wanglab/gogpt-training-data huggingface dataset:
Protein: Alanine--tRNA ligase, mitochondrial (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) (Q9VRJ1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03133}.
Interaction partners:
- Tyrosine--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
- Tyrosine--tRNA ligase, mitochondrial
- Probable proline--tRNA ligase, mitochondrial
- histidine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Alanine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase
- Glycine--tRNA ligase
Sequence:
MYNSAKQLQRVLTAREIRKTFLDHFTVNHGHKFVRSSPVVPFCDPTVAFVNAGMNQFKSVFLGTAAAPHKRVVNSQKCVRVGGKHNDLSVVGTDGYHHTFFEMLGNWSFGDYFKREACAMALELLRGPYNIDPGRLYVTYFAGDKVLGIPADLECFEIWRSLGFPASRILPFGCADNFWEMGATGPCGPCTEIHIDHRPDLGSVEQRAKLVNAGRSDLTELWNLVFIQYNRHADGSISQLPAHHVDTGMGFERLTAVLQNKSSNYDTDLFTPIFDGIQQAAKTPVYSGSFPDGGNAAVLDTSYRILADHARMVTACLADGMLPDQNQKLRRVLRKALNISEHVFAHDKLLTQLVPIVVETLGEAYPEMAAKQQAVIDLICHEQEVYKNLRESSSKAFAEVLMEFPNLDDIDLMECPGFVPAYRELQMQRCKFSNNTIPGDFLYKLTDTYGLTEESFLKLAELENMNCDLERYRAEVSLAKLKAKGNQRETAGGSLCDLATEQRIAEAQAMLTKRLTPTDNSHKYTYSFDKESDSYQIPPLKTRVLGMLLNDAEVSRTQGSRIQQPFTDLISIVTAGSNFYYESGGQQSDGGKILVSNHQQPDHPHSLDVIGVKHLNDCVVHICKLSSPTDAFQLAIGDEVELQVDAQQRQLNTCHHTATHLLNAAIRSLFKKVTYQVSSSVSSDQCKLELGLLGKRIQKTDVQLIEDLINRVICSAAPVEVQLLSAAEVLEQNDITMVPGEVYPEQGLRLVNVESPELQLSSKELCCGTHATNTSELSCFCIVNLKQTNRARFAFTAVAGQAAENVLKTAALLRHRVDLLEKQFQTDKLTNATEAELQTIRHNMLHTDIKLPYAFKMDTLERITEMLKRIKDSSRTTLKEFVDVEMRTLLQEKPLDTHPFILHYITSSALVEEIPLQRATKLCPDRPILVISVCDSVVKARCCVPEKCITEKFNASAWLQSFADTFNGQIAAPKGQNPQAVCNMKGRRVSNLFEEQLEQAMSKAHAYAKLYL
Protein: Calcium-binding protein 2 (P54653)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Not known; probably binds four calcium ions.
Interaction partners:
Sequence:
MSATVHYKDIRKGMEKDLESLFKKYDSDRNGKITYIEIVETLRKAGKKNPERIADLLFRDDTDKNGELTIEEAKLRIVRMNDEKIEKVLNWDVEKFINDNDKDGDRKITRDEVLQRFTEQGAEDPELITDSIFRQMDLDRDGVITCDEIKEFNRKKKFSFLKSSAPKQ
Protein: Basic leucine zipper transcriptional factor ATF-like 3 (B-ATF-3) (Jun dimerization protein 1) (JDP-1) (P97876)
Organism: Rattus norvegicus (Rat)
Function: AP-1 family transcription factor that controls the differentiation of CD8(+) thymic conventional dendritic cells in the immune system. Acts via the formation of a heterodimer with JUN family proteins that recognizes and binds DNA sequence 5'-TGA[CG]TCA-3' and regulates expression of target genes. Required for development of CD8-alpha(+) classical dendritic cells (cDCs) and related CD103(+) dendritic cells that cross-present antigens to CD8 T-cells and produce interleukin-12 (IL12) in response to pathogens (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Transcription factor Jun
- Interferon regulatory factor 8.
- T-cell surface glycoprotein CD4
- Chemokine XC receptor 1
- Interferon regulatory factor 4
- C-type lectin domain family 9 member A
- Integrin subunit alpha E
- Zinc finger and BTB domain-containing protein 46
Sequence:
MSQGPPAGGVLQSSVAAPGNQPQSPKDDDRKVRRREKNRVAAQRSRKKQTQKSDKLHEEHESLEQENSVLRREIAKLKEELRHLTEALKEHEKMCPLLLCPMNFVQLRPDPVASWSAHDAPDHPSFIWLGTLV
Protein: Cyanamide hydratase DDI2 (CAH) (EC 4.2.1.69) (DNA damage-inducible protein 2) (P0CH63)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cyanamide hydratase involved in the detoxification and/or utilization of cyanamide, a toxic nitrile compound distributed widely in the environment.
Interaction partners:
- Urea amidolyase
- Uncharacterized protein YGR045C
Sequence:
MSQYGFVRVPREVEKAIPVVNAPRPRAVVPPPNSETARLVREYAAKELTAPVLNHSLRVFQYSVAIIRDQFPAWDLDQEVLYVTCLLHDIATTDKNMRATKMSFEYYGGILSRELVFNATGGNQDYADAVTEAIIRHQDLTGTGYITTLGLILQIATTLDNVGSNTDLIHIDTVSAINEQFPRLHWLSCFATVVDTENSRKPWGHTSSLGDDFSKKVICNTFGYN
Protein: Transcriptional enhancer factor TEF-1 (H0YE88)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002603}.
Interaction partners:
Sequence:
IEPSSWSGSESPAENMERMSDSADKPIDNDAEGVWSPDIEQSFQEALAIYPPCGRRKIILSDEGKMYGRNELIARYIKLRTGKTRTRKQVSSHIQVLARRKSRDFHSKLKDQTAKDKALQHMAAMSSAQIVSATAIHNKLGLPGIPRPTFPGAPGFWPGMIQTGQPGSSQDVKPFVQQAYPIQPAVTAPIPGFEPASAPAPSVPAWQGRSIGTTKLRLVEFSAFLEQQRDPDSYNKHLFVHIGHANHSYSDPLLESVDIRQIYDKFPEKKGGLKELFGKGPQNAFFLVKFWADLNCNIQDDAGAFYGVTSQYESSENMTVTCSTKVCSFGKQVVEKVETEYARFENGRFVYRINRSPMCEYMINFIHKLKHLPEKYMMNSVLENFTILLVVTNRDTQETLLCMACVFEVSNSEHGAQHHIYRLVKD
Protein: Double-strand break repair protein (A0A1D8PQT2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR000882}.
Interaction partners:
- DNA repair protein RAD50
- Rad2 family nuclease
- Serine/threonine-protein kinase TEL1
- DNA helicase
- Serine/threonine-protein kinase MEC1
- ATP-dependent DNA helicase II subunit 2
- Flap endonuclease 1
- DNA repair protein RAD51 homolog
- DNA 3'-5' helicase
- Replication protein A subunit
Sequence:
MPLVERIEPGPDTIRVLLTTDNHVGAFENDPIRGDDAWKTFDEITTIAKDKDVDMIIQGGDLFHINKPTKKSMYHVMKSLRSNCMGDRPCELELLSDPAQSLNNGFDEINYEDPNLNISIPVFAISGNHDDATGESLLSALDVLAVTGLINNFGKVKNTEAITVSPILLQKGQTKLALYGMSNVRDERLHRLFRDGGVKFQRPNIQTEDWFNLFVIHQNHAAHTYTSSIPESFLPNFLDFILWGHEHECIPYPVHNPETTFDVLQAGSSVATSLAEGEVADKKIFILNIKGKDYSIEPVELKTVRPFVLREIILSKTDLIPGAASKADVIAYLTDEVEKSIERANKQFSSQNISNSNRAITNSSNNATADPIEKPLPLIRLRVEYSGGYEIENVTRFSNRFVGKIANVNDVVQFYKKKTPTKSDNKLTRKTKYDVDLIEENLHHKKTTELELQDIIRDFLQQTQLSLVPETEMNHAVKKFVENDDKQALNQFINQEIKRETKMLLDIDIDENEFHGADEKHAKTAFKHVLSQLKNINGPINIDYEPEIEPTNNNTNKKSATTKKRTPKKNTTIPKKITTTATKKPKIDDIIISSDDSNDYGNDDDDDKEEEEEENEHDSGLRLFVTDTPDTNSTRRSKSNRSKRPTSYVEDESGILSDEDDYVPPSKSKGIFSRSFNNRKRK
Protein: Pullulanase 1, chloroplastic (AtPU1) (EC 3.2.1.142) (Protein LIMIT DEXTRINASE) (AtLDA) (Q8GTR4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in starch degradation and also probably in the trimming of pre-amylopectin chains during starch synthesis.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:16495218, ECO:0000269|PubMed:18431481}.
Interaction partners:
- Starch synthase 3, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE2
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- Isoamylase 2, chloroplastic
- Alpha-glucan phosphorylase 2, cytosolic
- Alpha-amylase 3, chloroplastic
- Alpha-glucan phosphorylase 1
- starch synthase
- Probable alpha-amylase 2
- Alpha-amylase 1
Sequence:
MALTLTPTSSVHLLSSISVARPRIFAADFNLRSRWRRRRPVTSISNFRLRLPSKTSLHCLCSSSSASSPMSLEVSSPNSQFLDCLIYSRAYWVTQGVIAWNVDVGEGSCYFYASKSAGLSFSEDGIDGYDLRIKLEAESGSLPADVIEKFPHIRNYKSFKVPKDLDIRDLVKSQLAVVCFDAEGRLIQGTGLQLPGVLDELFSYDGPLGAHFTPEGVSLHLWAPTAQAVSVCIYKNPLDKSPMEICPLKEANGVWSTEGACSWGGCYYVYKVSVYHPSTMKLETCYANDPYARGLSADGRKTFLVNLDSDDLKPEGWDNLADKKPCLRSFSDISIYELHVRDFSANDETVEPENRGGYLAFTSKDSAGVKHLQKLVDAGLTHLHLLPTFQFGDVDDEKENWKSVDTSLLEGLRPDSTEAQARITEIQNDDGYNWGYNPVLWGVPKGSYASDPTGPCRIIEFRKMVQALNCTGLNVVLDVVYNHLHASGPHDKESVLDKIVPGYYLRRNSDGFIENSTCVNNTASEHYMVDRLIRDDLLNWVVNYKVDGFRFDLMGHIMKATIVNAKSAIGSLRKETDGVDGSRIYLYGEGWNFGEVAENGRGINASQFNLGGTGIGSFNDRIRDATLGGSPFGHPLQQGFITGLLLQPNAHDHGSEATQELMLSTAKNHIQTGMAANLKDYMLTNHEGKEVKGSEVLMHDATPVAYASLPTETINYVSAHDNETLFDIISLKTPMEISVDERCRINHLASSMIALSQGIPFFHAGDEILRSKSLDRDSYNSGDWFNRLDFSYSSNNWGVGLPPKGKNEHNWPLIKPRLQDPSFKPKSSHIVATLHNFLDLLRIRYSSPLFRLDTARAIQERVRFHNTGPSSIPGAIVMSIEDGHRGIPSVSQIDPIYSLIVVIFNARPSEFSYPSPALKDRKLELHPVQVMSADEIVKKSVYDSFSGGFTVPARTTTVFVESRNG
Protein: Spectrin beta chain (G3V6S0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MTTTVATDYDNIEIQQQYSDVNNRWDVDDWDNENSSARLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYTDLRDGRMLIKLLEVLSGERLPKPTKGRMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIILRFQIQDISVETEDNKEKKSAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDPEDISVDHPDEKSIITYVVTYYHYFSKMKALAVEGKRIGKVLDNAIETEKMIEKYESLASDLLEWIEQTIIILNNRKFANSLVGVQQQLQAFNTYRTVEKPPKFTEKGNLEVLLFTIQSKMRANNQKVYMPREGKLISDINKAWERLEKAEHERELALRNELIRQEKLEQLARRFDRKAAMRETWLSENQRLVSQDNFGFDLPAVEAATKKHEAIETDIAAYEERVQAVVAVARELEAESYHDIKRITARKDNVIRLWEYLLELLRARRQRLEMNLGLQKIFQEMLYIMDWMDEMKVLLLSQDYGKHLLGVEDLLQKHALVEADIAIQAERVRGVNASAQKFATDGEGYKPCDPQVIRDRVAHMEFCYQELCQLAAERRARLEESRRLWKFFWEMAEEEGWIREKEKILSSDDYGKDLTSVMRLLSKHRAFEDEMSGRSGHFEQAIKEGEDMIAEEHFGSEIRERISYIREQWANEQLSAIRKKRLEEASLLHQFQADADDIDAWMLDILKIVSSNDVGHDEYSTQSLVKKHKDVAEEISNYRPTIDTLHEQAGALPQAHAESPDVKGRLAGIEERYKEVAELTRLRKQALQDTLALYKMFSEADACELWIDEKEQWLNNMQIPEKLEDLEVIQHRFESLEPEMNNQASRVAVVNQIARQLMHSGHPSEKEIRAQQDKLNTRWSQFRELVDRKKDALLSALSIQNYHLECNETKSWIREKTKVIESTQDLGNDLAGVMALQRKLTGMERDLVAIEAKLSDLQKEAEKLESEHPDQAQAILSRLAEISDVWEEMKTTLKNREASLGEASKLQQFLRDLDDFQSWLSRTQTAIASEDMPNTLTEAEKLLTQHENIKNEIDNYEEDYQKMRDMGEMVTQGQTDAQYMFLRQRLQALDTGWNELHKMWENRQNLLSQSHAYQQFLRDTKQAEAFLNNQEYVLAHTEMPTTLEGAEAAIKKQEDFMTTMDANEEKINAVVETGRRLVSDGNINSDRIQEKVDSIDDRHRKNREAASELLMRLKDNRDLQKFLQDCQELSLWINEKMLTAQDMSYDEARNLHSKWLKHQAFMAELASNKEWLDKIEKEGMQLISEKPETEAVVKEKLTGLHKMWEVLESTTQTKAQRLFDANKAELFTQSCADLDKWLHGLESQIQSDDYGKDLTSVNILLKKQQMLENQMEVRKKEIEELQSQAQALSQEGKSTDEVDSKRLTVQTKFMELLEPLNERKHNLLASKEIHQFNRDVEDEILWVGERMPLATSTDHGHNLQTVQLLIKKNQTLQKEIQGHQPRIDDIFERSQNIITDSSSLNAEAIRQRLADLKQLWGLLIEETEKRHRRLEEAHKAQQYYFDAAEAEAWMSEQELYMMSEEKAKDEQSAVSMLKKHQILEQAVEDYAETVHQLSKTSRALVADSHPESERISMRQSKVDKLYAGLKDLAEERRGKLDERHRLFQLNREVDDLEQWIAEREVVAGSHELGQDYEHVTMLQERFREFARDTGNIGQERVDTVNHMADDLINSGHSDAATIAEWKDGLNEAWADLLELIDTRTQILAASYELHKFYHDAKEIFGRIQDKHKKLPEELGRDQNTVETLQRMHTTFEHDIQALGTQVRQLQEDAARLQAAYAGDKADDIQKRENEVLEAWKSLLDACEGRRVRLVDTGDKFRFFSMVRDLMLWMEDVIRQIEAQEKPRDVSSVELLMNNHQGIKAEIDARNDSFTACIELGKALLARKHYASEEIKEKLLQLTEKRKEMIDKWEDRWEWLRLILEVHQFSRDASVAEAWLLGQEPYLSSREIGQSVDEVEKLIKRHEAFEKSAATWDERFSALERLTTLELLEVRRQQEEEERKRRPPSPEPSAKVSEEAESQQWDTSKGDQVSQNGLPAEQGSPRMAGTMETSEMVNGAAEQRTSSKESSPVPSPTSDRKAKSALPAQSAATLPARTLETPAAQMEGFLNRKHEWEAHNKKASSRSWHNVYCVINNQEMGFYKDAKSAASGVPYHSEVPVSLKEAICEVALDYKKKKHVFKLRLSDGNEYLFQAKDDDEMNTWIQAITSAISSDKHDTSASTQSTPASSRAQTLPTSVVTITSESSPGKREKDKEKDKEKRFSLFGKKK
Protein: Small ribosomal subunit protein uS15c (30S ribosomal protein S15, chloroplastic) (P0C469)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- Small ribosomal subunit protein uS12cz/uS12cy
- Small ribosomal subunit protein uS2c
- Small ribosomal subunit protein uS9c
- Small ribosomal subunit protein bS16c
- Uncharacterized protein
- Small ribosomal subunit protein uS7cz/uS7cy
- Small ribosomal subunit protein uS14c
- S5 DRBM domain-containing protein
Sequence:
MKKKGGRKIFGFMVKEEKEENWGSVEFQVFSFTNKIRRLASHLELHKKDFSSERGLRRLLGKRQRLLAYLAKKNRVRYKKLISQLDIRER
Protein: C-C motif chemokine 25 (Chemokine TECK) (Small-inducible cytokine A25) (Thymus-expressed chemokine) (O15444)
Organism: Homo sapiens (Human)
Function: Potentially involved in T-cell development. Recombinant protein shows chemotactic activity on thymocytes, macrophages, THP-1 cells, and dendritics cells but is inactive on peripheral blood lymphocytes and neutrophils. Binds to CCR9. Isoform 2 is an antagonist of isoform 1. Binds to atypical chemokine receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4.
Subcellular location: Secreted.
Interaction partners:
- C-C chemokine receptor type 9
- C-X-C motif chemokine 11
- Atypical chemokine receptor 4
- Atypical chemokine receptor 2
- Stromal cell-derived factor 1
- C-C motif chemokine 17
- C-C motif chemokine 5
- Platelet factor 4
- C-X-C motif chemokine 17
- Platelet factor 4 variant
Sequence:
MNLWLLACLVAGFLGAWAPAVHTQGVFEDCCLAYHYPIGWAVLRRAWTYRIQEVSGSCNLPAAIFYLPKRHRKVCGNPKSREVQRAMKLLDARNKVFAKLHHNTQTFQAGPHAVKKLSSGNSKLSSSKFSNPISSSKRNVSLLISANSGL
Protein: Tripartite motif-containing protein 67 (Q505D9)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Microtubule-associated. {ECO:0000250}.
Interaction partners:
Sequence:
MEEELKCPVCGSLFREPIILPCSHNVCLPCARTIAVQTPDGEQHLPPPLLLSRGAAAAATPPDQDAAAGATSGGAGANTAGGLGGGATGGGDHADKLSLYSETDSGYGSYTPSLKSPNGVRVLPMVPAPPGSSAAAARGAACSSLCSSSSSITCPQCHRSASLDHRGLRGFQRNRLLEGIVQRYQQGRGVVPGAAAAPAVAICQLCDRTPPEPAATLCEQCDVLYCATCQLKCHPSRGPFAKHRLVQPPPPPTPPEATPAVTGTSTASSAGGCRSPGGAGASAPRKFPTCPEHEMENYSMYCVSCRSPVCYMCLEEGRHSKHEVKPLGATWKQHKAQLSQALNGVSDKAKEAKEFLVQLKNILQQIQENGLDYEACLVAQCDALVDALTRQKAKLLTKVTKEREHKLKMVWDQINHCTLKLRQSTGLMEYCLEVIKEDDPSGFLQISDALIKRVQTSQEQWVKGALEPKVSAEFDLTLDSEPLLQAIHQLDFVQMKLPPVPLLQLEKCCTRNNSVTLAWRTPPFTHSPAEGYILELDDGDGGQFREVYVGKETLCTIDGLHFNSTYNARVKAFNSSGVGPYSKTVVLQTSDVAWFTFDPNSGHRDIILSNDNQTATCSSYDDRVVLGTAAFSKGVHYWELHVDRYDNHPDPAFGVARASVVKDMMLGKDDKAWAMYVDNNRSWFMHCNSHTNRTEGGVCKGATVGVLLDLNKHTLTFFINGQQQGPTAFSHVDGVFMPALSLNRNVQVTLHTGLEVPTNLGRPKLSGN
Protein: ERBB receptor feedback inhibitor 1 (Mitogen-inducible gene 6 protein) (MIG-6) (Q9UJM3)
Organism: Homo sapiens (Human)
Function: Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratinocyte proliferation and differentiation. Plays a role in modulating the response to steroid hormones in the uterus. Required for normal response to progesterone in the uterus and for fertility. Mediates epithelial estrogen responses in the uterus by regulating ESR1 levels and activation. Important for regulation of endometrium cell proliferation. Important for normal prenatal and perinatal lung development (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:7641805}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associated with the plasma membrane of basal skin keratinocytes. Translocates into the nucleus of differentiating suprabasal keratinocytes (By similarity). {ECO:0000250}.
Interaction partners:
- Epidermal growth factor receptor
- Growth factor receptor-bound protein 2
- Receptor tyrosine-protein kinase erbB-2
Sequence:
MSIAGVAAQEIRVPLKTGFLHNGRAMGNMRKTYWSSRSEFKNNFLNIDPITMAYSLNSSAQERLIPLGHASKSAPMNGHCFAENGPSQKSSLPPLLIPPSENLGPHEEDQVVCGFKKLTVNGVCASTPPLTPIKNSPSLFPCAPLCERGSRPLPPLPISEALSLDDTDCEVEFLTSSDTDFLLEDSTLSDFKYDVPGRRSFRGCGQINYAYFDTPAVSAADLSYVSDQNGGVPDPNPPPPQTHRRLRRSHSGPAGSFNKPAIRISNCCIHRASPNSDEDKPEVPPRVPIPPRPVKPDYRRWSAEVTSSTYSDEDRPPKVPPREPLSPSNSRTPSPKSLPSYLNGVMPPTQSFAPDPKYVSSKALQRQNSEGSASKVPCILPIIENGKKVSSTHYYLLPERPPYLDKYEKFFREAEETNGGAQIQPLPADCGISSATEKPDSKTKMDLGGHVKRKHLSYVVSP
Protein: Metallophosphoesterase 1 (Post-GPI attachment to proteins factor 5) (K7EQ70)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000256|ARBA:ARBA00004457}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004457}. Golgi apparatus, cis-Golgi network membrane {ECO:0000256|ARBA:ARBA00004257}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004257}.
Interaction partners:
Sequence:
MAMIELGFGRQNFHPLKRKSSLLLKLIAVVFAVLLFCEFLIYYLAIFQCNWPEVKTTASDGEQTTREPVLKAMFLADTHLLGEFLGHWLDKLRREWQMERAFQTALWLLQPEVVFILGDIFDEGKWSTPEAWADDVERFQKMFRHPSHVQLKVVAGNHDIGFHY
Protein: HHIP-like protein 1 (Q96JK4)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MARARAGALLALWVLGAAAHPQCLDFRPPFRPTQPLRLCAQYSDFGCCDEGRDAELTRRFWALASRVDAAEWAACAGYARDLLCQECSPYAAHLYDAEDPFTPLRTVPGLCQDYCLDMWHKCRGLFRHLSTDQELWALEGNLARFCRYLSLDDTDYCFPYLLVNKNLNSNLGHVVADAKGCLQLCLEEVANGLRNPVAMVHARDGTHRFFVAEQVGLVWAYLPDRSRLGKPFLNISRVVLTSPWEGDERGFLGIAFHPSFQHNRRLYVYYSVGIRSSEWIRISEFRVSEDDENAVDHSSERIILEVKEPASNHNGGQLLFGDDGYLYIFTGDGGMAGDPFGTFGNAQNKSALLGKVLRIDVDRKERGLPYGIPPDNPFVGDPAAQPEVYALGVRNMWRCSFDRGDPSSGTGRGRLFCGDVGQNKFEEVDVVERGGNYGWRAREGFECYDRSLCANTSLNDLLPIFAYPHTVGKSVTGGYVYRGCEYPNLNGLYIFGDFMSGRLMSLQENPGTGQWQYSEICMGHGQTCEFPGLINNYYPYIISFGEDEAGELYFMSTGEPSATAPRGVVYKIIDASRRAPPGKCQIQPAQVKIRSRLIPFVPKEKFIPKTRSTPRPTARAPTRAPRRGRPTAAPPAPTPRPARPTQQPGSRRGGGRRRGRLNSASRAFRDGEVRLVRPAGLSSGSGRVEVFVGGRWGTVCDDSWNISGAAVVCRQLGFAYAVRAVKRAEFGQGGSLPILLDDVRCAGWERNLLECQHNGVGTHNCEHDEDAGVVCSHQNPDL
Protein: RING finger protein 175 (Q8N4F7)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAAGTAARKAAPVLEAPPQQEQLSHTKLSAEDTWNLQQERMYKMHRGHDSMHVEMILIFLCVLVIAQIVLVQWRQRHGRSYNLVTLLQMWVVPLYFTIKLYWWRFLSMWGMFSVITSYILFRATRKPLSGRTPRLVYKWFLLIYKLSYAFGVVGYLAIMFTMCGFNLFFKIKARDSMDFGIVSLFYGLYYGVMGRDFAEICSDYMASTIGFYSVSRLPTRSLSDNICAVCGQKIIVELDEEGLIENTYQLSCNHVFHEFCIRGWCIVGKKQTCPYCKEKVDLKRMISNPWERTHFLYGQILDWLRYLVAWQPVVIGIVQGIIYSLGLE
Protein: Fumarate reductase flavoprotein subunit (EC 1.3.5.1) (Quinol-fumarate reductase flavoprotein subunit) (QFR flavoprotein subunit) (P00363)
Organism: Escherichia coli (strain K12)
Function: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; fumarate reductase is used during anaerobic growth, and succinate dehydrogenase is used during aerobic growth. The QFR enzyme complex binds 2 quinones in or near the membrane; 1 near the [3Fe-4S] cluster (QP is proximal to the [3Fe-4S] cluster, on the cytoplasmic side of the membrane) while QD (the distal cluster) is on the other side of the membrane. It is not clear if both of the quinol-binding sites are functionally relevant.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:10373108, ECO:0000305|PubMed:20484676}; Peripheral membrane protein {ECO:0000305|PubMed:10373108}; Cytoplasmic side {ECO:0000305|PubMed:10373108}.
Interaction partners:
- Fumarate reductase subunit C
- Fumarate reductase iron-sulfur subunit
- Fumarate reductase subunit D
- Succinate dehydrogenase iron-sulfur subunit
- Succinate dehydrogenase cytochrome b556 subunit
- FAD assembly factor SdhE
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- Succinate--CoA ligase subunit beta
- Succinate--CoA ligase subunit alpha
- NADH-quinone oxidoreductase subunit C/D
Sequence:
MQTFQADLAIVGAGGAGLRAAIAAAQANPNAKIALISKVYPMRSHTVAAEGGSAAVAQDHDSFEYHFHDTVAGGDWLCEQDVVDYFVHHCPTEMTQLELWGCPWSRRPDGSVNVRRFGGMKIERTWFAADKTGFHMLHTLFQTSLQFPQIQRFDEHFVLDILVDDGHVRGLVAMNMMEGTLVQIRANAVVMATGGAGRVYRYNTNGGIVTGDGMGMALSHGVPLRDMEFVQYHPTGLPGSGILMTEGCRGEGGILVNKNGYRYLQDYGMGPETPLGEPKNKYMELGPRDKVSQAFWHEWRKGNTISTPRGDVVYLDLRHLGEKKLHERLPFICELAKAYVGVDPVKEPIPVRPTAHYTMGGIETDQNCETRIKGLFAVGECSSVGLHGANRLGSNSLAELVVFGRLAGEQATERAATAGNGNEAAIEAQAAGVEQRLKDLVNQDGGENWAKIRDEMGLAMEEGCGIYRTPELMQKTIDKLAELQERFKRVRITDTSSVFNTDLLYTIELGHGLNVAECMAHSAMARKESRGAHQRLDEGCTERDDVNFLKHTLAFRDADGTTRLEYSDVKITTLPPAKRVYGGEADAADKAEAANKKEKANG
Protein: Copper-exporting P-type ATPase (Protein CopA) (EC 7.2.2.8) (Copper-exporting P-type ATPase A) (Cu(+)-exporting ATPase) (O32220)
Organism: Bacillus subtilis (strain 168)
Function: Involved in copper export.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Copper chaperone CopZ
- Superoxide dismutase-like protein YojM
- Copper-sensing transcriptional repressor CsoR
- Cadmium, zinc and cobalt-transporting ATPase
Sequence:
MSEQKEIAMQVSGMTCAACAARIEKGLKRMPGVTDANVNLATETSNVIYDPAETGTAAIQEKIEKLGYHVVTEKAEFDIEGMTCAACANRIEKRLNKIEGVANAPVNFALETVTVEYNPKEASVSDLKEAVDKLGYKLKLKGEQDSEAAAKKKEERKQTARLIFSAVLSFPLLWAMVSHFTFTSFIWVPDIFLNPWMQFALATPVQFLIGWPFYVGAYKALRNKSANMDVLVALGTTAAYAYSLYLTFQSIGSHGHTDGLYYETSAILLTLILLGKLFETKAKGRSSDAIKKLMKLQAKTATVVRDGQEQIIPIDEVLVNDIVYVKPGERIPVDGEVVEGRSAVDESMITGESLPVDKNPGDSVTGSTVNANGFLKIKAVNVGKDTALSHIIKIVEEAQGSKAPIQRLADQISGIFVPIVLGIAVLTFLIWYLWAAPGDFAEAISKFIAVLVIACPCALGLATPTSIMAGSGRAAEFGILFKGGEHLEKTHRLDTIVLDKTGTVTNGKPRLTDAIPFGRFEEKDLLQFAAAAETGSEHPLGEAIIAGVKDKGLEIPKLTRFEAKVGAGILAEAGGKSILVGTRKLMESEQVEHGALLAQMEELEAEGKTVMLVSIDGEAAGLVAVADTIKDTSRKAVARLKELGLDVIMMTGDNRRTAEAIAKEAGIANIIAEVLPEQKAAEIARLQKEGRQTAMVGDGINDAPALATADIGMAIGTGTDIAMETADITLIRGDLNSIADAIRMSRLTMKNIKQNLFWALGYNSLGIPIAALGFLAPWIAGAAMAFSSVSVVLNALRLQKVK
Protein: LD18904p (Longevity protein) (Schlank, isoform A (EC 2.3.1.24)) (Schlank, isoform B) (Q9W423)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Neutral ceramidase
- sphingosine kinase
- Ceramide kinase, isoform A
- Sphingolipid delta
- Putative neutral sphingomyelinase
- Alkaline ceramidase
- ceramide glucosyltransferase
- 3-dehydrosphinganine reductase
- sphingosine kinase
- serine C-palmitoyltransferase
Sequence:
MDILNEFSNVFWSTHIWLPPNTTWADIAPGSRPDVVHANYKDLIWPIPFAAVVMLVRYTLERFWISPVGKSLGIRSSRPKKAANVPILEKTYAKSTRLDKKKLVPLSKQTDMSEREIERWWRLRRAQDKPSTLVKFCENTWRCIYYLYSFIFGVIVLWDKPWFWDVKSCWYGYPHQSISNDIWWYYMISMSFYWSLTGTQFFDVKRKDFWQMFIHHMVTLLLMSLSWVCNLHRVGSLVLVVHDCADIFLEAAKLTKYAKYQKLCDAIFAIFTVVWIVTRLGFYPRIIYSSSVEAPRILPMFPAYYIFNSLLLMLLVLHVIWTYMILKIVVDSLQKGLMSGDIRSSDSEDLTDSSGNARLTNGSARSKNKSISSAPSDKGSAGGAGSRAGARVATTERREE
Protein: LD04190p (Q95RX2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKNSSSKTLAAGSRLANSGNGSHNGGPCSVEDLLIRIGLKEYTSVFVLNGYEDLELFKELEPADLDYLGILNQEHRAKLLTAVQLLHDIECSDVDIPGSSSENDEARLNNINMKHGASPFGRRHFPRDSGCYEGSPLPSSQTPTQAVNSTDESNSLDDVVTKCSSEIMKRVESARRCKDNPFKTTLPGGGRLGKKSFLGGNGLMADDTLTRGGLSEKSSDSGVSSSSLSSGPLKSST
Protein: Transcription factor SOX-17 (Q61473)
Organism: Mus musculus (Mouse)
Function: Acts as transcription regulator that binds target promoter DNA and bends the DNA. Binds to the sequences 5'-AACAAT-'3 or 5'-AACAAAG-3'. Modulates transcriptional regulation via WNT3A. Inhibits Wnt signaling. Promotes degradation of activated CTNNB1. Plays a key role in the regulation of embryonic development. Required for normal development of the definitive gut endoderm. Required for normal looping of the embryonic heart tube. Plays an important role in embryonic and postnatal vascular development, including development of arteries. Plays an important role in postnatal angiogenesis, where it is functionally redundant with SOX18. Required for the generation and maintenance of fetal hematopoietic stem cells, and for fetal hematopoiesis. Probable transcriptional activator in the premeiotic germ cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:20802155, ECO:0000269|PubMed:24153254, ECO:0000269|PubMed:8636240}.
Interaction partners:
- POU domain, class 5, transcription factor 1
- Lymphoid enhancer-binding factor 1
- Transcription factor 7-like 1
- Catenin beta-1
- Transcription factor 7-like 2
- Transcription factor 7
- Homeobox protein NANOG
- Transcription factor GATA-6
- Hepatocyte nuclear factor 3-beta
- Homeobox protein MIXL1
Sequence:
MSSPDAGYASDDQSQPRSAQPAVMAGLGPCPWAESLSPLGDVKVKGEVVASSGAPAGTSGRAKAESRIRRPMNAFMVWAKDERKRLAQQNPDLHNAELSKMLGKSWKALTLAEKRPFVEEAERLRVQHMQDHPNYKYRPRRRKQVKRMKRVEGGFLHALVEPQAGALGPEGGRVAMDGLGLPFPEPGYPAGPPLMSPHMGPHYRDCQGLGAPALDGYPLPTPDTSPLDGVEQDPAFFAAPLPGDCPAAGTYTYAPVSDYAVSVEPPAGPMRVGPDPSGPAMPGILAPPSALHLYYGAMGSPAASAGRGFHAQPQQPLQPQAPPPPPQQQHPAHGPGQPSPPPEALPCRDGTESNQPTELLGEVDRTEFEQYLPFVYKPEMGLPYQGHDCGVNLSDSHGAISSVVSDASSAVYYCNYPDI
Protein: RIIa domain-containing protein (Q584I5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSDSVRKKEFFDYESRVRIEKHAQQLNTNNKQYISRHPEITLVLHDILQHLLIHKPEDPLAAIQEYAIDRQPPARRAQLLKKEE