo sapiens (Human)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Parathyroid hormone
- Fibroblast growth factor 23
Sequence:
MLVLLAGIFVVHIATVIMLFVSTIANVWLVSNTVDASVGLWKNCTNISCSDSLSYASEDALKTVQAFMILSIIFCVIALLVFVFQLFTMEKGNRFFLSGATTLVCWLCILVGVSIYTSHYANRDGTQYHHGYSYILGWICFCFSFIIGVLYLVLRKK
Protein: Deoxynucleoside kinase (EC 2.7.1.145) (Deoxyribonucleoside kinase) (Dm-dNK) (Multispecific deoxynucleoside kinase) (Q9XZT6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Deoxyribonucleoside kinase that has a broad specificity phosphorylating thymidine, 2'-deoxyriboadenosine, 2'-deoxyribocytidine and 2'-deoxyriboguanosine. Specificity is higher for pyrimidine nucleosides. Several anti-viral and anti-cancer nucleoside analogs are also efficiently phosphorylated.
Interaction partners:
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 13 kDa B subunit
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 subunit C2
- NADH-ubiquinone oxidoreductase chain 4L
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase iron-sulfur protein 4
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Ribonucleoside-diphosphate reductase subunit M2
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
Sequence:
MAEAASCARKGTKYAEGTQPFTVLIEGNIGSGKTTYLNHFEKYKNDICLLTEPVEKWRNVNGVNLLELMYKDPKKWAMPFQSYVTLTMLQSHTAPTNKKLKIMERSIFSARYCFVENMRRNGSLEQGMYNTLEEWYKFIEESIHVQADLIIYLRTSPEVAYERIRQRARSEESCVPLKYLQELHELHEDWLIHQRRPQSCKVLVLDADLNLENIGTEYQRSESSIFDAISSNQQPSPVLVSPSKRQRVAR