wanglab/gogpt-training-data huggingface dataset:
Protein: C-X-C motif chemokine 14 (B-cell and monocyte-activating chemokine) (Chemokine BRAK) (Kidney-expressed chemokine CXC) (MIP-2G) (Small-inducible cytokine B14) (Q9WUQ5)
Organism: Mus musculus (Mouse)
Function: Chemotactic for CESS B-cells and THP-1 monocytes, but not T-cells.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Stromal cell-derived factor 1
- C-X-C motif chemokine 17
- C-X-C motif chemokine 5
- C-X-C chemokine receptor type 4
- C-X-C motif chemokine 9
- C-X-C motif chemokine 10
- C-C motif chemokine 5
- C-C motif chemokine
- Chemokine subfamily B Cys-X-Cys
- C-C motif chemokine ligand 26
Sequence:
MRLLAAALLLLLLALCASRVDGSKCKCSRKGPKIRYSDVKKLEMKPKYPHCEEKMVIVTTKSMSRYRGQEHCLHPKLQSTKRFIKWYNAWNEKRRVYEE
Protein: Nuclear pore complex protein Nup205 (205 kDa nucleoporin) (Nucleoporin Nup205) (Q8IQV9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in the nuclear pore complex (NPC) assembly and maintenance, but with limited role in NPC permeability. Required for specific nuclear import pathways such as Mad import.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:Q92621}.
Interaction partners:
- Nuclear pore complex protein Nup154
- Nuclear pore complex protein Nup160 homolog
- Nuclear pore glycoprotein p62
- Nuclear pore complex protein Nup107
- Nucleoporin Nup188
- Nucleoporin Nup35
- Nuclear pore protein
- Nuclear pore complex protein Nup98-Nup96
- Probable nucleoporin Nup54
- Nuclear pore complex protein Nup153
Sequence:
MDGECLANEQMCVGRQITNATHASTAVIEDMWTPYKHLYNTFQTAVSNRSGFTSDLEQCLKKYKHNFSNLLRNPPRSEKSRNLLRNALNEGVPMQGHSRKTKMSQDLADEAVILSDMFDLDEGFAVELLCTAQRQQKHHPGLSRGLVAVLLYYDGRKAISCTLRDMFQVVSGVSWNTELPKEITGLVTNYAESLVDGSGILGRLLQLLEEMDVDKECAMLTTNRAFGSKKHQNQVLGLYEDIQQALAMALFNWSAQRGLPRHIAIRLMHQLANRKNHDAGGNMDDVTLIMLMALLYAYDTSMLLVTEEPNEHTTRLPIFSDREFAECFLEELYAQSSWQAPRLNAIIAYSFGLTLASLRHAPLQLQATAISIINRDEMLIDEALGAQVFVFFHSLLLEKDLVYSTQFFYRRVHLLITDFIDFMNSKVSELRGRADESSHTIISFLNEGLEPPPNLDSNFELLMLCVAKMHGDPRVTIRLCNEYWGPGDPNGSTAFKNTSRSVSLFKFISLASDLLPQTLFKAYLKMISGLTRTDFSARCAFNMLRVPQMATGGKYAVSWDHFFTTLGNYYTSMRNDFNTNIGMSGETIYRTRSTPKAITQREAEHLVAVMGIIQAVAEHDEVSRIMICDHPNWQTPQVLLGLVACATPLFLKAEILHTLAALAKSKETARVIWFHLEASQIIPTVPVSRSYAQCSLLEEMEQIESRSEQYNLTRGILQLLYTLMTTNLPKSLGAGQRTPAYEGYLKSMINSVLLKFYNRAYKVPSEKWQVGAQCLKLLYYLLATYRPSAMDFLETVDEPPYPGFHVMMQLQLKSEMLQLLLCIVEEVRERLDNYNRFQGKKLLEECSLYALLILEAALAKQNAFFEAHSAANCPILLSGLNRMLLDLNPRSRKPDHVLNIIKYVTYNSWLPRHALAAIKILASVTQLPNVSTQILSMYGQGSNEKLEIRQGFVECLEMEVCVGKHDDDLLDQLALNNHVPYLGFGDDLDNEREMSGEREYSTIESQLELQAGDGALESKPASIELQLKEAIIKLFEMNLSQQLPNFVYFLLGVDVLREFMANGRQHLAIEMQSSCVNSVVLLLEKYMDKQRHSDKYCEHTARIVERIYHLFHGLCANRRTAETILRYFRLTCSDFLLRHLRSLPFRQHREDHVLHAMGHLLNCVSIDVKLAAKHGQMTRFNQMCDILLIGNGMERSSHGLSMELGHSLISQPSSSFLAMDVLPAGGSISAVAHGAGSASLGAPNTGVKSLKPSLLQETSQGLHVTRLLDILVLEAGTLSQPQLEFFDGHLITQLLRDCEASAEAGANSRANLINVRKLYYILTDELYMVQSIIASGQRKAISTEIMLLLNHAVNINRVRTQRCATLAFMAAWGQLVQVLFSNMPDAVLPATQRRQHIIDIVEKVLIKVQPIQPIIEISVQVSETVLLLLANLRYCCYQAEDQSPEDLAAEDSLSNGNGNAIGNDSQVNALCLGQRAIGTGSDGGSGGGRDIGSGGNSSNLRFILKNLVQWIMISEVKSQKLRINLYSSLLNCLRIAKRLRTDEHLEYQETLISRQESARTYNKEQRRDDRLRLKAMAAEVIGTFGEKLIDTICHDAVTGHDVCRMLALACLDMISELQAVSTLCDFVASRGYLKHILESLDQSSTALCGILQPVPDHLRPLYVYESRMAFLTRMANSNVGARLLLTEQALGVLSNMKVYDQQPDLKSSELNRNEPQTFLPSIDDRFRSILLPALSLCDAIVNSLGPRNNSAAVQVLNFLFAHIDMVEAMLRSATPYMDLGHLQQVAVISNLFARASTHELTALEDSVQLDLRNRLGRVQQLMIVVFGRFCVSEPTIRRMLQQDEEQQTNPTDDSKRLRVKYFLDIAANVSLYCRNVVTSHSKDSMTSKYLLTTVINDVTLLTGKMSSKKLTTIMHTILNQLKGSIGYYLSQKSIADNLLQQRASLPNISFGPNGKQSYIELSQRYNEKRSELRQAVFIAEQNLYLLWIHLDFYLRNTIDYANENRNAINESNMDDDNDMSVLNASQEEIVQLKQLLISTFNETFCTQLINASEDYSIKCKGFNGSLLRRIKALVQFAPITANDVNSSFDS
Protein: RNA helicase (EC 3.6.4.13) (A0A0A0MT12)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEI
Protein: Dual specificity protein phosphatase 1 (EC 3.1.3.16) (EC 3.1.3.48) (Mitogen-activated protein kinase phosphatase 1) (MAP kinase phosphatase 1) (MKP-1) (Protein-tyrosine phosphatase CL100) (Protein-tyrosine phosphatase non-receptor type 16) (Q64623)
Organism: Rattus norvegicus (Rat)
Function: Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q91790}.
Interaction partners:
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 3
- mitogen-activated protein kinase
- Mitogen-activated protein kinase 8
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 9
- Mitogen-activated protein kinase 10
- Mitogen-activated protein kinase 12
- Mitogen-activated protein kinase 13
- Protein c-Fos
Sequence:
MVMEVGILDAGGLRALLRERAAQCLLLDCRSFFAFNAGHIVGSVNVRFSTIVRRRAKGAMGLEHIVPNTELRGRLLAGAYHAVVLLDERSAALDGAKRDGTLALAAGALCREARSTQVFFLQGGYEAFSASCPELCSKQSTPMGLSLPLSTSVPDSAESGCSSCSTPLYDQGGPVEILSFLYLGSAYHASRKDMLDALGITALINVSANCPNHFEGHYQYKSIPVEDNHKADISSWFNEAIDFIDSIKDAGGRVFVHCQAGISRSATICLAYLMRTNRVKLDEAFEFVKQRRSIISPNFSFMGQLLQFESQVLAPHCSAEAGSPAMAVLDRGTSTTTVFNFPVSIPVHPTNSALNYLQSPITTSPSC
Protein: Transcription factor 23 (TCF-23) (Basic helix-loop-helix transcription factor OUT) (Ovary, uterus and testis protein) (Q9JLR5)
Organism: Mus musculus (Mouse)
Function: Inhibits E-box-mediated binding and transactivation of bHLH factors. Inhibitory effect is similar to that of ID proteins. Inhibits the formation of TCF3 and MYOD1 homodimers and heterodimers. Lacks DNA binding activity. May be involved in the regulation or modulation of smooth muscle contraction of the uterus during pregnancy and particularly around the time of delivery. Seems to play a role in the inhibition of myogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:10652346}.
Interaction partners:
Sequence:
MSQEATEAPAMPGEGHGHNKAKARWLLGTDRKRSRINRTRQDLWEDTSWSNHRLSRATSAPRGTRARGTAHGRSEASPENAARERTRVKTLRQAFLALQAALPAVPPDTKLSKLDVLVLATSYIAHLTRTLGHELPGPAWPPFVRGLRYLHPLKKWPMRSRLYAGGLGCSDLDSTTAITTGQRCKDAELGSQDSVAAESLLTSPAFGNK
Protein: Sorting nexin 25 (A0A494C0S0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MHPDATDSGGAGPSPARAAGAGGRPVSGFRGERRPESPGDAEAAAAAAPGAPGGRSWWKPVAVAALAAVALSFLGPGSGEAAGAAGLSSVLFRLSLYLSCAAAAFLLGILFALVCRSPRAQPPDFAAAWSRLAATSAARRPPGSPVYGNSHESAQSRRVVISHNMDKALKEVFDYSYRDYILSWYGNLSRDEGQLYHLLLEDFWEIARQLHHRLSHVDVVKVVCNDVVRTLLTHFCDLKAANARHEEQPRPFVLHACLRNSDDEVRFLQTCSRVLVFCLLPSKDVQSLSLRIMLAEILTTKVLKPVVELLSNPDYINQMLLAQLAYREQMNEHHKRAYTYAPSYEDFIKLINSNSDVEFLKQLRYQIVVEIIQATTISSFPQLKRHKGKETAAMKADLLRARNMKRYINQLTVAKKQCEKRIRILGGPAYDQQEDGALDEGEGPQSQKILQFEDILANTFYREHFGMYMERMDKRALISFWESVEHLKNANKNEIPQLVGEIYQNFFVESKEISVEKSLYKEIQQCLVGNKGIEVFYKIQEDVYETLKDRYYPSFIVSDLYEKLLIKEEEKHASQMISNKDEMGPRDEAGEEAVDDGTNQINEQASFAVNKLRELNEKLEYKRQALNSIQNAPKPDKKIVSKLKDEIILIEKERTDLQLHMARTDWWCENLGMWKASITSGEVTEENGEQLPCYFVMVSLQEVGGVETKNWTVPRRLSEFQNLHRKLSECVPSLKKVQLPSLSKLPFKSIDQKFMEKSKNQLNKFLQNLLSDERLCQSEALYAFLSPSPDYLKVIDVQGKKNSFSLSSFLERLPRDFFSHQEEETEEDSDLSDYGDDVDGRKDALAEPCFMLIGEIFELRGMFKWVRRTLIALVQVTFGRTINKQIRDTVSWIFSEQMLVYYINIFRDAFWPNGKLAPPTTIRSKEQSQETKQRAQQKLLENIPDMLQSLVGQQNARHGIIKIFNALQETRANKHLLYALMELLLIELCPELRVHLDQLKAGQV
Protein: WD repeat domain 62 (F1M5K2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton, spindle pole {ECO:0000256|ARBA:ARBA00004647}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Assembly factor for spindle microtubules
- Centrosomal protein of 63 kDa
- Centrosomal P4.1-associated protein
- STIL, centriolar assembly protein
- Microcephalin
- Dual specificity mitogen-activated protein kinase kinase 7
- Centrosomal protein 135
Sequence:
MMAALAAGGYARSDTIEKLSSVMAGVPARRNQSSPPPAPPLCLRRRTRLAAAPEDTVQNRVTLEKVLGITAQNSSGLTCDPGTGHVAYLAGCVVVVLNPKENKQQHIFNTTRKSLSALAFSPDGKYIVTGENGHRPAVRIWDVEEKTQVAEMLGHKYGVACVAFSPNMKHIVSMGYQHDMVLNVWDWKKDIVVASNKVSCRVIALSFSEDSSYFVTVGNRHVRFWFLEASTEAKVTSTMPLVGRSGILGELHNNIFCGVACGRGRMAGNTFCVSYSGLLCQFNEKRVLDKWINLKVSLSSCLCVSDELIFCGCTDGIVRIFQAHSLLYLTNLPKPHYLGIDVAQGLDSSFLFHRKAEAVYPDTVALTFDPIHQWLSCVYKDHSVYIWDVKDINEVSKIWSELFHSSFVWNVEVYPEFEDQRACLPSGTFLTCSSDNTIRFWNMDSGSDTQWRKNIFSDSLLKVVYVENDIQHLQDMSHFPDRGSENGTPMDMKAGVRVMQVSPDGQHLASGDRSGNLRIHELHFMDELIKVEAHDAEVLCLEYSKPETGVTLLASASRDRLIHVLNVEKNYNLEQTLDDHSSSITAIKFAGTRDVQMISCGADKSIYFRSAQQTSDGLHFVRTHHVAEKTTLYDMDIDITQKYVAVACQDRNVRVYNTVSGKQKKCYKGSQGDEGSLLKVHVDPSGTFLATSCSDKSISVIDFYSGECVAKMFGHSEIVTGMKFTYDCRHLITVSGDSCVFIWHLGPEITTCMKQHLMEINHQEQQHLPKDQKWSGPPSQETSASTPSEIRSLSPGEQTEDEMEEECEPEETLKTPSKESLDPDPRCLLTNGKLPLWAKRLLGDDDVTDSSAFHAKRSYQPHGRWAERAEQEPLKTILDAWALDSYFTPMKPGNLEDSVLDSVEPQNLAGLLSECSPENGHTAPGEGLVSYLCHSESGSPKEDSRGHPSYLPLQREGTETRELILCSPEVEVTVTGMHREYYEEAEAGPEDQQGDSYLRVSSVSSKDQSPPEDSGESEAELECSFAAAHVSAPRTDPGPHLTMTGKPEHSSTDELAQPGVPGLGNGSLPQTPEQEKFLRHHFETLTDAPAEELFPGSLGDIKISETDDYFFNPRLSISTQFLSRLQKTSRFPPRLPLHLMKSPEVQPVGQGGNQPKAGPLRAGTGYMSSDGTNVLSGQMAEETPEASCLPTPPITGLASCVPPSSVIPTDRKPPTPTSGLTTGREQSIPAPSPCSYLESTTSSHAKMTRSTSLGDSEGPVTGELPRPLHKPVSPGQEPQAVPTTVALTSSVKGHEPALPAWGNHEARASLRLTLSSVCEQLLSPPQLEPPTTPVWSQEAVDVPPSMAVTVASFSAPSPEDMSTLGLHSSVFLPKTSASGPLTPPAHPNSLQLLETRSRMPGSTPALLEPTPDASSGSPDSPGHCGEPGRRAEVPPPGPLELDSVESVLYRLQTAFQEALDLYRMLASSNQLGAEQQQAQTELASAFHWIHHQLEASNCVGAASVAPPLTLPSPGPPSPPTLCPLASPNLQALLEHYSELLVQAVRRKVRGD
Protein: Uncharacterized protein YrdD (P45771)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Threonylcarbamoyl-AMP synthase
- Uncharacterized protein YrdB
- DNA topoisomerase 3
- Shikimate dehydrogenase
- Protein Smg
- Protein Smf
Sequence:
MAKSALFTVRNNESCPKCGAELVIRSGKHGPFLGCSQYPACDYVRPLKSSADGHIVKVLEGQVCPACGANLVLRQGRFGMFIGCINYPECEHTELIDKPDETAITCPQCRTGHLVQRRSRYGKTFHSCDRYPECQFAINFKPIAGECPECHYPLLIEKKTAQGVKHFCASKQCGKPVSAE
Protein: Aklavinone 12-hydroxylase RdmE (EC 1.14.13.180) (Aklavinone 11-hydroxylase) (Q54530)
Organism: Streptomyces purpurascens
Function: Involved in the biosynthesis of the anthracyclines carminomycin, rhodomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the incorporation of a hydroxyl group at position C-11 of aklavinone, resulting in epsilon-rhodomycinone. It cannot accept substrates glycosylated at position C-7 and is specific for the C-9R configuration of anthracyclines. It can use both NAD or NADP but it is slowly inactivated in the presence of NADH.
Interaction partners:
Sequence:
MNDHEVDVLVVGAGLGGLSTAMFLARQGVRVLVVERRPGLSPYPRAAGQNPRTMELLRIGGVADEVVRADDIRGTQGDFVIRLAESVRGEILRTVSESFDDMVAATEPCTPAGWAMLSQDKLEPILLAQARKHGGAIRFGTRLLSFRQHDDDAGAGVTARLAGPDGEYDLRAGYLVGADGNRSLVRESLGIGRYGHGTLTHMVGVIFDADLSGIMEPGTTGWYYLHHPEFKGTFGPTDRPDRHTLFVEYDPDEGERPEDFTPQRCVELIGLALDAPEVKPELVDIQGWEMAARIAERWREGRVFLAGDAAKVTPPTGGMSGNAAVADGFDLAWKLAAVLQGQAGAGLLDTYEDERKVAAELVVAEALAIYAQRMAPHMAEVWDKSVGYPETLLGFRYRSSAVLATDDDPARVENPLTPSGRPGFRGPHVLVSRHGERLSTVDLFGDGWTLLAGELGADWVAAAEAVSAELGVPVRAYRVGAGLTDPESAVSERYGIGKAGASLVRPDGIVAWRTDEAAADAAQTLEGVLRRVLDR
Protein: Ubiquitin-conjugating enzyme E2 30 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 30) (Ubiquitin carrier protein 30) (Q9FKT3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Interaction partners:
- E3 ubiquitin-protein ligase UPL4
- E3 ubiquitin-protein ligase UPL3
- Adenylyltransferase and sulfurtransferase MOCS3
- E3 ubiquitin-protein ligase RGLG3
- Proline-rich cell wall protein-like
- Putative RING zinc finger protein
- Ubiquitin-activating enzyme E1 2
- Ubiquitin-activating enzyme E1 1
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 1
- Anaphase-promoting complex subunit 10
Sequence:
MASKRINKELRDLQRDPPVSCSAGPTGDDMFQWQATIMGPADSPFAGGVFLVTIHFPPDYPFKPPKVAFRTKVYHPNINSNGSICLDILKEQWSPALTVSKVLLSICSLLTDPNPDDPLVPEIAHIYKTDRVKYESTAQSWTQKYAMG
Protein: Sphingosine-1-phosphate lyase (S1PL) (SP-lyase) (SPL) (EC 4.1.2.27) (Sphingosine-1-phosphate aldolase) (Q9V7Y2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Sphingolipid catabolism is required for normal development including viability, reproduction and muscle development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O95470}; Single-pass type III membrane protein {ECO:0000255}.
Interaction partners:
- sphingosine kinase
- sphingosine kinase
- serine C-palmitoyltransferase
- GH04282p
- FI04477p
- RE35159p
- FI20175p1
- RH32172p
- HL01743p
- Putative phosphatidate phosphatase
Sequence:
MRPFSGSDCLKPVTEGINRAFGAKEPWQVATITATTVLGGVWLWTVICQDENLYIRGKRQFFKFAKKIPAVRRQVETELAKAKNDFETEIKKSNAHLTYSETLPEKGLSKEEILRLVDEHLKTGHYNWRDGRVSGAVYGYKPDLVELVTEVYGKASYTNPLHADLFPGVCKMEAEVVRMACNLFHGNSASCGTMTTGGTESIVMAMKAYRDFAREYKGITRPNIVVPKTVHAAFDKGGQYFNIHVRSVDVDPETYEVDIKKFKRAINRNTILLVGSAPNFPYGTIDDIEAIAALGVKYDIPVHVDACLGSFVVALVRNAGYKLRPFDFEVKGVTSISADTHKYGFAPKGSSVILYSDKKYKDHQFTVTTDWPGGVYGSPTVNGSRAGGIIAACWATMMSFGYDGYLEATKRIVDTARYIERGVRDIDGIFIFGKPATSVIALGSNVFDIFRLSDSLCKLGWNLNALQFPSGIHLCVTDMHTQPGVADKFIADVRSCTAEIMKDPGQPVVGKMALYGMAQSIPDRSVIGEVTRLFLHSMYYTPSQK
Protein: Large ribosomal subunit protein eL8 (50S ribosomal protein L7Ae) (Ribonuclease P protein component Rpp38) (RNase P component Rpp38) (Ribosomal protein L8e) (P62009)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Multifunctional RNA-binding protein that recognizes the K-turn motif in ribosomal RNA, box H/ACA, box C/D and box C'/D' sRNAs (By similarity). When added to reconstituted ribonuclease P (RNase P) it increases the optimum temperature to that of the partially purified enzyme and causes a 5-fold increase in apparent Vmax. Binds the RNase P catalytic RNA.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00326}.
Interaction partners:
- Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL2
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein eL30
Sequence:
MAKPSYVKFEVPKELAEKALQAVEIARDTGKIRKGTNETTKAVERGQAKLVIIAEDVDPEEIVAHLPPLCEEKEIPYIYVPSKKELGAAAGIEVAAASVAIIEPGKARDLVEEIAMKVRELMK
Protein: [Val1,Thr6]-bradykinyl-Val,Asp (A0A088MI62)
Organism: Physalaemus nattereri (Cuyaba dwarf frog) (Eupemphix nattereri)
Function: Induces contraction of rat ileum smooth muscle (EC(50)=2.73 uM) but has no activity towards rat smooth muscle from tail artery, urinary bladder or uterus. Binds to both bradykinin receptor B1 (BDKRB1) and B2 (BDKRB2); the effect via BDKRB1 is stronger.
Subcellular location: Secreted {ECO:0000269|PubMed:26443407}.
Interaction partners:
Sequence:
MAFLKKSLFLVLFLGVVSLSFCEEEEREEHEEEKREAEAAESAENLISKRVPPGFTPFRVD
Protein: Phospholipase A1 PLIP3, chloroplastic (EC 3.1.1.32) (Galactolipase PLIP3) (EC 3.1.1.26) (Protein PLASTID LIPASE 3) (Q940L4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sn-1-specific phospholipase A1 that catalyzes the initial step of oxylipins and jasmonate (JA) biosynthesis. Hydrolyzes polyunsaturated acyl groups preferentially from chloroplastic phosphatidylglycerol (PG). May function downstream of abscisic acid (ABA), and provide a link between ABA-mediated abiotic stress responses and oxylipin and JA signalings. In vitro, possesses broad substrate specificity. Can hydrolyze the galactolipids monogalactosyldiacylglycerol (MGDG) and digalactosyldiacylglycerol (DGDG), the sulfolipid sulfoquinovosyldiacylglycerol (SQDG), and the phoshpolipids phosphatidylcholine (PC), and phosphatidylglycerol (PG).
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:29666162}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Protein CHLOROPLAST VESICULATION
- GDSL esterase/lipase At1g28590
- Uncharacterized protein At5g39520
- Cytochrome b561 and DOMON domain-containing protein At5g47530
- GDSL esterase/lipase At2g30310
- CASP-like protein 1A1
- GDSL esterase/lipase At1g28650
- GDSL esterase/lipase At1g74460
- Putative fructokinase-8
- Cytochrome b561 and DOMON domain-containing protein At4g17280
Sequence:
MEGVFLKMSVVGVSPMIPVGPSSFICAIGGSVEEKSTAASLPRWVSLRRLRPLEFLRIGGKREEKGTVRDDDAVLLERRDRNRNENDNGNWVLKILEVGSIWKGKRQRSGGGGGGEEDEEEEVAEPKKKEDLCEECDFCRIDDDDEDEEKEKTVFEFSEMLSKIPVEDAQMFAKLSFLGNLAYSIPKIKPENLLKYQKLRFVTSSIEKRMSLKVEENNNGEEDEEKKKLINPAVAYRIAASAASRLFSHSKSVLPFGSSKRQDNEEASLLATADSVTAVVAAKEEVKQAVADDLKSNRSPPCEWFVCDDDKSGTRFFFIQGSDSLASWQANLLFEPVPFEDLDVLVHRGIYEAAKGIYEQMLPEVHAHLNSRGKNRAFLRFSGHSLGGSLSLLVNLMLLIRGQVPASSLLPVITFGSPCIMCGGDRLLQKLGLPKSHLLGISMHRDIVPRAFSCNYPNRAAKLLKALNGNFRNHPCLNNQNVLYSPMGKLLILQPSERFSPPHPLLPPGSGLYLLASKNTDETEKSLRAAKILFFNSPHPLEILSDRRSYGSEGKIKRNHDMSSYLKALRHVIRKELKQMKAERDQWLRKFFIINILFSGRDSLKLITRFVASRSSQLVIIFFLPIRLLIMSVYSVVFHHSQAHFSFFK
Protein: Cytochrome c oxidase subunit 4 isoform 2, mitochondrial (Cytochrome c oxidase subunit IV isoform 2) (COX IV-2) (Q91W29)
Organism: Mus musculus (Mouse)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00423}; Single-pass membrane protein {ECO:0000250|UniProtKB:P00423}.
Interaction partners:
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
Sequence:
MFSRAARSLVMRTGLRTRGTGTHSPGDAAGSQRRMTPYVDCYAQRSYPMPDEPFCTELSEEQRALKEKEKGSWTQLSQAEKVALYRLQFHETFAEMNHRSNEWKTVMGCVFFFIGFTALVIWWQRVYVFPKKVVTLTEERKAQQLQRLLDMKSNPIQGLAAHWDYEKKEWKK
Protein: Linear element protein rec10 (Meiotic recombination protein rec10) (Q09823)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Organizes linear element components on chromosomes and is thus required for meiotic DNA recombination.
Subcellular location: Nucleus {ECO:0000269|PubMed:23395004, ECO:0000269|PubMed:31665745, ECO:0000269|PubMed:33825974}. Chromosome {ECO:0000269|PubMed:31665745}. Note=Localizes to DNA double-strand break (DSB) hotspots. {ECO:0000269|PubMed:31665745}.
Interaction partners:
- Linear element protein rec25
- Meiotic recombination protein rec11
- Linear element protein rec27
- Linear element protein Mug20
- Meiotic recombination protein rec15
- Linear element-associated protein hop1
- Meiotic recombination protein rec12
- Meiotic recombination protein rec7
- Meiotic recombination protein rec24
- Meiotic recombination protein rec8
Sequence:
MDIFSEFLNCLSSDGTLNESSIYKTYQILESLNPKDVDTKENYIKLSNTFSTLGSGVGFQDNLLIEMFKILTVLFFKTRSTDLGDLLIESFTSLEIEKLMRVKKTIGSIVLTKGIQELQEIELPKVGFNCMTYDESIFQGISLERLILQLMSIFIAKCEENKLWLVNNRKDLDLRVIGQRLLHRDFACRFLSGLFISRFSVSGDTDESKHQNGIRLQLFIDFSKFETRLTMQILKADRIFSTCVANTVHAYEGLFSSGSNIDSTIATLVLEPRDLIVYRKGFALLQIPWTSVTTIDKIKKVKSLKIITEVSSLDEFVFQCKDGDKFDELFSTSEEIMNKLLPAIIVSPKLTLRNRSIIQIKEGESKLPNTSKQASQNLPHLDDELAYQRFEDQVIDKSVCDDECTNTENTPSSNIPADVKDSLSADDYAYDTKRKTQIEDLEEDQNKSKIASKDGTNLKEINSVPEFSDENVINQTGPAKKTPVQRRKDGKFAKSTKRKKQKSLKPDTENQESSVKNKKAKSNVNLQYSPKTPICKINDETLKPPTIANIAGHKQMNHLTSENIETPVPVPNGNWYNGVKHETATDIFTTCHDGNNSLKSSVWKELLKEKHWKQESKPQLTGNSRQIDLSTFVKQANTPNITSLLDGTCSSPPNNECFNDKEPDSSSSTLISDRQELEYRNPNAETVKLEEIPYNKFFKTVEKNEAYNPSSKSATIDGLQRYTSMIGNQIYEGILQNEKELRSKLEAYHINCNKVIKEFSKRQTARYKIIEKELAQIEVNLVSQIDSLMFK
Protein: Helix-loop-helix protein 15 (Q18590)
Organism: Caenorhabditis elegans
Function: Transcription factor which binds the E box motif 5'-CA[TC][AG]TG-3' (By similarity). Involved in modulating physiological aging, probably by regulating expression of branched-chain amino acid transferase-1, bcat-1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Helix-loop-helix protein hlh-2
Sequence:
MLMEDGGLDTTSEEYRKLSKAERRKRRRATPKYRNLHATRERIRVESFNMAFSQLRALLPTLPVEKKLSKIEILRFSIAYISFLDNLLQ
Protein: Protein trichome birefringence-like 25 (Q84JH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the O-acetylation of mannan. May act as a bridging protein that binds pectin and other cell wall polysaccharides. Probably involved in maintaining esterification of pectins (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- At5g50410
Sequence:
MDSLRLISKSIKIEGTPFGSSHQRNQIFLKSVAFFLLIGLAYRFLITNSTVSPVPTVRSSPESLPPDPSGLTAITQTSASVDSPANITTIASQNVSTKCDIFIGNWVPDPSGPIYTNVSCRHIQDYQNCLKNGRPDVNYLRWRWQPRDCDLPRFNPEQFLDNMRNKWLAFIGDSISRNHVQSLLCILSQVEEVEDIFHDKEYKSRIWRFPSYNFTLSVIWSPFLVKAETFENGVPFSDIRVHLDKLDQKWTDQYINFDYVVISGGKWFLKTTIFHENNTVTGCHYCQGKNNMTELGYLYSYRKVLHLVLDFVAEPNHKAQVLFRTTTPDHFENGEWDSGGFCNRTMPFTEGSEGEMKSEDVSMRDIELEEFYKTTTTQQEGSNSNIVLLDTTSMSLLRPDGHPGPYRYPNPFAGLKNKELNQVQNDCLHWCLPGPIDSWNDLMVEVMLNRERQRRE
Protein: Candida glabrata strain CBS138 chromosome L complete sequence (Q6FLH9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MKFVSAILMASAVLAAPAVQHQDKHAHEKRDLVVVTEYVDQDGNIFTPTEVVNDAPAATPTPAPAAAPSSAAPAAPAASPAKDTTTLAPSSSKQQASQPTTGSSFTGGAFQDGTIPCSQFPSGNGVVALDWLNMGGWASIMDLNGNTASSCQEGFYCSYACESGMSKTQWPSNQPADGRSVGGLYCKGGFLYRANTNANTLCEQDAGTAFAENQVGQSIAICRTDYPGSENMVIPTVVGAGSTQPISVVKEDSYYQWKGMKTSAQFYVNNAGVSVENGCIWGNEGSGVGNWAPVVLGAGETNGITYLSIIPNPNNRTPPNFNVKIVATDGSSVNGACKYENGVYSGSGSDGCTVSVTSGSAKFVFY