wanglab/gogpt-training-data huggingface dataset:
Protein: Protein ERGIC-53 (ER-Golgi intermediate compartment 53 kDa protein) (Lectin mannose-binding 1) (p58) (Q9D0F3)
Organism: Mus musculus (Mouse)
Function: Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins (By similarity).
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Multiple coagulation factor deficiency protein 2 homolog
- Protein transport protein Sec31A
- Protein transport protein Sec23A
- Endoplasmic reticulum resident protein 44
- Vesicle-trafficking protein SEC22b
- Protein SEC13 homolog
- SEC24 homolog C, COPII coat complex component
- Calnexin
- Coatomer subunit beta
- SEC24 homolog B, COPII coat complex component)
Sequence:
MAVSRRRVPQAGARSFFCALLLSFSQFTGSDGTGGDAAAPGAAGTQAELPHRRFEYKYSFKGPHLVQSDGTVPFWAHAGNAIPSADQIRIAPSLKSQRGSVWTKAKAAFENWEVEVTFRVTGRGRIGADGLAIWYTENQGLDGPVFGSADTWNGVGIFFDSFDNDGKKNNPAIVVIGNNGQINYDHQNDGATQALASCQRDFRNKPYPVRAKITYYQKTLTVMINNGFTPDKNDYEFCAKVENMVIPTQGHFGISAATGGLADDHDVLSFLTFQLTEPGKEPPTAEKDISEKEKEKYQEEFEHFQQELDKKKEEFQKGHPDLQGQPADDIFESIGDRELRQVFEGQNRIHLEIKQLNRQLDMILDEQRRYVSSLTEEISRRGAGTPGQPGQVSQQELDTVVKSQQEILRQVNEVKNSMSETVRLVSGIQHPGSAGVYETTQHFMDIKEHLHVVKRDIDSLAQRSMPSNEKPKCPDLPPFPSCLSTIHFVIFVVVQTVLFVGYIMYRTQQEAAAKKFF
Protein: Homoserine kinase (HK) (HSK) (EC 2.7.1.39) (P29364)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Phosphoserine phosphatase ThrH
- Homoserine dehydrogenase
- Threonine synthase
- DUF2782 domain-containing protein
- Branched-chain-amino-acid aminotransferase
- Methionine synthase
- Homocysteine synthase
- Cysteine synthase B
- Adenosylhomocysteinase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
Sequence:
MSVFTPLERSTLEAFLAPYDLGRLRDFRGIAEGSENSNFFVSLEHGEFVLTLVERGPVQDLPFFIELLDVLHEDGLPVPYALRTRDGEALRRLEGKPALLQPRLAGRHERQPNAHHCQEVGDLLGHLHAATRGRILERPSDRGLPWMLEQGANLAPRLPEQARALLAPALAEIAALDAERPALPRANLHADLFRDNVLFDGPHLAGLIDFYNACSGWMLYDLAITLNDWCSNTDGSLDPARARALLAAYANRRPFTALEAEHWPSMLRVACVRFWLSRLIAAEAFAGQDVLIHDPAEFEIRLAQRQNVEIHLPFAL
Protein: Chitin synthase chs-2 (EC 2.4.1.16) (Chitin-UDP acetyl-glucosaminyl transferase chs-2) (G5EBQ8)
Organism: Caenorhabditis elegans
Function: May be involved in chitin synthesis in the pharynx during larval development.
Subcellular location: Cell membrane {ECO:0000305|PubMed:16098962}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable UDP-N-acetylglucosamine pyrophosphorylase
- Chitin synthase chs-1
- Protein adenylyltransferase fic-1
- Phosphoacetylglucosamine mutase
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- UDP-glucose 6-dehydrogenase
- JmjC domain-containing protein
- EGF-like domain-containing protein
- EGF-like domain-containing protein
- Mob1/phocein
Sequence:
MMNTLDHRPLGRMETMEGKPDEDEVPTSSNSDAKGKGYYYSSGTVPTDDSTLEEKCQQKTFDPSCPTPKTPVIVPNREFDPNFSTVTENKGWDIFRLLPPKPDRLGHGFWHDASLQVLKLATFLVLFLLTLGSAVVAKSTFILMTSAIGWGGQTITICNQVISEATQNTVKLKNAHVVKWVWATLLALSAPEALCFVRSMHRTMFRNVKRPTFIQFVFVLIIETFHSIGVGILVFRIFPDLDAVTAAQLTNAMCFVPAILSVISRKPNKSALLLVIIDFAAIAAQSSGFWALPMFLPNLQKHLVAIPVSLTLISLAWWQNFVHRDSVFPPVRTLAKFAQRLSERRSKTYAFVSLWKICIYVVCCFLFISSRMKIEDMLQKDPFGEKLLSVAGHDMNQTQIEKFQLRINQMIEQANREAGFYAAAEKKKQPPKKQPKADEAEQVDAGEYMMKRFKRFIGDAGENEEEEPEEEEFSSYNIYSNYVERNQLTMAYDALWLVIFQFGAVFVCYHSSKFACKVMMQRMGFALPMALSVPVTVLLLSTNCRMRQKDSCYGTNVLTVELFWQCNGASMSLADFILTPQTWIWLCWLASQFWITIHLWNPKHERLAKSEKLFILPYYIGAFVDQSLAFNRRRDDKAKIKAEDLEFDAEDSSLTYETIPGLQNKTPPSVCSASSSKLENGLIRDSASSADAITKIYACATMWHETGVEMTCMLKSLFRMDEDQCARRNAQKYLKVIDPDYYEFEAHIFFDDAYDVNEYGEPEINKFVKQIVNVIDQAASAVHQTQMRLKPPKKAKTPYGGKLTYIMPGKNKLFIHLKDNQKIRHRKRWSQVMYLYYLLGYRLMMKVDDPSRKEIISENTFILTLDGDVDFTPSSVYLLVDLMKKNRRLGAACGRIHPRGDGAMVWYQKFEYAIGHWLQKATEHMIGCVMCSPGCFSLFRAYALMDDNVARRYALKSEEPKHFIQYDQGEDRWLCTLLLQRGYRVEYCAASDAQTFAPEGFNEFFNQRRRWIPSTIFNIMDLLKDYRNVVRVNESISIWYIIYQLVMLISSILGPGTIFVMIIGAISISFSIDTLISLVIVSIPVVVFIVVCLTAKPEHQLICAQTIGAIFAMLMTAVVVGTSLQLQKDGLLSPHSMFTVAVATSFLTAAILHPLEFTCIIPGTIYFLAIPCMYMLLPIYSVCNMHTVSWGTREDPRPTEKNTLAKKTPGNLESGDGAGNSENWCTRFLCCGRGTVHPMTMVINEKLNEVIKKVDRLDRKHHPSLARRASILSSTGGTIQIDKCSEADEDEQAEIEDALEMSNQSHAAKKNQKWKQAQSEAWLADKALKRAEREYLEPEEESFWNDVIERYLSPLIMDGKDMDRLRAGLIAIRNSHTVYFLMINIVFIISVLVLQIHKDCLNIEWPLGPKFNHTVRPCYANHDDNQKEEVWVMTRLQLEPIGLVFLIFFVSILVIQFLAMLCHRFGTLAHIIASTELFCFRKTMDRLSEDELVAQNAVEIARELQAIRGIDENAHNIDNPTEDRGISRRRVVQNLESSRKSMMKRKTETLDAAFKKRFFALSSEQTPDPAGFSARDNSKRLTLRKGTIRALEHRRDSLFGTLDNRKDDEVDATSMRGPAQRRLERLFTAQQDQNSPTSDGNRRKSNSRPWDQPTSSATSSGDVELRRF
Protein: Oxidoreductase UcpA (EC 1.-.-.-) (P37440)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Lactaldehyde reductase
- NADH-quinone oxidoreductase subunit C/D
Sequence:
MGKLTGKTALITGALQGIGEGIARTFARHGANLILLDISPEIEKLADELCGRGHRCTAVVADVRDPASVAAAIKRAKEKEGRIDILVNNAGVCRLGSFLDMSDDDRDFHIDINIKGVWNVTKAVLPEMIARKDGRIVMMSSVTGDMVADPGETAYALTKAAIVGLTKSLAVEYAQSGIRVNAICPGYVRTPMAESIARQSNPEDPESVLTEMAKAIPMRRLADPLEVGELAAFLASDESSYLTGTQNVIDGGSTLPETVSVGI
Protein: Rifin (Q8IM84)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFAFPLNILVNTHKKPSITPHHTPKIPTTRLLCECELFEPANYDSDPQMRAVMDNFSKQTQQRFHEYDESLQSKRMQCKDKCDKEIQKIILKDKLEKQMKQELTTLETKITTDDIPTCICEKSVADKMEKGCLRCAGVFSGGVAPSVGLLGGIGVYGWKMGAPTVAMELAKQAGIEEGVKTVIAQIKGISIFNPYLESVECSKYITKLNYDNVSGLMKAVQAAIKSTGETCEANSGDIVCETIYNKVERFLPVVQAGKQATTTTTETVKNAALDTIESTATTCTTAITASIIAIVVIVLIMVIIYKILRYRRKKKMKKKLQYIKLLEE
Protein: Olfactory receptor 5AN6 (Olfactory receptor 1440) (Olfactory receptor 202-4) (Q8VFV4)
Organism: Mus musculus (Mouse)
Function: Odorant receptor involved in the detection of muscone.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Guanine nucleotide-binding protein G
Sequence:
MPGGRNSTVITKFILVGFSDFPKLKLVLFVIFLGSYLSTVVWNLGLIILIRIDPYLHTPMYFFLSNLSFLDFCYISSTTPKMLSGFFQKSKSISFVGCTMQYFIFSSLGLSECCLLAAMAYDRYAAICNPLLYTAIMSPSLCVHMVVGAYSTGLLGSLIQLCAILQLHFCGPNIINHFFCDLPQLLVLSCSETFPLQVLKFVIAVIFGVASVIVILISYGYIIGTILNISSVEGRSKAFNTCASHLTAVTLFFGSGLFVYMRPSSNSSQGYDKMASVFYTVVIPMLNPLIYSLRNKEIKDALQRCKNKCFSQCHC
Protein: Ribosomal protein S24/S35 (Q683K3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MRGALFRNASLCARRIILSSRISPNVPFLTPIAAPAPPKFRFFSSESGENSTTATESSPTDSSDKKDLVVEDVSNKELKSRIDKSFNEGNEDALPGVIEALLQRRLVDKHAETDDELMEKIESLPFKDDVKDEDFESDFEEAHSTDEELEDLYNSPEYVAEKMRKKEFFNMDDNKWDHMIREGIQHGCLTDTKQCEEILEDMLKWDQLLPDDLKKKVEAKFNELGDMCERGEIEAEAAYELFKEFEDEMVIQYGDQMEAEGPPQFGETDTSDRNTDLDDPSGKGPILRWQSRIVFAPGGDAWHPKNRKVKMSVTVKELGLSNHQAKRLRELVGKRYHSGKDELTITCERFEHREENRKDCLRTLYGLIEEAGKANKIAEDIRTSYVKQRLRASPAFMQKLQAKIIRSKESNAINA
Protein: NAD(P)H-quinone oxidoreductase subunit 3, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 3) (NADH-plastoquinone oxidoreductase subunit 3) (P56751)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01394}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01394}.
Interaction partners:
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
Sequence:
MFLLYEYDIFWAFLLISSAIPVLAFLISGVLSPIRKGPEKLSSYESGIEPIGDAWLQFRIRYYMFALVFVVFDVETVFLYPWAMSFDVLGVSAFIEAFIFVLILILGLVYAWRKGALEWS
Protein: Ribonuclease G (Q726Q1)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Polyribonucleotide nucleotidyltransferase
- Enolase
- RNA-binding protein KhpB
- ATP-dependent RNA helicase RhlE
- RNA-binding protein KhpA
- Epoxyqueuosine reductase QueH
- Nucleotide-binding protein DVU_1631
- ATP-dependent RNA helicase, DEAD/DEAH box family
- DEAD-box ATP-dependent RNA helicase RhpA
Sequence:
MTTAKKGKRKMYISVLPGEQVEVALSEDGAVTEYYVEMLHQAKTKGNIYKGVINNIDTNLQAAFVNYGAEKNGFLQIDEVHPEYYISPHDPTKGKKYPLMQKVLKAGQEVLVQVVKEPTGNKGAFLTSYLSLPGRFLVLTPGREQIGVSRKVEDDEERSRLREMLEGLSAGPGLGVIVRTVSAGTSKTTLQRDLQFLKRLWKDVRKKGTTEQTPCQIYQEPDLATRSVRDYLTDDVSEVWVDDAATAELIREFVTLVFPRKASLVKLHTDPERTLWERFGIRKQLDQIYSREVILPSGGRLVFDQTEALMAIDINSGKIAGKTNFESMALKTNTEAAESIAQQLRLRDIGGQVVIDFIEMRDHNHWREVEKTLRNAMKGDRARHDVGKMSRFGLLQVVRQRTGSSALSITMEACPCCRGSGLRRNMEWQSLQALRELHRQLRALPQGQCVHVFETSPELAFYLLNHKRERLLELERRFNLRLEVRPTGK
Protein: Major capsid protein 2 (MCP2) (Q914J5)
Organism: Sulfolobus islandicus filamentous virus (isolate Iceland/Hveragerdi) (SIFV)
Function: Self-assembles to form a helical, filamentous nucleocapsid mesuring 1980 nm in length and 24 nm in width. Together with capsid protein 1, wraps arounds the DNA and maintains it in an A-form. Capsid proteins probably maintain the DNA in A-form by non-specific desolvation and specific coordination of the DNA phosphate groups by positively charged residues. This certainly protects the viral DNA under conditions such as the extreme desiccation of its host.
Subcellular location: Virion {ECO:0000269|PubMed:32759221}.
Interaction partners:
Sequence:
MARRNRRLSSASVYRYYLKRISMNIGTTGHVNGLSIAGNPEIMRAIARLSEQETYNWVTDYAPSHLAKEVVKQISGKYNIPGAYQGLLMAFAEKVLANYILDYKGEPLVEIHHNFLWELMQRQSGAGLGVTSGFIYTFVRKDGKPVTVDMSKVLTEIEDALFKLVKK
Protein: Poly(A)-specific ribonuclease PARN (EC 3.1.13.4) (Polyadenylate-specific ribonuclease) (A0A494C1K5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEYMGRKQEEKQIKRKWTEDSWKEADSKRLNPQCIPYTLQNHYYRNNSFRISSRIPYYIWPSYLHRLL
Protein: EGF-containing fibulin-like extracellular matrix protein 2 (Fibulin-4) (FIBL-4) (Mutant p53-binding protein 1) (Q9WVJ9)
Organism: Mus musculus (Mouse)
Function: Plays a crucial role in elastic fiber formation in tissue, and in the formation of ultrastructural connections between elastic laminae and smooth muscle cells in the aorta, therefore participates in terminal differentiation and maturation of smooth muscle cell (SMC) and in the mechanical properties and wall integrity maintenance of the aorta. In addition, is involved in the control of collagen fibril assembly in tissue throught proteolytic activation of LOX leading to cross- linking of collagen and elastin. Also promotes ELN coacervation and participates in the deposition of ELN coacervates on to microfibrils but also regulates ELN cross- linking through LOX interaction. Moreover adheres to the cells through heparin binding in a calcium-dependent manner and regulates vascularlar smooth muscle cells proliferation through angiotensin signaling.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17324935, ECO:0000269|PubMed:26178373, ECO:0000269|PubMed:26690653}. Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:17324935}. Note=Localizes on the microfibrils surrounding ELN cores. {ECO:0000269|PubMed:17324935}.
Interaction partners:
- Elastin
- Fibrillin-1
- Microfibrillar-associated protein 2
- Protein-lysine 6-oxidase
- Lysyl oxidase homolog 1
- Microfibrillar-associated protein 5
- Peptidyl-prolyl cis-trans isomerase FKBP10
- Latent-transforming growth factor beta-binding protein 1
- Collagen alpha-1
Sequence:
MLPFASCLPGSLLLWAFLLLLLGAASPQDPEEPDSYTECTDGYEWDADSQHCRDVNECLTIPEACKGEMKCINHYGGYLCLPRSAAVISDLHGEGPPPPAAHAQQPNPCPQGYEPDEQESCVDVDECTQALHDCRPSQDCHNLPGSYQCTCPDGYRKIGPECVDIDECRYRYCQHRCVNLPGSFRCQCEPGFQLGPNNRSCVDVNECDMGAPCEQRCFNSYGTFLCRCNQGYELHRDGFSCSDIDECGYSSYLCQYRCVNEPGRFSCHCPQGYQLLATRLCQDIDECETGAHQCSEAQTCVNFHGGYRCVDTNRCVEPYVQVSDNRCLCPASNPLCREQPSSIVHRYMSITSERSVPADVFQIQATSVYPGAYNAFQIRSGNTQGDFYIRQINNVSAMLVLARPVTGPREYVLDLEMVTMNSLMSYRASSVLRLTVFVGAYTF
Protein: Pulmonary surfactant-associated protein D (PSP-D) (SP-D) (Collectin-7) (Lung surfactant protein D) (P35247)
Organism: Homo sapiens (Human)
Function: Contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
Subcellular location: Secreted, extracellular space, extracellular matrix. Secreted, extracellular space, surface film.
Interaction partners:
- Surfactant protein C
- Deleted in malignant brain tumors 1 protein
- Pulmonary surfactant-associated protein B
- Leukocyte-associated immunoglobulin-like receptor 1
- Tyrosine-protein phosphatase non-receptor type substrate 1
- Prolow-density lipoprotein receptor-related protein 1
- Calreticulin
- Pulmonary surfactant-associated protein A1
- Uteroglobin
- Surfactant protein A2
Sequence:
MLLFLLSALVLLTQPLGYLEAEMKTYSHRTMPSACTLVMCSSVESGLPGRDGRDGREGPRGEKGDPGLPGAAGQAGMPGQAGPVGPKGDNGSVGEPGPKGDTGPSGPPGPPGVPGPAGREGPLGKQGNIGPQGKPGPKGEAGPKGEVGAPGMQGSAGARGLAGPKGERGVPGERGVPGNTGAAGSAGAMGPQGSPGARGPPGLKGDKGIPGDKGAKGESGLPDVASLRQQVEALQGQVQHLQAAFSQYKKVELFPNGQSVGEKIFKTAGFVKPFTEAQLLCTQAGGQLASPRSAAENAALQQLVVAKNEAAFLSMTDSKTEGKFTYPTGESLVYSNWAPGEPNDDGGSEDCVEIFTNGKWNDRACGEKRLVVCEF
Protein: Cellulose synthase-like protein B5 (AtCslB5) (EC 2.4.1.-) (Q0WT40)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable pectinesterase/pectinesterase inhibitor 60
- Probable pectinesterase/pectinesterase inhibitor 59
- RING-H2 finger protein ATL11
- Receptor protein kinase-like protein
- Protein DETOXIFICATION 13
- Pectin lyase-like superfamily protein
- DUF21 domain-containing protein At5g52790
- GRAS family transcription factor family protein
- WAT1-related protein At4g01440
- Sulfite exporter TauE/SafE family protein 2
Sequence:
MADSSSSLHPLCERISHKSYVLRAVDLTILGLLYSLLLYRILHISENDNVWLLAFFCESCFSLVWLIFTCLKWSPAEDIPYINTLNERVHDLPSLDMFVPTADTVRESPIITVNTVLSLLAVNYPANKLACYVSDDGCSPLTYFSLKEASKFVKIWAPFCKKYNVRVRAPFRYFLNPLVATDDSVFSKDWKMMKREYVKLCRKVEDATGDSHWLDADDDFEAFSNTKPNDHSTIVKVVWENKGGVGDEKEVPHLVYISREKRPNYLHHYKTGAMNFLLRVSGLMTNAPYTLNVDCDMYANEPDVVRQAMCVFLQNSKNSNHCAFVQFPQKFYDSYTNELAVLQSILGRGVAGIQGPFYIGTGCFHTRRVMYGLSSDDLEDNGNISQVATREFLAEDSLVRKYGNSKELVKSVVDALQRKSNPQKSLANLIEAAQEVGHCHYEYQTSWGNLGWMYDSVAEDINTSVGIHLRGWTSSFISPDPPAFIGSTPTLGLEAIVQQRRWATGAIEVLFNKQSPFMGMFHGKIKFRQRLAYFWALMCLRSIPELIYCLLPAYCLLHDSALFPKGPCLCTIVTLVGMHCLYSLWQFMSLGFSVQSWYVVQSLWRIIATSSWLFSIQDIILKLLGISQIGFVIAKKTIPETKSVYESKPSQGEDDVPKLNLGKFEFDSSGLFIPGTFIMLVNLAALAGYLVRLQRSSCSHGGGGSGLAEACGCILVVMLFLPFLKGLFEHGKYSIPLSTLSKAAFLTVLFVFFCVGK
Protein: Hadley, isoform A (Hadley, isoform C) (RE63660p) (Q8SXY1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNRTSLSSGSTSRRLPALLFVLLLCLVARTNGRPSQEDESDLAIIPPDADNVEIHKVKIVNGVMQEDHPVIMYKEDFVSEDYDPTKSETNPSHHKKHKRTRLHHAKQVTGTEKKEDQILFDILPDKPIVLEEDLKALPHSKVGAAQLAEPIKEEWLAKHPKKYHSRQRRQAPVSFEKVLQYYYGTPEIKFVSPLTYTHFRISVKGKKPHLVGPPNRRNQGQENIPTPDSVDSRGEFDLIHNSNQADADFSIYNRSSTTTARPIFQINDSDFVTSAPSWRPSNSIRRPPPTRSPVVGLPTMRPNARPVPQTGGVDSEPKVSRCVWAIVNCCTGESKKVRYNCFEEFGCHGAFWDINPCADEGVKQGALTKVLDAFQNQ
Protein: Protein DROOPING LEAF (Protein CRABS CLAW homolog) (Protein CRC homolog) (Q76EJ0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Regulates carpel specification in flower development. Severe or intermediate mutation in DL causes complete or partial homeotic conversion of carpels into stamens without affecting the identities of other floral organs. Interacts antagonistically with class B genes and controls floral meristem determinacy. Regulates midrib formation in leaves probably by inducing cell proliferation in the central region of the leaf.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDLVSPSEHLCYVRCTYCNTVLAVGVPCKRLMDTVTVKCGHCNNLSFLSPRPPMVQPLSPTDHPLGPFQGPCTDCRRNQPLPLVSPTSNEGSPRAPFVVKPPEKKHRLPSAYNRFMREEIQRIKAAKPDIPHREAFSMAAKNWAKCDPRCSSTVSTSNSNPEPRVVAAPIPHQERANEQVVESFDIFKQMERSG
Protein: Pheophorbide a oxygenase, chloroplastic (AtPaO) (Pheide a oxygenase) (EC 1.14.15.17) (Accelerated cell death 1) (Lethal leaf-spot 1 homolog) (Lls1) (Q9FYC2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the key reaction of chlorophyll catabolism, porphyrin macrocycle cleavage of pheophorbide a (pheide a) to a primary fluorescent catabolite (pFCC). Works in a two-step reaction with red chlorophyll catabolite reductase (RCCR). Creates the intermediate RCC through the opening of the porphyrin macrocycle by the introduction of one atom of molecular oxygen at the alpha-methine bridge. Seems to be specific for pheide a. Belongs to the chlorophyll catabolic enzymes (CCEs).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:22366162}.
Interaction partners:
- Red chlorophyll catabolite reductase, chloroplastic
- Probable chlorophyll
- pFDCC methylesterase MES16
- Pheophytinase, chloroplastic
- Magnesium dechelatase SGR1, chloroplastic
- Chlorophyll
- 7-hydroxymethyl chlorophyll a reductase, chloroplastic
- Chlorophyllase-2
- Chlorophyllase-1
- Magnesium dechelatase SGRL, chloroplastic
Sequence:
MSVVLLSSTSATITKSQSKKIPFLSPTTKFPLKVSISPSRSKLFHNPLRVAAPPSVPTSDSTEEKRIEEEYGGDKEEEGSEFKWRDHWYPVSLVEDLDPNVPTPFQLLGRDLVLWFDRNDQKWAAFDDLCPHRLAPLSEGRLDENGHLQCSYHGWSFGGCGSCTRIPQAATSGPEARAVKSPRACAIKFPTMVSQGLLFVWPDENGWDRANSIEPPRLPDDFDKPEFSTVTIQRDLFYGYDTLMENVSDPSHIDFAHHKVTGRRDRAKPLPFKVESSGPWGFQGANDDSPRITAKFVAPCYSMNKIELDAKLPIVGNQKWVIWICSFNIPMAPGKTRSIVCSARNFFQFSVPGPAWWQVVPRWYEHWTSNLVYDGDMIVLQGQEKVFLAKSMESPDYDVNKQYTKLTFTPTQADRFVLAFRNWLRRHGKSQPEWFGSTPSNQPLPSTVLTKRQMLDRFDQHTQVCSSCKGAYNSFQILKKFLVGATVFWAATAGVPSDVQIRLVLAGLSLISAASAYALHEQEKNFVFRDYVHSEIE
Protein: Homeodomain-like superfamily protein (Q9XEB2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQDPMVRSYIRSDNPRMHWTDDLDIRFIQVIEKLGGEESATPKRILSLMGVRDLTISHVKSHLQMYRNKKKEESSKEIKMMREMTQRQSQQYLQIYERATQFIQNQQRLQLDNTEKITPVLGSSNKSLDQSSKVGLNENRGNDVVVVGGATGEEELSLELTLGRKY
Protein: Very-long-chain aldehyde decarbonylase GL1-1 (EC 4.1.99.5) (Protein GLOSSY 1-1) (Q69PA8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aldehyde decarbonylase involved in the conversion of aldehydes to alkanes. Core component of a very-long-chain alkane synthesis complex.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:F4HVY0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:F4HVY0}.
Interaction partners:
Sequence:
MGAAFLSSWPWDNLGAYKYVLYAPLVGKAVAGRAWERASPDHWLLLLLVLFGVRALTYQLWSSFSNMLFATRRRRIVRDGVDFGQIDREWDWDNFLILQVHMAAAAFYAFPSLRHLPLWDARGLAVAALLHVAATEPLFYAAHRAFHRGHLFSCYHLQHHSAKVPQPFTAGFATPLEQLVLGALMAVPLAAACAAGHGSVALAFAYVLGFDNLRAMGHCNVEVFPGGLFQSLPVLKYLIYTPTYHTIHHTKEDANFCLFMPLFDLIGGTLDAQSWEMQKKTSAGVDEVPEFVFLAHVVDVMQSLHVPFVLRTFASTPFSVQPFLLPMWPFAFLVMLMMWAWSKTFVISCYRLRGRLHQMWAVPRYGFHYFLPFAKDGINNQIELAILRADKMGAKVVSLAALNKNEALNGGGTLFVNKHPGLRVRVVHGNTLTAAVILNEIPQGTTEVFMTGATSKLGRAIALYLCRKKVRVMMMTLSTERFQKIQREATPEHQQYLVQVTKYRSAQHCKTWIVGKWLSPREQRWAPPGTHFHQFVVPPIIGFRRDCTYGKLAAMRLPKDVQGLGACEYSLERGVVHACHAGGVVHFLEGYTHHEVGAIDVDRIDVVWEAALRHGLRPV
Protein: DNA mismatch repair protein MSH5 (AtMSH5) (MutS protein homolog 5) (F4JEP5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in meiotic recombination in association with MSH4. Required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis. Promotes homologous recombination through facilitating chiasma formation during prophase I. Involved in the control of class I crossovers formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:18318687}. Chromosome {ECO:0000269|PubMed:18318687}. Note=In pollen mother cells during meiosis, localizes to unsynapsed axes during leptotene and zygotene, but is not present on synapsed regions of zygotene nuclei. {ECO:0000269|PubMed:18318687}.
Interaction partners:
- DNA mismatch repair protein MLH1
- DNA mismatch repair protein PMS1
- DNA mismatch repair protein MLH3
- DNA mismatch repair protein MSH3
- DNA mismatch repair protein MSH6
- Exonuclease 1
- DNA mismatch repair protein MSH7
- DNA mismatch repair protein MSH1, mitochondrial
- DNA mismatch repair protein MSH4
- ATP-dependent DNA helicase homolog MER3
Sequence:
MEEMEDTETEPQVYMACIQHGRRVGVSYYDCSVRQLHVLEFWEEDCSDFTLINMVKYQAKPSIIYASTKSEESFVAALQQNDGTDETTMVKLVKSSTFSYEQAWHRLVYLRVTGMDDGLNIKERICYLSSMMDVGSEVQVRVSGGLLAILESERIVETLEQNESGSASIAIDSVMEVPLNKFLKLDAAAHEALQIFQTDKHPSHMGIGRAKEGFSVFGMMNKCATPMGRRLLRSWFMRPILDLEVLDRRLNAISFFISSVELMASLRETLKSVKDISHLLKKFNSPTSLCTSNDWTAFLKSISALLHVNKIFEVGVSESLREHMRRFNLDIIEKAGLCISTELDYVYELVIGVIDVTRSKERGYQTLVKEGFCAELDELRQIYEELPEFLQEVSAMELEHFPHLHKEKLPPCIVYIQQIGYLMCIFGEKLDETALNRLTEFEFAFSDMDGETQRFFYHTSKTRELDNLLGDIYHKILDMERAIIRDLLSHTLLFSAHLLKAVNFVAELDCILSLACVAHQNNYVRPVLTVESLLDIRNGRHVLQEMAVDTFIPNDTEINDNGRIHIITGPNYSGKSIYVKQVALIVFLSHIGSFVPADAATVGLTDRIFCAMGSKFMTAEQSTFMIDLHQVGMMLRQATSRSLCLLDEFGKGTLTEDGIGLLGGTISHFATCAEPPRVVVCTHLTELLNESCLPVSEKIKFYTMSVLRPDTESANMEEIVFLYRLIPGQTLLSYGLHCALLAGVPEEVVKRAAIVLDAFESNNNVDKLSLDKISSQDQAFKDAVDKFAELDISKGDIHAFFQDIFTS
Protein: E3 ubiquitin-protein ligase CSU1 (EC 2.3.2.27) (Protein COP1 SUPPRESSOR 1) (RING-type E3 ubiquitin transferase CSU1) (Q9SY88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: RING-finger E3 ubiquitin-protein ligase that plays an major role in maintaining COP1 homeostasis in darkness. Negatively regulates COP1 protein accumulation by targeting COP1 for ubiquitination and subsequent proteasomal degradation in dark-grown seedlings. Negatively regulates the accumulation of SPA1 protein in the dark.
Subcellular location: Nucleus {ECO:0000269|PubMed:24838976}. Nucleus speckle {ECO:0000269|PubMed:24838976}. Note=Is recruited to nuclear speckles by COP1 in the dark. {ECO:0000269|PubMed:24838976}.
Interaction partners:
- Protein COP1 SUPPRESSOR 2
- Probable E3 ubiquitin-protein ligase RHA1A
- At3g29270
- E3 ubiquitin-protein ligase RMA
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Probable E3 ubiquitin-protein ligase WAVH2
- SBP family protein
- AP-3 complex subunit mu
- Putative E3 ubiquitin-protein ligase ORTHRUS 4
- B-box zinc finger protein 22
Sequence:
MPQRHSKNNNDLAYFTYDEKKKLGYGTQRERLGRDSIKPFDACSLCLKPFIDPMCCHKGHVFCRECILECFLAQKKDIQRRLAAHSSQKKQDKDEEEERLMLQKARELDEFDQQNHSAMPRNSDKNHNEDKNGFHGANSVKTTSFEEEALRTMKAFWLPSATPAASVRVDAPETHTVCPEGKEKLKLKNLFAIRFTEDNSEEEETKTKSASSSSYDKSYICPSCKVTLTNTMSLVALSSCGHVFCKKCAEKFMPVDKVCLVCDKPCKDRNLVGLKKGGTGFAEHDDHLEAKEYKHLGSGSGLGLVRPVKT