wanglab/gogpt-training-data huggingface dataset:
Protein: Baccatin III:3-amino-3-phenylpropanoyltransferase (EC 2.3.1.-) (Q8H2B5)
Organism: Taxus cuspidata (Japanese yew)
Function: Acyltransferase involved in taxol biosynthesis. Catalyzes the selective 13-O-acylation of baccatin III with (3R)-3-amino-3-phenylpropanoyl-CoA as the acyl donor to form 3'-N-debenzoyl-2'-deoxytaxol.
Interaction partners:
Sequence:
MKKTGSFAEFHVNMIERVMVRPCLPSPKTILPLSAIDNMARAFSNVLLVYAANMDRVSADPAKVIREALSKVLVYYYPFAGRLRNKENGELEVECTGQGVLFLEAMADSDLSVLTDLDNYNPSFQQLIFSLPQDTDIEDLHLLIVQVTRFTCGGFVVGANVYGSACDAKGFGQFLQSMAEMARGEVKPSIEPIWNRELVKLEHCMPFRMSHLQIIHAPVIEEKFVQTSLVINFEIINHIRRRIMEERKESLSSFEIVAALVWLAKIKAFQIPHSENVKLLFAMDLRRSFNPPLPHGYYGNAFGIACAMDNVHDLLSGSLLRTIMIIKKSKFSLHKELNSKTVMSSSVVDVNTKFEDVVSISDWRHSIYYEVDFGWGDAMNVSTMLQQQEHEKSLPTYFSFLQSTKNMPDGIKMLMFMPPSKLKKFKIEIEAMIKKYVTKVCPSKL
Protein: G1/S-specific cyclin-D2 (P30279)
Organism: Homo sapiens (Human)
Function: Regulatory component of the cyclin D2-CDK4 (DC) complex that phosphorylates and inhibits members of the retinoblastoma (RB) protein family including RB1 and regulates the cell-cycle during G(1)/S transition. Phosphorylation of RB1 allows dissociation of the transcription factor E2F from the RB/E2F complex and the subsequent transcription of E2F target genes which are responsible for the progression through the G(1) phase. Hypophosphorylates RB1 in early G(1) phase. Cyclin D-CDK4 complexes are major integrators of various mitogenenic and antimitogenic signals.
Subcellular location: Nucleus {ECO:0000269|PubMed:18827403}. Cytoplasm {ECO:0000269|PubMed:18827403}. Nucleus membrane {ECO:0000269|PubMed:18827403}. Note=Cyclin D-CDK4 complexes accumulate at the nuclear membrane and are then translocated into the nucleus through interaction with KIP/CIP family members. {ECO:0000269|PubMed:18827403}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:17873913}.
Interaction partners:
- Cyclin-dependent kinase 4
- Cyclin-dependent kinase 6
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase inhibitor 1B
- Cyclin-dependent kinase 2
- Cyclin-dependent kinase inhibitor 1C
- Retinoblastoma-like protein 2
- Cyclin-dependent kinase inhibitor 2A
- Retinoblastoma-associated protein
- Proliferating cell nuclear antigen
Sequence:
MELLCHEVDPVRRAVRDRNLLRDDRVLQNLLTIEERYLPQCSYFKCVQKDIQPYMRRMVATWMLEVCEEQKCEEEVFPLAMNYLDRFLAGVPTPKSHLQLLGAVCMFLASKLKETSPLTAEKLCIYTDNSIKPQELLEWELVVLGKLKWNLAAVTPHDFIEHILRKLPQQREKLSLIRKHAQTFIALCATDFKFAMYPPSMIATGSVGAAICGLQQDEEVSSLTCDALTELLAKITNTDVDCLKACQEQIEAVLLNSLQQYRQDQRDGSKSEDELDQASTPTDVRDIDL
Protein: SD03282p (Q8T9F5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHAASLTTVEGLLQEFYQPSTSNARKREIETNLLAFKSQPEAWQLCLRVATSSDTTENQFLWFFSTSTLEHTITRRWTQLTSTDKTLLRETLWNSYAQLGATPNVAKRHRDTLAQLIALLGKREFPEQDPNYMQHCMELTKTRFQLGINLLKITSEEVVSNRGDLTTEWKQYFYSCISMCVPDVLDLVTKYLLIAVCHINGKDIQTTIPNTLMDFSLTSALPNDNQLSSSILDLLGCVQHLVSWIRTELISEYFLMSILDLSQWRPAHEPISLAALSVLNELLYLQKPLPFPGPLMGGVTSLLEQHNNNRRQSEMYSDKFRELLRLYTTKYAAKLMQEPDLLETFLNLLYSCTTELHGALDFTEKLEIWTPIIKGIAQHPAKITRYNNVLTQLVDEIMRRTQFEANKPELEVLDNELMEDDTSATEWQQFLDQCFESLALLANTRGAHIVFAQVYNHWSRPQMYLLSLEHALDHGSARSYEAARKLKGANVGEILRDFATVCQAVVRLAPLMDSSTAAPGVADEMECQLQMLSDSLLQTLQLLASNRLYSGGSEMDKATFQTDLDNLYAQVLLAMRSIFPLTKAMSGEELLHRLFAILGSIFACNGSLTAASPIVQQAASELLLFISTVIRPKCLLDIPQIQSLLQAGSRLGAQLPRQVCINVHISLVSYMVLPWKSVPEQQQEYPRRLWMLREYVQGLAQNFLDLDLGQANESKVAATTLSLLGTFTALIEYFKATGGNAKDMLASTFKPILTKALMIFNNFGQSSIAMAITVAEFSLSMLRTLPTHLGAQFIKEMITLFISVSSREQLTLSRLAVMEKILQMFKLIVEQPGSASLGLLPSILDFSTQQILPLLQQQNAATDNSEITSLLYALFDSVLTCKWQFFYKNQLSNGHSGGGSGNFNCSDNLHPAHFMAILNAYGQMLVSGTDPSNVRSVLFSMQNVNERSRLYQRALFKEQLLASFQRALLNLLLSGEGSLHFDMIAQALYAMGQVDRRQLLESFVHASLPVAQTSLEEICQTNDIPTFTQKLTQLMQDAHCVHLNETA
Protein: rRNA-processing protein (A0A1D8PGP2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- RNA cytidine acetyltransferase
- SnoRNA-binding rRNA-processing protein
- U3 small nucleolar ribonucleoprotein protein IMP4
- Nucleolar protein 56
- SnoRNA-binding rRNA-processing protein
- Nan1p
- Nucleolar protein 58
- Utp20p
- Ribosome biosynthesis protein
- Utp13p
Sequence:
MTETVIEKKRKVDLNASGITKQPKASKIFSPFRVLGNVTDSTPFAMGTLGSTFYAVTSVGRSFQIYDLATLHLLFVSQTQTPSRITSLAAHHHYVYASYGDRIGIFRRGRLEHELVCEGNSTVNQLLVFGEYLIATTLEGDIFVFRKTEGKKFPTELYTTIRIINSLVEGEIVGLIHPPTYLNKVIVATTQSVFVINVRTGKLLYKSRELQFEGEKISSIEAAPVLDVIAVGTSNGNVFLFNIKKGKVLGQKIITSGTESSSKVASISFRTDGAPHLVAGLNNGDLYFYDLDKKSRVHVLRNAHKETHGGVANAKFLNGQPIVLSNGGDNHLKEFVFDPNLTTSNSSIVPPPRHLRSRGGHSAPPVAIEFPQEDKTHFLLSASRDKTFWTFSLRKDAQAQEMSQRLQKSKDGKRQAGQVVSMREKFPEIISISSSYAREGDWENIITAHKDETFARTWDSRNKRVGRHLLNTIDGGIVKSVCVSQCGNFGLVGSSSGGIGSYNLQSGLLRKKYVLHKQAVTGLAIDGMNRKMVSCGLDGIVGFYDFGKSVYLGKLQLEAPITSMIYHKSSDLVACALDDLSIVVIDVTTQKVIRILYGHTNRISGMDFSPDGRWIVSVALDSTLRTWDLPTGGCIDGVILPIVATAVKFSPIGDILATTHVSGNGVSLWTNRAQFKPVSTRHVEEDEFSTILLPNASGDGGSTMLDGFLDEDSNEDGTIDEQYTSAAQIDASLITLSSEPRSKFNTLLHLDTIKQQSKPKEAPKKPENAPFFLQLTGQAVGDRASVAEGKTSEQTNNTVEETNSKLRKLDTNGNHAFESEFTKLLREAGESGQFERFLTYLLNLSPAVLDLEIRSLNSFVPLTEMTNFIQALNAGLKSNANYEIWETLYAMFFNIHGDVIHQFENETSLHEALEEYRQLNDEKNNKMDSLVKYCASIVSFIS
Protein: Protein SHI RELATED SEQUENCE 5 (Q9LQZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that binds DNA on 5'-ACTCTAC-3' and promotes auxin homeostasis-regulating gene expression (e.g. YUC genes), as well as genes affecting stamen development, cell expansion and timing of flowering. Synergistically with other SHI-related proteins, regulates gynoecium, stamen and leaf development in a dose-dependent manner, controlling apical-basal patterning. Promotes style and stigma formation, and influences vascular development during gynoecium development. May also have a role in the formation and/or maintenance of the shoot apical meristem (SAM).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Electron carrier/iron ion-binding protein
- Probable U3 small nucleolar RNA-associated protein 11
Sequence:
MAGFFYLGGRDNNSNNNKQDHHQVDKDHHHQDKSNYLYLYKDEIYNNNKGFEIWPPQYFQQQEHQQQQQQQQHASAPANFYSFGMVPSGSSSNNNNNRSRSLYFNVVSDHEPGGFTVTRQGGMNCQDCGNQAKKDCPHMRCRTCCKSRGFHCQTHVKSTWVPAAKRRERLAQLASLQHHSASSRETQNAKRLREASGGDNNDDKDHSGGGGSALANTRVVNANSNSGLEVSQHLPPEVNSPAIFRCVRVSSIEEDEDDQAYAYQTAVNIGGHIFKGILYDQGPEHQDNHHLNLLASTATTTNVEETATKTVTGNNNNGLMLDPSSLYPAQLNSFIAGTPFFTPPRS
Protein: Cell surface A33 antigen (Glycoprotein A33) (mA33) (Q9JKA5)
Organism: Mus musculus (Mouse)
Function: May play a role in cell-cell recognition and signaling.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MLGKAGSVVWMLCAIWVAADALTVETTQDILRAARGRSVTLPCTYNTYVSDREGFIQWDKLLRSQTERVVTWNFVTKKYIYGNRYENRVRVSNDAELSNASITIDQLTMDDNGTYECSVSLMSDQDVNAKSRVRLLVLVPPSKPDCSIQGEMVIGNNIQLTCHSAEGSPSPQYSWKSYNAQNQQRPLTQPVSGEPLLLKNISTETAGYYICTSSNDVGIESCNITVAPRPPSMNIALYAGIAGGVFVALIIIGVIVYCCCCREKDDKDQDREDARPNRAAYQVPKKEQKEISRGREDEDDHRHEDRWSSGRSTPDQPFQ
Protein: Protein bag of marbles (P22745)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required to initiate both male and female gametogenesis. May regulate cystoblast cell divisions.
Interaction partners:
- Meiotic P26, isoform F
- Deubiquitinase otu
- Protein benign gonial cell neoplasm
- Protein decapentaplegic
- poly
- Protein tumorous testis
- receptor protein serine/threonine kinase
- G2/mitotic-specific cyclin-A
- CCR4-NOT transcription complex subunit 9
- Protein sex-lethal
Sequence:
MLNARDVCPEGNDDQQLDHNFKQMEEHLALMVEGNENEDPRKATCEYEDTNEDGATCTSGVLSEIQENFGRLRLCDVTAPLLEFHGLDCLQQIQKRSRHFAFDGSPAKKSRSGGVLVTGPKQKQLQKENVWNRKSKGSASADNIEKLPITIEKLHMIGLHGDCLEHNAVLRLMNLFRSLHDHLTADLGFSRQNSMPSDYLFDMPVKSTMPKSLNVRYQLQVLCTKVERFLVQQRRTLEANRHFDFEKYDECDKLLKGFASYLDNFKLLLKPKMRNRNGNSGSNADKFHTQRMERLLIGLRDWIKAAHLSVHVFNWEMDLEHRYSGAMTESHKSLNERAILLSGAELRAAEARGISAEDLFIAQRYKLGGPIYCVLEQHEFLSALIANPETYFPPSVVAICGPQKLGAVSMEQPSASEEEFEETEEVPSSPPRHTGRVPRFRS
Protein: Cytochrome P450 705A5 (EC 1.14.-.-) (Thalian-diol desaturase) (AtTHAD) (Q9FI39)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts thalian-diol to a desaturated thalian-diol.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Thalianol synthase 1
- Marneral synthase
- UDP-glycosyltransferase 79B4
- Cysteine-rich repeat secretory protein 58
- Cytochrome P450 708A2
- BAHD acyltransferase At5g47980
- Baruol synthase
- Lupeol synthase 1
Sequence:
MASMITVDFENCFIFLLLCLFSRLSYDLFFRKTKDSRAGCALPPSPPSLPIIGHLHLILFVPIHQSFKNISSKYGPLLHLRFFNFPIVLVSSASTAYEIFKAQDVNVSSRPPPPIEESLILGSSSFINTPYGDYSKFMKKFMVQKLLGPQALQRSRNIRADELERFYKTLLDKAMKKQTVEIRNEAMKLTNNTICKMIMGRSCSEENGEAETVRGLVTESIFLTKKHFLGAMFHKPLKKLGISLFAKELMNVSNRFDELLEKILVEHEEKLQEHHQTSDMLDMLLEAYGDENAEYKITRDQIKSLFVDLFSAGTEASANTIQWTMAEIIKNPKICERLREEIDSVVGKTRLVQETDLPNLPYLQAIVKEGLRLHPPGPVVRTFKETCEIKGFYIPEKTRLFVNVYAIMRDPDFWEDPEEFKPERFLASSRLGEEDEKREDMLKYIPFGSGRRACPGSHLAYTVVGSVIGMMVQHFDWIIKGEKINMKEGGTMTLTMAHPLKCTPVPRNLNT
Protein: Mite allergen Der p 21.0101 (Allergen Der p 21) (allergen Der p 21.0101) (Q2L7C5)
Organism: Dermatophagoides pteronyssinus (European house dust mite)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18445190}. Endoplasmic reticulum {ECO:0000269|PubMed:18445190}. Vesicle {ECO:0000269|PubMed:18445190}. Secreted {ECO:0000269|PubMed:18445190}. Note=Associated with cytoplasmic matrix, detached cytoplasmic material and with electron-dense droplets, which presumably represent transport vesicles. {ECO:0000269|PubMed:18445190}.
Interaction partners:
Sequence:
MKFIITLFAAIVMAAAVSGFIVGDKKEDEWRMAFDRLMMEELETKIDQVEKGLLHLSEQYKELEKTKSKELKEQILRELTIGENFMKGALKFFEMEAKRTDLNMFERYNYEFALESIKLLIKKLDELAKKVKAVNPDEYY
Protein: Endoplasmic reticulum aminopeptidase 1 (EC 3.4.11.-) (ARTS-1) (Adipocyte-derived leucine aminopeptidase) (A-LAP) (Aminopeptidase PILS) (Puromycin-insensitive leucyl-specific aminopeptidase) (PILS-AP) (Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator) (Q9NZ08)
Organism: Homo sapiens (Human)
Function: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play a role in the inactivation of peptide hormones. May be involved in the regulation of blood pressure through the inactivation of angiotensin II and/or the generation of bradykinin in the kidney.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:15908954}; Single-pass type II membrane protein {ECO:0000305|PubMed:15908954}.
Interaction partners:
- Nucleobindin-2
- HLA class I histocompatibility antigen, C alpha chain
- HLA class I histocompatibility antigen, B alpha chain
- Tripeptidyl-peptidase 2
- Tapasin
- Interleukin-23 receptor
- Anthrax toxin receptor 2
- Tumor necrosis factor
Sequence:
MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAMENWGLTTYRESALLFDAEKSSASSKLGITMTVAHELAHQWFGNLVTMEWWNDLWLNEGFAKFMEFVSVSVTHPELKVGDYFFGKCFDAMEVDALNSSHPVSTPVENPAQIREMFDDVSYDKGACILNMLREYLSADAFKSGIVQYLQKHSYKNTKNEDLWDSMASICPTDGVKGMDGFCSRSQHSSSSSHWHQEGVDVKTMMNTWTLQKGFPLITITVRGRNVHMKQEHYMKGSDGAPDTGYLWHVPLTFITSKSDMVHRFLLKTKTDVLILPEEVEWIKFNVGMNGYYIVHYEDDGWDSLTGLLKGTHTAVSSNDRASLINNAFQLVSIGKLSIEKALDLSLYLKHETEIMPVFQGLNELIPMYKLMEKRDMNEVETQFKAFLIRLLRDLIDKQTWTDEGSVSERMLRSQLLLLACVHNYQPCVQRAEGYFRKWKESNGNLSLPVDVTLAVFAVGAQSTEGWDFLYSKYQFSLSSTEKSQIEFALCRTQNKEKLQWLLDESFKGDKIKTQEFPQILTLIGRNPVGYPLAWQFLRKNWNKLVQKFELGSSSIAHMVMGTTNQFSTRTRLEEVKGFFSSLKENGSQLRCVQQTIETIEENIGWMDKNFDKIRVWLQSEKLERM
Protein: Dixin (Coiled-coil protein DIX1) (Coiled-coil-DIX1) (DIX domain-containing protein 1) (Q155Q3)
Organism: Homo sapiens (Human)
Function: Positive effector of the Wnt signaling pathway; activates WNT3A signaling via DVL2. Regulates JNK activation by AXIN1 and DVL2.
Subcellular location: Cell junction, focal adhesion {ECO:0000269|PubMed:16814745}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:16814745}. Cytoplasm {ECO:0000269|PubMed:20085589}. Note=Colocalizes with gamma-tubulin at the centrosome, both during interphase and mitosis (PubMed:19375513). Associated with actin stress fiber at the filament ends (PubMed:16814745). {ECO:0000269|PubMed:16814745, ECO:0000269|PubMed:19375513}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:16814745}. Note=Not associated with stress fibers. {ECO:0000269|PubMed:16814745}.
Interaction partners:
- Disrupted in schizophrenia 1 protein
- Axin-1
- Nuclear distribution protein nudE-like 1
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Segment polarity protein dishevelled homolog DVL-1
- Mitogen-activated protein kinase kinase kinase 4
Sequence:
MLACLTRGNLLDVLQEGFNEQQLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQTSAKDIVDGNLKSIMRLVLALAAHFKPGSSRTVNQGRDSRAPLQSHRPHCATAVAQGAAAALADVCHDMSRSGRDVFRYRQRNSSMDEEIENPYWSVRALVQQYEGQQRSPSESSCSSLTSPSPIHSAKSESIITQSEEKADFVIIPAEGIENRTEGTDSPLSRDWRPGSPGTYLETSWEEQLLEQQEYLEKEMEEAKKMISGLQALLLNGSLPEDEQERPLALCEPGVNPEEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEALRKLSDVSYHQVDLERELEHKDVLLAHCMKREADEATNYNSHNSQSNGFLLPTAGKGATSVSNRGTSDLQLVRDALRSLRNSFSGHDPQHHTIDSLEQGISSLMERLHVMETQKKQERKVRVKSPRTQVGSEYRESWPPNSKLPHSQSSPTVSSTCTKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWVEEDHGEN
Protein: Insulin-1 [Cleaved into: Insulin-1 B chain; Insulin-1 A chain] (P01325)
Organism: Mus musculus (Mouse)
Function: Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Subcellular location: Secreted.
Interaction partners:
- Insulin-like growth factor 1 receptor
- Insulin receptor
- Insulin-like growth factor 1
- Insulin receptor substrate 1
- Insulin-2
- Insulin receptor substrate 2
- Pro-epidermal growth factor
- Cation-independent mannose-6-phosphate receptor
- Albumin
- Epidermal growth factor receptor
Sequence:
MALLVHFLPLLALLALWEPKPTQAFVKQHLCGPHLVEALYLVCGERGFFYTPKSRREVEDPQVEQLELGGSPGDLQTLALEVARQKRGIVDQCCTSICSLYQLENYCN
Protein: Putative peptidoglycan bound protein (LPXTG motif) (Q8Y783)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004168}; Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00004168}.
Interaction partners:
- Putative secreted protein
- Lmo1290 protein
- Lmo0610 protein
- Lmo1036 protein
Sequence:
MKHAKKSLFTFIIFMTILSITFNPFSAKAAPLMLNLPAPQVDQLYIGDDYITGKLQQEVPMHYPGNAAYVLFNNKQYNITDYTVENDVNFRLKLPKTLEAGDTLNYFTITGNVLDPVAYPGQESYKLAGPFSPIEKANIQVNYVDETNQTLATSDTLSGKLGETYTTSPKAIDGYQVKETPTNATGTYTTNTETIQINYVYEKTAVEGANVSVEYINEATNESIAPTETLSGKIGTTFQAEVKEIDGYELSQVPSNQSGTYTDQTQSVIFKYKKITTPDEVAKDVTVTYKDTKGNQLADPVILKGDIGSTFETEAKSFKGYKLTKTPSNHSSVFTSDSQEVEYVYSKDDAVITPPVTPVNPDKPIINPVKPVNPATSTVPNKNISKKNTTKTVNQTGKTSTALQLPKTGDSENNLPLIIGVSLLISGVYIFTTRRKRVK
Protein: Homeobox protein Hox-D9 (Homeobox protein Hox-4.4) (Homeobox protein Hox-5.2) (P28357)
Organism: Mus musculus (Mouse)
Function: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular location: Nucleus.
Interaction partners:
- Homeobox protein Hox-D10
- Homeobox protein Hox-D8
- Homeobox protein Hox-D3
Sequence:
MSSSGTLSNYYVDSLIGHEGDEVFAARFGPPGPGTQGRPAGVADGPAAATAEFASCSFAPKSSVFSASWSAVAAQPPAAATMSGLYHPYVSPPPLAAAEPGRYVRSWMEPLPGFPGGAGGGGGSGGGGGGGPGPVPSPGGPANGRHYGIKPETGAAPAPAAASTSSSSSTSSSSSSKRTECSAARESQGSGGPEFPCNSFLRDKAAAATGNGPGVGIGTGPGAVGSSEPSACSDHPSPGCSLKEEEKQPPQPPQQQLDPNNPAANWIHARSTRKKRCPYTKYQTLELEKEFLFNMYLTRDRRYEVARILNLTERQVKIWFQNRRMKMKKMSKEKCPKGD
Protein: Candida glabrata strain CBS138 chromosome D complete sequence (Q6FWG3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MVNLAVHRSAHRAAKKYTHPDTYPNAKQLKRSTEVLLFSVCILFLFTTFITFIVATAGSTANYSPIHNIYIGDADIKHINVTKVLPQIAPILTVLGTALSAPNSSLSEVFNSLKAIADTPALTPLLNLLKNAKNTSDSVVALTELAPLAISSDSSSSTKELIAISGLLSFSNNTNQTLESLGNLVMPTLAQLKSGQPSDNSTSIVLSILQGSDNKVASVDSLITLNNMTLAEKTKLLPVFQLFGYTTNINNTVDALGDLMNANVPTQLGVTLLTTIQSSLNGEADQDLSPLFDRIGGSVPEDNKQSVEAVEALLNDSSNKNGTINNLLSLLRQNVTTSPSAKAAFQAMSTLLDHSNNQTMVLQSLPILAAVRNTTLAQAQLEGLQGMLQVSTNPVQTLGIIAALQAGMADPNTNTDAVPALFNLLSASDNPANSFTSLVALTSWATSNPDTFRPIVSILEDANSVEPVTQEQLKAMTPALLDFLHVPVDFRLSIFTLCHVNGQGEITDCNSPHAVQNLDFRSIIYDALLDSDFQPYLKALNISKYDLYLEGKLLHRQHEYVPAVKAVLAMNILTIITSFFGIIGFILLIAPKYNRKLGLWIYTVVLTLSTALFSCLGAGIIAIMISIIKSGTSHDKFNVVFSTGGAYSGCVWAGFAVAFFACLIVLYCAFYARVGKPRGQPFGDEKGYDNDMSSMSNSSENNNYESEKVVQTVDVADVDEDDSSSPEQVNKQQPKDTDIIV
Protein: Phosphatidate cytidylyltransferase, photoreceptor-specific (EC 2.7.7.41) (CDP-DAG synthase) (CDP-DG synthase) (CDP-diacylglycerol synthase) (CDS) (CDP-diglyceride pyrophosphorylase) (CDP-diglyceride synthase) (CTP:phosphatidate cytidylyltransferase) (P56079)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an important precursor for the synthesis of phosphatidylinositol (PtdIns) and phosphatidylglycerol (PG). Required for the regeneration of the signaling molecule phosphatidylinositol 4,5-bisphosphate (PtdInsP2) from PA and maintenance of its steady supply during signaling thus playing an essential role during phospholipase C-mediated transduction. In the salivary glands and possibly other adipose tissues, function is essential for regulating cell growth and neutral lipid storage by coordinating PtdIns metabolism and insulin pathway activity. Acts by positively regulating activity of the insulin pathway through synthesis of PtdIns, and in turn the insulin pathway up-regulates the synthesis of CdsA. This CdsA-insulin positive feedback loop may be one of the mechanisms for coordinating cell growth and fat storage; switching to fat storage when cells reach homeostasis or converting from growth to fat storage under nutrient-poor conditions. Required for spermatid individualization by regulating lipid compositions and lipid-mediated signaling during spermatogenesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26791243}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- phosphatidate phosphatase
- Diacylglycerol kinase
- Probable cardiolipin synthase
- Diacylglycerol kinase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Eye-specific diacylglycerol kinase
- Phospholipase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Diacylglycerol kinase 1
Sequence:
MAEVRRRKGEDEPLEDTAISGSDAANKRNSAADSSDHVDSEEEKIPEEKFVDELAKNLPQGTDKTPEILDSALKDLPDRWKNWVIRGIFTWIMICGFALIIYGGPLALMITTLLVQVKCFQEIISIGYQVYRIHGLPWFRSLSWYFLLTSNYFFYGENLVDYFGVVINRVEYLKFLVTYHRFLSFALYIIGFVWFVLSLVKKYYIKQFSLFAWTHVSLLIVVTQSYLIIQNIFEGLIWFIVPVSMIVCNDVMAYVFGFFFGRTPLIKLSPKKTWEGFIGGGFATVLFGILFSYVLCNYQYFICPIQYSEEQGRMTMSCVPSYLFTPQEYSLKLFGIGKTLNLYPFIWHSISLSLFSSIIGPFGGFFASGFKRAFKIKDFGDMIPGHGGIMDRFDCQFLMATFVNVYISSFIRTPSPAKLLTQIYNLKPDQQYQIYQSLKDNLGDMLT
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FUW4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Cysteine desulfurase, mitochondrial
- ferroxidase
- Candida glabrata strain CBS138 chromosome K complete sequence
Sequence:
MEIFSYNYKKKYHTRNILFEPNMNWKIALFCWTFFLQALNAQNLGAMQSDKYFPKSKDPTSFPMGCSPQVLKTQPGLAVKLYSYGHPVPGCAYNTYQYPDFPRSGYKKERKLADITGVNGRIDIDLKPNDPCRVLSGNLPSNYNYQNTLTYTNFTMILYGYFQPKVTGYHTFNLEADDLLFMNLGAGNAFDCCRAESTLDNFGNYQSYSIWGTDKATADLTVFLVSGIYYPIRLFYVNRDNNAVLDFSFSTEFNKEIIHDFTSYFFSASDEEQCPGNINYNYHCADVKSSTILTSSTTVDKQEGNIVPITKTIYEIGVPCDPEQPTQKCEGEFYNPIRDVCEPLPTPSQENKSSSSSSSSSSSSSSSSSSSSSPSVNPSSVNPSSVNPSSKPVDPSPADPSHNPSSVNPSSVNPSSVNPSSVNPSSKPADPSPADPSHNPSSVNPSSVNPSSKPVDPSPADPSHNPSSVNPSSVNPSSVNPSSVNPSSKPADPSPADPSHNPSSVNPSSVNPSSKPVDPSPADPSSVNPSSVNPSSVNPSSVNPSSVNPSSKPVDPSPADPSHNPSSVNPSSVNPSSVNPSSVNPSSKPADPSPADPSHNPSSVNPSSVNPSSKPVDPSPADPSHNPSSVNPSSVNPSSVNPSSKPADPSPADPSHNPSSVNPSSVNPSSVNPSSVIPSSVNPSSVNPSSVNPSSKPVDPSPADPSHNPSSVNPSSVNPSSKPADPSPADPSHNPSSVNPSSVNPSSVNPSSKPADPSPADPSSVNPSSVNPSSVNPSSKPADPSPADPSHNPSSVNPSSVNPSSVNPSSKPADPSPADPSHNPSSVNPSSVNPSSVNPSPSIVSPSISTRTVTLSNGSTTTVTVTVTPPSPNGGSSNSNTDSFSLPPPYTTTVSKSTTTETDIVSFFPSTDSDGHTRTGTTTITLTGSKPGNNGDSDSFSLPPPYTTTVSKSTTTETDIVSFFPSTDSDGHTRTGTTTITLTGSKPGNNGDSDSFSLPPPYTTTVSKSTTTETDIVSFFPSTDSDGHTRTGTTTITLTGSKPGNNGDSDSFSLPPPYTTTVSKSTTTETDIVSFFPSTDSDGHTRTGTTTITLTGSKPGNNGDSDSFSLPPPYTTTVSKSTTTITLTGSKPSNNGNVGTSSVPPVGNIAITPSVSTRTVTFTNGIISTITTTIRPPSPNGGGSGNNGNTPSPNGGGSGNNGNTPSPNGGGSGNNGNTPSPNGGGSGNNGNTPSPNGGGSGNTGNTPSPNGGGSGNNGNTPSPNGGGSGNNGNTPSPNGGGSGNNGNTPSPNGGGSGNNGNTPSPNGGGSGNTGNTPSPNGGGSGNNGNTPSPNGGGSGNNGNTPSPNGGGSGNNGNTPSPNGSGSGNNGNGNLSPSISTSITSVQSVPSIFKGEGFRAAHLSSIFIWTIITVLVAPILV
Protein: Elastase, neutrophil expressed (D4A488)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Proteinase 3
- Myeloperoxidase
- Cathepsin G
- Lactotransferrin
- Gasdermin D
- Matrix metalloproteinase-9
- Neutrophil collagenase
- Membrane spanning 4-domains A3
- Secretory leukocyte peptidase inhibitor
- Macrophage metalloelastase
Sequence:
MQPTMALHRPSNQTLASMLLALLLVCPALASEIVGGRPAQPHAWPFMVSLQRRGGHFCGATLIARNFVMSAAHCVNGRNFQSVQVVLGAHDLRRREPTRQIFSVQRIFENGFDPSRLLNDIVIIQLNGSATINANVQVAELPAQGQGVGNRTPCVAMGWGRLGTNRPLPSVLQELNVTVVTNLCRRRVNVCTLVPRRQAGICFGDSGGPLVCNNLVQGIDSFIRGGCGSGFYPDAFAPVAEFADWINSIIRSHDDRPLTNPKDREREGRTN
Protein: Uncharacterized fimbrial-like protein SfmA (Type-1A pilin) (P0ABW5)
Organism: Escherichia coli (strain K12)
Function: Part of the sfmACDHF fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Increases adhesion to eukaryotic T24 bladder epithelial cells in the absence of fim genes.
Subcellular location: Fimbrium {ECO:0000250}.
Interaction partners:
- Type 1 fimbrin D-mannose specific adhesin
- Uncharacterized fimbrial-like protein SfmH
- Probable fimbrial chaperone SfmC
- Chaperone protein FimC
- Uncharacterized fimbrial-like protein SfmF
- Probable autotransporter YfaL
- Type 1 fimbriae regulatory protein FimB
- Protein FimF
- Type 1 fimbriae regulatory protein FimE
- Flagellin
Sequence:
MKLRFISSALAAALFAATGSYAAVVDGGTIHFEGELVNAACSVNTDSADQVVTLGQYRTDIFNAVGNTSALIPFTIQLNDCDPVVAANAAVAFSGQADAINDNLLAIASSTNTTTATGVGIEILDNTSAILKPDGNSFSTNQNLIPGTNVLHFSARYKGTGTSASAGQANADATFIMRYE