wanglab/gogpt-training-data huggingface dataset:
Protein: Zip homologous protein 1 (Q95R14)
Organism: Caenorhabditis elegans
Function: Recruited co-dependently with zhp-2 to the synaptonemal complex between homologous chromosome pairs to regulate the formation and number of crossover events between homologs during meiotic recombination. Together with zhp-2, promotes the accumulation of pro-crossover proteins, including zhp-3 and zhp-4, at a designated crossover site along the recombination intermediate. Limits the number of crossover sites along a recombination intermediate by restricting the association of these pro-crossover proteins with other recombination sites during late prophase. Also, together with zhp-2, plays a role in chromosome remodeling following crossover formation to promote two successive rounds of chromosome segregation during meiosis.
Subcellular location: Chromosome {ECO:0000269|PubMed:29521627}. Note=In association with zhp-2, localizes to chromosomes from pachytene to early diakinesis in the germ line (PubMed:29521627). Co-localizes with syp-1, a component of the synaptonemal complex from early prophase to mid-pachytene (PubMed:29521627). From mid-pachytene to diplotene, co-localizes with syp-1 on one side of each crossover site (PubMed:29521627). Remains co-localized with syp-1 along the short arm of homologous chromosomes through to late diakinesis (PubMed:29521627). At late pachytene, localization at chromosomes is not dependent on syp-1 (PubMed:29521627). {ECO:0000269|PubMed:29521627}.
Interaction partners:
- Histidine-rich glycoprotein-like
- Cyclin N-terminal domain-containing protein
- MutS protein homolog 5
- Meiotic recombination protein spo-11
- Zip homologous protein 2
- Long arms of the bivalent protein 1
- HORMA domain-containing protein
Sequence:
MEFIVCNGCGCSPSKRQFFITACSHVFCETCRTTPTADFCHLCKIPTKTLKMDASLPKNVKKMFGDVGVMSTDIHKRLARVIGFQKIQKSIQLKMENKKSVMRKEQTKKVEKKTEEMHCQLSKLTSFEENNRKKLEDIERENEKLRNLISALELKVASSRDIDDDEFFMQGTPTSSNPSVAGSDVDNDELLDYDLLGLRNRSDSSSSNCSSQSNRGGSLF
Protein: Myosin-2 essential light chain (Q9XVI9)
Organism: Caenorhabditis elegans
Function: Required for cytokinesis and embryo elongation. May regulate myosin II complex formation and/or the association of myosin with actin. May be involved in the organization of mlc-4 and nmy-2 into bundles.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19675126}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19675126}. Note=Forms a filamentous structure during 2-fold embryonic stage which may co-localize with actin and whose formation may be regulated by mlc-4. {ECO:0000269|PubMed:19675126}.
Interaction partners:
- Myosin regulatory light chain
- Myosin-11
- Myosin-11
- Myosin regulatory light chain 1
- Myosin regulatory light chain 2
- Troponin I 4
- Troponin I 3
- Troponin I 2
- Myosin-2
- Myosin-3
Sequence:
MDDLADCREVFAYFDSKGDERISVQQVGDVLRALGQNPTEAEIHKCVGSFDREARLSFEDFVPIFQSVSKNREKHTVEEFVEGLSHFDKEGNGMINVAELRHLLTTLGERLSDEDVDQLLSGHNDSHGNVNISDFVRAVMNS
Protein: Splicing factor U2af large subunit A (U2 auxiliary factor 65 kDa subunit A) (U2 small nuclear ribonucleoprotein auxiliary factor large subunit A) (U2 snRNP auxiliary factor large subunit A) (O23212)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Necessary for the splicing of pre-mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:24580679}.
Interaction partners:
- Splicing factor U2af small subunit A
- Nuclear protein-like
- Splicing factor U2af small subunit B
- Zinc finger C-x8-C-x5-C-x3-H type family protein
- Serine/arginine-rich splicing factor SR30
- RNA-binding KH domain-containing protein
- U1 small nuclear ribonucleoprotein 70 kDa
- Serine/arginine-rich splicing factor SR34B
- Splicing factor U2af large subunit B
- RNA-binding
Sequence:
MSEFEDHEGNGTVADAIYDEENGGRDGEIEDQLDSKPKRESRDHERETSRSKDREREKGRDKDRERDSEVSRRSRDRDGEKSKERSRDKDRDHRERHHRSSRHRDHSRERGERRERGGRDDDDYRRSRDRDHDRRRDDRGGRRSRRSRSRSKDRSERRTRSRSPSKSKQRVSGFDMAPPASAMLAAGAAVTGQVPPAPPTLPGAGMFPNMFPLPTGQSFGGLSMMPIQAMTQQATRHARRVYVGGLSPTANEQSVATFFSQVMAAVGGNTAGPGDAVVNVYINHEKKFAFVEMRSVEEASNAMSLDGIIFEGAPVKVRRPSDYNPSLAATLGPSQPSPHLNLAAVGLTPGASGGLEGPDRIFVGGLPYYFTESQVRELLESFGGLKGFDLVKDRETGNSKGYAFCVYQDLSVTDIACAALNGIKMGDKTLTVRRANQGTMLQKPEQENVLLHAQQQIAFQRVMLQPGAVATTVVCLTQVVTEDELRDDEEYGDIMEDMRQEGGKFGALTNVVIPRPSPNGEPVAGLGKVFLKYADTDGSTRARFGMNGRKFGGNEVVAVYYPEDKFEQGDYGA
Protein: RalBP1-associated Eps domain-containing protein 2 (Partner of RalBP1) (RalBP1-interacting protein 2) (Q8NFH8)
Organism: Homo sapiens (Human)
Function: Involved in ligand-dependent receptor mediated endocytosis of the EGF and insulin receptors as part of the Ral signaling pathway. By controlling growth factor receptors endocytosis may regulate cell survival. Through ASAP1 may regulate cell adhesion and migration.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12771942}.
Interaction partners:
- RalA-binding protein 1
- Epsin-1
- AP-2 complex subunit alpha-1
- Epsin-2
- RalBP1-associated Eps domain-containing protein 1
- Growth factor receptor-bound protein 2
- AP-2 complex subunit mu
- Epsin-3
- Epidermal growth factor receptor substrate 15
- Ras-related protein Ral-A
Sequence:
MEAAAAAAAAAAAAAAAGGGCGSGPPPLLLSEGEQQCYSELFARCAGAAGGGPGSGPPEAARVAPGTATAAAGPVADLFRASQLPAETLHQITELCGAKRVGYFGPTQFYIALKLIAAAQSGLPVRIESIKCELPLPRFMMSKNDGEIRFGNPAELHGTKVQIPYLTTEKNSFKRMDDEDKQQETQSPTMSPLASPPSSPPHYQRVPLSHGYSKLRSSAEQMHPAPYEARQPLVQPEGSSSGGPGTKPLRHQASLIRSFSVERELQDNSSYPDEPWRITEEQREYYVNQFRSLQPDPSSFISGSVAKNFFTKSKLSIPELSYIWELSDADCDGALTLPEFCAAFHLIVARKNGYPLPEGLPPTLQPEYLQAAFPKPKWDCQLFDSYSESLPANQQPRDLNRMEKTSVKDMADLPVPNQDVTSDDKQALKSTINEALPKDVSEDPATPKDSNSLKARPRSRSYSSTSIEEAMKRGEDPPTPPPRPQKTHSRASSLDLNKVFQPSVPATKSGLLPPPPALPPRPCPSQSEQVSEAELLPQLSRAPSQAAESSPAKKDVLYSQPPSKPIRRKFRPENQATENQEPSTAASGPASAATMKPHPTVQKQSSKQKKAIQTAIRKNKEANAVLARLNSELQQQLKEVHQERIALENQLEQLRPVTVL
Protein: Myosin heavy chain 2 (F1LMU0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, myofibril {ECO:0000256|ARBA:ARBA00004657}.
Interaction partners:
Sequence:
MSSDAEMAVFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVVDAKESYVKATVQSREGGKVTAKTEGGATVTVKEDQVFSMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAVTGDKKKEEAPSGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQVMSNKKPELIEMLLITTNPYDFAYVSQGEITVPSIDDQEELMATDTAVDILGFTADEKVAIYKLTGAVMHYGNMKFKQKQREEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKAMYEKMFLWMVTRINQQLDTKQPRQYFIGVLDIAGFEIFDFNTLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSNNFQKPKPAKGKAEAHFSLVHYAGTVDYNIIGWLDKNKDPLNETVVGLYQKSGLKTLAFLFSGGQAAEAEGGGGKKGGKKKGSSFQTVSALFRENLNKLMTNLKSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFKAGLLGTLEEMRDEKLAQLITRTQAVCRGYLMRVEFRKMMERRESIFCIQYNVRAFMNVKHWPWMKLYFKIKPLLKSAETEKEMATMKEDFEKAKEDLAKSEAKRKELEEKMVALMQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDENIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKLAQESTMDIENDKQQLDEKLKKKEFEMSNLQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEQQRLINELSAQKARLHTESGEFSRQLDEKDAMVSQLSRGKQAFTQQIEELKRQLEEESKAKNALAHALQSARHDCDLLREQYEEEQEAKAELQRAMSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQRNFDKVLAEWKQKYEETQAELEASQKESRSLSTELFKVKNAYEESLDQLETLKRENKNLQQEISDLTEQIAEGGKHIHELEKIKKQIDQEKSELQASLEEAEASLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIRNLRNTQGMLKDTQLHLDDALRGQDDLKEQLAMVERRANLMQAEIEELRASLEQTERSRRVAEQELLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELENEVENEQKRNIEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQTKVKAYKRQAEEAEEQSNVNLAKFRKIQHELEEAEERADIAESQVNKLRVKSREVHTKVISEE
Protein: Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial (MM-ALDH) (MMSDH) (Malonate-semialdehyde dehydrogenase [acylating]) (EC 1.2.1.27) (Aldehyde dehydrogenase family 6 member B2) (Q0WM29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000305|PubMed:25732537}.
Interaction partners:
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Probable 3-hydroxyisobutyrate dehydrogenase-like 1, mitochondrial
- Probable 3-hydroxyisobutyrate dehydrogenase-like 3, mitochondrial
- Probable 3-hydroxyisobutyrate dehydrogenase-like 2, mitochondrial
- Acetyl-CoA acetyltransferase 2
- Probable 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase 1
- 3-ketoacyl-CoA thiolase 1, peroxisomal
- 3-ketoacyl-CoA thiolase 5, peroxisomal
- 3-ketoacyl-CoA thiolase 2, peroxisomal
Sequence:
MVRVKQKNLESYRSNGTYPPTWRNPTTSFAPDQHRVSIHSSLKSKTKRRRLYKEADDNTKLRSSSSTTTTTTTMLLRISGNNLRPLRPQFLALRSSWLSTSPEQSTQPQMPPRVPNLIGGSFVESQSSSFIDVINPATQEVVSKVPLTTNEEFKAAVSAAKQAFPLWRNTPITTRQRVMLKFQELIRKNMDKLAMNITTEQGKTLKDSHGDIFRGLEVVEHACGMATLQMGEYLPNVSNGVDTYSIREPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAICDDEDIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFVGDAKSWEDKLVERAKALKVTCGSEPDADLGPVISKQAKERICRLIQSGVDDGAKLLLDGRDIVVPGYEKGNFIGPTILSGVTPDMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIPVPLPFFSFTGNKASFAGDLNFYGKAGVDFFTQIKTVTQQWKDIPTSVSLAMPTSQKQ
Protein: rRNA-processing protein fcf1 (O13610)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Essential protein involved in pre-rRNA processing and 40S ribosomal subunit assembly. Required for the early cleavage steps of 35S rRNA at the A(0), A(1), and A(2) sites (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- KRR1 small subunit processome component homolog
- Probable U3 small nucleolar RNA-associated protein 11
- Probable U3 small nucleolar RNA-associated protein 7
- rRNA-processing protein fcf2
- Uncharacterized protein C57A7.06
- Ribosome biogenesis protein bms1
- Uncharacterized WD repeat-containing protein C2E1P5.05
- Nucleolar protein 58
- Uncharacterized protein C3B8.09
- U3 small nucleolar RNA-associated protein 20
Sequence:
MGKAKTTRKFAQVKRVINLKDQRLQKKDQKKEKEKTTKNGELVREIPQMASNLFFQFNESLGPPYHVIIDTNFINFCLQQKIDLFEGLMTCLYAKTIPCISDCVMAELEKLGIRYRIALRIAKDERFERLPCTHKGTYADDCIVQRVMQHKCYLVATNDKNLKQRIRKIPGIPILSVANHKIRVERLVDVVD
Protein: Germin-like protein subfamily 3 member 3 (AtGER3) (AtGLP2) (P94072)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in plant defense. Probably has no oxalate oxidase activity even if the active site is conserved.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000250}.
Interaction partners:
- Calcium-dependent lipid-binding
- Altered inheritance of mitochondria protein
- Tryptophan RNA-binding attenuator protein-like protein
- At2g10940/F15K19.1
- Tryptophan RNA-binding attenuator protein-like protein
Sequence:
MKMIIQIFFIISLISTISFASVQDFCVADPKGPQSPSGYSCKNPDQVTENDFAFTGLGTAGNTSNIIKAAVTPAFAPAYAGINGLGVSLARLDLAGGGVIPLHTHPGASEVLVVIQGTICAGFISSANKVYLKTLNRGDSMVFPQGLLHFQLNSGKGPALAFVAFGSSSPGLQILPFALFANDLPSELVEATTFLSDAEVKKLKGVLGGTN
Protein: YY1-associated factor 2 (Q1JPU4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGDKRSPTRPKRQAKPSSDDGYWDRSVCTFKNTAEAFKCMMCDVRKGTSTRKPRPVSQLVSQQVTQQFASATLPKKEKKEKTEKDKNEREPTLKKNNHKKMRPRLKNVDRSSAQHLEVTVGDLTVIITDYKEKTKPSSSSSSSATSADHHSQSGSNSDNTEKGISRSSSPRGEVSSLNGESH
Protein: Caudal type homeobox 1 b (Caudal type homeodomain protein) (Cdx1b protein) (Homeobox protein CDX-1b) (A5PLE8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MYVSYLLDKDSSMYPNSVRHPSLNLNPQNFVPAPPQYPDFTGYHHVPGITTNDPHHSQTGSWNPAYPPPREEWTPYGPGSGVSSSSTGQLGFSPPEFSSVQTPGLLQSSINSSVGQLSPNAQRRNPYDWMRRSVPPASSGGKTRTKDKYRVVYTDHQRLELEKEFHYSRYITIRRKAELATALSLSERQVKIWFQNRRAKERKINKKKMQQPQPASTTTPTPPGSALPGNVPMVTSSSSGGLVSPPMPMSIKEEY
Protein: Monocopper oxidase-like protein SKS1 (Q8VXX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- Eukaryotic translation initiation factor 4C
- Small COPII coat GTPase SAR1A
- Eukaryotic translation initiation factor 4C
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Cytochrome P450, family 89, subfamily A, polypeptide 3
- Cytochrome P450 like protein
- Cytochrome P450, family 702, subfamily A, polypeptide 3
- Cytochrome P450, family 96, subfamily A, polypeptide 3
- S-formylglutathione hydrolase
- At1g78490
Sequence:
MAATCSLLASFLLCFALLSAVSFAADPFVSYDFRVSYLTASPLGVPQQVIAVNGQFPGPLLNATTNYNVVVNVFNHLDEPLLLTWPGIQMRRNSWQDGVLGTNCPIPPRWNFTYQFQVKDQIGSFFYSPSLNFQRASGGFGPIVINNRDIIPIPFPQPDGELIFIIGDWYTQDHKALRRALDSGKELGMPDGVLINGKGPYKYNSSVPDGIDYLTFHVEPGKTYRIRVHNVGISTSLNFRIQNHSLLLVETEGHYTSQANFTDFDVHVGQSYSFLVTMDQDATSDYYIVASARFVNETVWQRVTGVAILHYSNSKGPVSGPLPVPKTDVSSPWSAMSQPKTIRQNTSASGARPNPQGSFHYGQINITNTYILRSLPPTIINGALRATLNGISFVNPSTPVRLADRNKVKGAYKLDFPDRPFNRPLRLDRSMINATYKGFIQVVFQNNDTKIQSFHVDGYSFFVVGMDFGIWSEDKKGSYNNWDAISRSTIEVYPGGWTAVLISLDNVGVWNIRVENLDRWYLGEETYMRITNPEEDGKTEMDPPDNVLYCGALKNLQKEQHHSAATSILNGHLKLMLLMVLLASVFRFC
Protein: Allantoinase (EC 3.5.2.5) (Allantoin-utilizing enzyme) (P77671)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring.
Interaction partners:
- Allantoate amidohydrolase
- Aspartate carbamoyltransferase catalytic subunit
- Putative allantoin permease
- Carbamoyl phosphate synthase large chain
- Carbamoyl phosphate synthase small chain
- Glycerate 3-kinase
- Putative purine permease YbbY
- (S)-ureidoglycine aminohydrolase (UGHY) (UGlyAH)
- Ureidoglycolate lyase
- Ureidoglycolate dehydrogenase
Sequence:
MSFDLIIKNGTVILENEARVVDIAVKGGKIAAIGQDLGDAKEVMDASGLVVSPGMVDAHTHISEPGRSHWEGYETGTRAAAKGGITTMIEMPLNQLPATVDRASIELKFDAAKGKLTIDAAQLGGLVSYNIDRLHELDEVGVVGFKCFVATCGDRGIDNDFRDVNDWQFFKGAQKLGELGQPVLVHCENALICDELGEEAKREGRVTAHDYVASRPVFTEVEAIRRVLYLAKVAGCRLHVCHVSSPEGVEEVTRARQEGQDVTCESCPHYFVLDTDQFEEIGTLAKCSPPIRDLENQKGMWEKLFNGEIDCLVSDHSPCPPEMKAGNIMKAWGGIAGLQSCMDVMFDEAVQKRGMSLPMFGKLMATNAADIFGLQQKGRIAPGKDADFVFIQPNSSYVLTNDDLEYRHKVSPYVGRTIGARITKTILRGDVIYDIEQGFPVAPKGQFILKHQQ
Protein: OXPP cycle protein OpcA (O06813)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- 6-phosphogluconolactonase
- Glucose-6-phosphate 1-dehydrogenase 2
- Transaldolase
- Transketolase
- ATPase
- Aldo-keto reductase Rv2971
Sequence:
MIVDLPDTTTTAVNKKLDELREKIGAVAMGRVLTLIIAPDSEAMLEESIEAANDASHEHPSRIIVTMRGDPYADRPRLDAQLRVGADAGAGEFVVLRLSGPLAGHADSVVIPFLLPDIPVVAWWPDIAPAVPAQDALGKLAIRRITDATNAIDPLSAIKSRLAGYGAGDTDLAWSRITYWRALLTSAVDQPRHEPIESALVSGLKTEPALDVLAGWLASRIEGPVRRAVGELKVELVRNSETIVLSRPQEGITATLTRTGKPDALVPLARRVTGECLAEDLRRLDPDEIYCAALEGIKKVQYR
Protein: GPI-anchored wall transfer protein 1 (EC 2.3.-.-) (Q873N2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- N-acetylglucosaminylphosphatidylinositol deacetylase
- GPI mannosyltransferase 1
- Skn2p
- GPI ethanolamine phosphate transferase 1
Sequence:
MSSSLKQLKEQFVSDLTGGTIEEIYAVTSIALSSYLSFRLLKKSLGDLALIYDYILNVLTILASITVYSNSPSYLHYFIVIPSLVIYLVNYHVEKPSSPHRQNDTKEDKSDELLPRKQFITAYRSQMLIITNLAILAVDFPIFPRRFAKVETWGTSMMDLGVGSFVFSMGLANSRQLIKNHTDNYKFSWKSYLKTIKQNFIKSVPILVLGAIRFVSVKQLDYQEHETEYGIHWNFFFTLGFLPIVLGILDPVLNLVPRFIIGIGISIAYEVALNKTGLLKFILSSENRLESLITMNKEGIFSFIGYLCIFIIGQSFGSFVLTGYKTKNNLITISKIRISKKQHKKESSSFFSVATTQGLYLACIFYHLAFSLFISNLSFLQPISRRLANFPYVMWVVSYNATFLLCYDLIEKFIPGNLTSTVLDSINNNGLFIFLVSNLLTGFINMSINTLETSNKMAVIILIGYSLTWTLLALYLDKRKIYIKL
Protein: Cis-zeatin O-glucosyltransferase 2 (cisZOG2) (EC 2.4.1.215) (Q8RXA5)
Organism: Zea mays (Maize)
Function: Utilizes UDP-glucose as the sugar donor and catalyzes the formation of O-beta-D-glucosyl-cis-zeatin from cis-zeatin. May regulate active versus storage forms of cytokinins and could have an impact on seed growth.
Interaction partners:
- Oleosin Bn-V
Sequence:
MAVDTMESVAVVAVPFPAQGHLNQLLHLSLLLASRGLSVHYAAPPPHVRQARARVHGWDPRALGSIHFHDLDVPAYDSPAPDLAAPSPFPNHLMPMFEAFAAAARAPLAALLQRLSTSYRRVAVVFDRLNPFAATEAARLANADAFGLQCVAISYTVGWLDPGHRLLSDYGLQFLPPDDCMSREFVDLVFRMEEEEQGAPVAGLVMNTCRALEGEFLDAVAAQPPFQGQRFFAVGPLNPLLLDADARTAPRHECLEWLDRQPPESVLYVSFGTTSCLHADQVAELAAALKGSKQRFVWVLRDADRADIYAESGDSRHAKFLSEFTRETEGTGLVVTGWAPQLEILAHGATAAFMSHCGWNSIIESLSHGKPVLAWPMHSDQPWDSELLCNYFKAGLLVRPWEKHAEIIPAQAIQKVIEEAMLSDSGMAVRQRAKELGEAVRASVADGGNSRKDLDDFIGYITR
Protein: Olfactomedin-4 (OLM4) (Q3UZZ4)
Organism: Mus musculus (Mouse)
Function: May promote proliferation of pancreatic cancer cells by favoring the transition from the S to G2/M phase. In myeloid leukemic cell lines, inhibits cell growth and induces cell differentiation and apoptosis. May play a role in the inhibition of EIF4EBP1 phosphorylation/deactivation. Facilitates cell adhesion, most probably through interaction with cell surface lectins and cadherin (By similarity).
Subcellular location: Secreted, extracellular space {ECO:0000250}. Mitochondrion {ECO:0000250}.
Interaction partners:
- Leucine-rich repeat-containing G-protein coupled receptor 5
- Achaete-scute homolog 2
- Chromogranin-A
- Leucine-rich repeats and immunoglobulin-like domains protein 1
- Villin-1
Sequence:
MSYSLLFLLALQFCLGSASRTTLTSAHSRELTTPPTSPQATAAWLPPGGTSWAEGGTVSQPLSNFTGSVDSHGTCQCSVSLPDTAFPADRVERLEYTAHILSQKFEREFSKVKEYVQLISVYEKRLLNLTVRVEVMEKDSISYTELDFELIKLEVKEMQKLVLQLKKNFVGSTHIIDMLEVEIRNMTLLVEKLESLDQNNVLSIRRQILALKTKLKECEASKSDLVPATPPPPAPGSCSHGGVVNISAPSVIQLNWLGFSYKYGAWGRDYSPQHPERTLYWVAPLNTDARALEYYRLYDSLDNLLIYSHFRDYRIRYGQGGGTVAFNNNLYVNWYNGGNIAKINLTTNVVDVNRPLPLAAYNNRFSYANVNWQDIDLAVDEQALWAIYATEASTGNIVISKLNDTTLEVISTWVTKQYKPSVSNAFMVCGVLYATRTLNTKTEEIFYYYDTNTEREGNLGITMRKMQERIQSINYHPFDQKLYVYNDGYLLNYDLVFLQTPRQPV
Protein: Melanocyte-inducing transcription factor b (Microphthalmia-associated transcription factor b) (F1Q885)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Tyrosinase.
- Melanocyte-stimulating hormone receptor
- Mitogen-activated protein kinase
- Melanocyte inducing transcription factor a isoform 1
- Mitogen-activated protein kinase
- Transcription factor EB
- Dopachrome tautomerase.
- Sodium/potassium/calcium exchanger 5
Sequence:
MQSESGIVPDFEVGDDFHEEPKTYYELKSQPLQNSNPSEQQHGSCKPPLGSSRVLLRQQLMREQLQQQERREQQKRQISITHSPAINVSHPCGPPSAAQVPMEVLKVQTHLENPTKYHIQQAQRQQVKAYLSTTLGGKQAVSLPCPSQASDHGGMPPGPGNSAPNSPMALLTLNPNCEKEMDDVIDDIIGLESSYSDDIMGLSLDPGLQMANTIPVSANLLDMYSNPGLPPPGISISNSCPANMTSVKREFSVTPSPALMHMMDKPSSCSKFESYQRPEGFPVEVEVRALAKERQKKDNHNLIERRRRFNINDRIKELGTLIPKSNDPDMRWNKGTILKASVDYIRKLQREQHRTKELENRQKKLEHTNRNLLLRIQELEIQARAHGLAMASSALCASELAARAIKQEPLLGDCSQDMYTSTHAHPSCADMSRSSTLDLNNGTISFSDTHLSDTHAAKLDDILMDETLTSGATNESLISAASNESTHKDSMNMEENQHAC
Protein: AsmA family protein YhjG (P37645)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- AsmA family protein YicH
- Probable phospholipid transport protein YdbH
- Protein AsmA
- Cyclic di-GMP phosphodiesterase PdeH
- Translocation and assembly module subunit TamB
- Intermembrane phospholipid transporter YhdP
- Stationary phase-inducible protein CsiE
Sequence:
MSKAGKITAAISGAFLLLIVVAIILIATFDWNRLKPTINQKVSAELNRPFAIRGDLGVVWERQKQETGWRSWVPWPHVHAEDIILGNPPDIPEVTMVHLPRVEATLAPLALLTKTVWLPWIKLEKPDARLIRLSEKNNNWTFNLANDDNKDANAKPSAWSFRLDNILFDQGRIAIDDKVSKADLEIFVDPLGKPLPFSEVTGSKGKADKEKVGDYVFGLKAQGRYNGEPLTGTGKIGGMLALRGEGTPFPVQADFRSGNTRVAFDGVVNDPMKMGGVDLRLKFSGDSLGDLYELTGVLLPDTPPFETDGRLVAKIDTEKSSVFDYRGFNGRIGDSDIHGSLVYTTGKPRPKLEGDVESRQLRLADLGPLIGVDSGKGAEKSKRSEQKKGEKSVQPAGKVLPYDRFETDKWDVMDADVRFKGRRIEHGSSLPISDLSTHIILKNADLRLQPLKFGMAGGSIAANIHLEGDKKPMQGRADIQARRLKLKELMPDVELMQKTLGEMNGDAELRGSGNSVAALLGNSNGNLKLLMNDGLVSRNLMEIVGLNVGNYIVGAIFGDDEVRVNCAAANLNIANGVARPQIFAFDTENALINVTGTASFASEQLDLTIDPESKGIRIITLRSPLYVRGTFKNPQAGVKAGPLIARGAVAAALATLVTPAAALLALISPSEGEANQCRTILSQMKK
Protein: Succinate-CoA ligase subunit beta (EC 6.2.1.-) (Q68FT4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
SAVAIAAQAGKLLRERSLRPRLLAVRSQAGHLTPRRWLNLQEYQSKKLMSEHGVRVQRFFVASTAKEAQEAAKRLNAKEIVLKAQILAGGRGKGVFDSGLKGGVHLTKDPKVVGQLAQQMIGYNLATKQTPKEGVKVNKVMVAEALDISRETYLAILMDRSHNGPVLVGSPQGGVDIEEVAASSPELIFKEQIDIFEGIKDSQAQRMAENLGFLGSLKNQAADQIKKLYHLFLKIDATQVEVNPFGETPEGQVVCFDAKINFDDNAEFRQKDIFAMDDKSENEPIENEAARYDLKYIGLDGNIACFVNGAGLAMATCDIIFLNGGKPANFLDLGGGVKESQVYQAFKLLTSDPKVEAILVNIFGGIVNCAIIANGITKACQELELKVPLVVRLEGTNVQEAQNILKSSGLPITSAVDLEDAAKKAVASVAKK
Protein: Jen2p (A0A1D8PLY7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Isocitrate lyase
Sequence:
MTAADTHSITSADVQEHNRHIIRPPKFTWPAIRKYAITRVTSLWVGWDELKQYSWHEVLNPFEPLVEMNLHQWNFFFLGFWAWTWDALDFFVTSLNVSNIAEDLDSTVKDVSWGITLVLMLRTVGALIFGAIGDTYGRKWPYIINLSCLMVIQIGTGFVTTFQQFLGLRALFGVAMGGLFGICAAEALGDAPKKARGVLSGIFQEGYAFGYLLAVVFQRAIADTTEKTWRSVFWFSAGPPIILIIWRFINPETDSYQRQKERFDQGAVQKNSKAAEFKSQAKKALNQYWLIIVYLIFLMAGFNFSSHGSQDLYPTMLTKQYHYGKDKSTVVNVCANLGALAGGIVIAHLSTFIGRRTAILIGNVIAGIMIYFWAFHPMWITAFFMQFGIQGSWSVVPIHLSELSPPHFRSFVSGVSYQLGNLVSSASSTIEATIEEQIHDYGKTMAIFIGAVLAYLMFVVFIGPENRGAELGVERDDEYSAYDSDREDRGDSDLEEGNITQKTLEKPEVEHKE
Protein: Flavo-diiron protein FprA2 (FDP 2) (Flavoprotein A2) (H(2)O-forming NADH oxidase) (EC 1.6.3.4) (NADH oxidase) (NADH:O(2) oxidoreductase) (Q97GC0)
Organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
Function: Catalyzes the four-electron reduction of molecular oxygen to water. In fact, functions as the terminal component of an NADH oxidase (NADH:O(2) oxidoreductase) when using NADH:rubredoxin oxidoreductase (NROR) and rubredoxin (Rd) as electron transport intermediaries between NADH and FDP. Is thus able to reductively scavenge intracellular dioxygen and is part of an oxidative stress defense system in C.acetobutylicum, an obligate anaerobic bacterium. Can also serve as the terminal component of an NADH:nitric oxide oxidoreductase (NOR) with a catalytic efficiency comparable to that of its NADH oxidase activity, and therefore might have an in vivo role in scavenging nitric oxide.
Interaction partners:
- NADH-rubredoxin oxidoreductase
- Desulfoferrodoxin
- Rubredoxin
- Reverse rubrerythrin-2
- Reverse rubrerythrin-1
Sequence:
MPAIKIKDNIFSVGVLNPSLRIFDIIMKTEYGTSYNAYLIKGKKNVLIDTVHGRFFDEYLENIKSVIDPSSIDYVIMNHCEPDHSGSLARLYEVAPQIKVIASNAGKIYLKNITNKETLDVKAVKTNDTLDIGNGKVLKFAIAPFLHWPDSMFTILEEDKIAFTCDFLGCHFCEPRMFDTKITYMPKYEKSFKEYYDAIFSPFKPYVVKGLDILDALDLDFIATSHGPILTREGLLAASKQKYRDLSSEIQSTTKYIPIFYCSAYGNTEILANEIASGIKSVLNDANIEMLDIINYDYSDLKEKINICDAFMLGTPTINKDALFPIWELIGGIDAVNCKNKPASAFGSFGWSGEAIPFVISRLKELKLKVFQDGFTCLFVPSEDDIKKAFKFGEDFAKSI