wanglab/gogpt-training-data huggingface dataset:
Protein: Argininosuccinate synthase (EC 6.3.4.5) (Citrulline--aspartate ligase) (P00966)
Organism: Homo sapiens (Human)
Function: One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:28985504, ECO:0000305|PubMed:27287393}.
Interaction partners:
- Ornithine transcarbamylase, mitochondrial
- Argininosuccinate lyase
- Carbamoyl-phosphate synthase, mitochondrial
- N-acetylglutamate synthase, mitochondrial
- Multifunctional protein CAD
- Adenylosuccinate synthetase isozyme 2
- Argininosuccinate lyase
- Ornithine aminotransferase, mitochondrial
- Asparagine synthetase
- Nitric oxide synthase, inducible
Sequence:
MSSKGSVVLAYSGGLDTSCILVWLKEQGYDVIAYLANIGQKEDFEEARKKALKLGAKKVFIEDVSREFVEEFIWPAIQSSALYEDRYLLGTSLARPCIARKQVEIAQREGAKYVSHGATGKGNDQVRFELSCYSLAPQIKVIAPWRMPEFYNRFKGRNDLMEYAKQHGIPIPVTPKNPWSMDENLMHISYEAGILENPKNQAPPGLYTKTQDPAKAPNTPDILEIEFKKGVPVKVTNVKDGTTHQTSLELFMYLNEVAGKHGVGRIDIVENRFIGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLGLKFAELVYTGFWHSPECEFVRHCIAKSQERVEGKVQVSVLKGQVYILGRESPLSLYNEELVSMNVQGDYEPTDATGFININSLRLKEYHRLQSKVTAK
Protein: Collectrin, amino acid transport regulator (Collectrin-like protein) (W8FKQ5)
Organism: Dicentrarchus labrax (European seabass) (Morone labrax)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MLEKILILLCLSSALAEQPCKPDASDGYKVRLSIKTALGDEAYVWNENEMFLFRATLAFAMRSHLNGQEFDVSNIIVCDETPRVTFWFVVTSPLNTSGLVDKGVVEEAIRMSRNRINSAFLLTDKTLEFIGITPTLTAPVNPDTPPWLIVFGVVMGAVGAGIIVVLVSPLVLKKRKKNEETDEDEEETGVKAVENGSTREGVYNMSFSDDERLTQM
Protein: Casein kinase II subunit alpha (CK II alpha) (EC 2.7.11.1) (A0A8I6AW60)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU369118}.
Interaction partners:
Sequence:
AAAAAAPLPAGGCRCRCRCRHHRLWGPRAERRPPRSTNPAVPPAAEGPGPAWPAPPAPPARASVRPPAPAGPAWRGRPPPPRSSSCSGGPRPAASRACRPALRAAPPPPSAPRGAPRSRPPCPARPRAVGPGSTPSNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGQDNYDQLVRIAKVLGTDDLYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPCAENTVLSSGLTAAR
Protein: Kinesin-like protein KIN-14R (F4IJK6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein POLLENLESS 3-LIKE 2
- At5g20110
- Calcium-binding EF-hand family protein
- Thaumatin-like protein
- Pathogenesis-related thaumatin superfamily protein
- Kinesin-like protein KIN-5A
- Dynein light chain
- Kinesin-like protein KIN-10A
- Cell division cycle protein 27 homolog A
- Early nodulin-like protein 14
Sequence:
MDDVQIDDTFPVDLNGVTSLCSPEIPSFDFVSDETEKLEIGDTSIDDCDDALGDSMVCDPNSRLVPTGLTRTNRTDETIMFINAGGDDSKVLDSELNISRDDYFEGGDVLRTEESIVEAGDFPFIYQSARVGNFCYQLNNLLPGEYLIDFHFAEIINTNGPKGIRVFNVYVQDEKATEFDIFSVVGANRPLLLVDLRVMVMDDGLIRVRFEGINGSPVVCGICLRKAPQVSVPRTSQDFIKCENCATEIEISPTRKRLMRAKAHDKYEKKIAELSERYEHKTNECHEAWMSLTSANEQLEKVMMELNNKIYQARSLDQTVITQADCLKSITRKYENDKRHWATAIDSLQEKIEIMKREQSQLSQEAHECVEGIPELYKMVGGVQALVSQCEDLKQKYSEEQAKRKELYNHIQETKGNIRVFCRCRPLNTEETSTKSATIVDFDGAKDGELGVITGNNSKKSFKFDRVYTPKDGQVDVFADASPMVVSVLDGYNVCIFAYGQTGTGKTFTMEGTPQNRGVNYRTVEQLFEVARERRETISYNISVSVLEVYNEQIRDLLATSPGSKKLEIKQSSDGSHHVPGLVEANVENINEVWNVLQAGSNARSVGSNNVNEHSSRSHCMLSIMVKAKNLMNGDCTKSKLWLVDLAGSERLAKTDVQGERLKEAQNINRSLSALGDVIYALATKSSHIPYRNSKLTHLLQDSLGGDSKTLMFVQISPSEHDVSETLSSLNFATRVRGVELGPARKQVDTGEIQKLKAMVEKARQESRSKDESIKKMEENIQNLEGKNKGRDNSYRSLQEKNKDLQNQLDSVHNQSEKQYAQLQERLKSRDEICSNLQQKVKELECKLRERHQSDSAANNQKVKDLENNLKESEGSSLVWQQKVKDYENKLKESEGNSLVWQQKIKELEIKHKDEQSQEAVLLRQKIKELEMRLKEQEKHIQEMATTREFPEVANATPNEVKTCFKEDNFGNENMESNTNILRTSNRLKTKRHDSLNLNEMTRKKRASRSGETENNGDDPQMKEKRIRKSDPPKVFSRVVRPTRTASGSSSQVPVAQKRVIKREQQEVPVVKERDSKKKIWSR
Protein: Cell division protein kinase 5 (Q9DE44)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Cyclin-dependent kinase 5 activator
- Cellular tumor antigen p53
- Cyclin-dependent kinase 5 activator
- Protein phosphatase 1 regulatory subunit 1B
- Cyclin-dependent kinase 5 activator
- Dihydropyrimidinase-related protein 3
- Microtubule-associated protein.
- Cyclin-dependent kinase 5 activator.
- Cyclin-dependent kinase 5 activator
- Dihydropyrimidinase-like 2b.
Sequence:
MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEYCDQDLKKYFDSCNGDLDPEIVKSFMYQLLKGLAFCHSRNVLHRDLKPQNLLINRNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWQTMNKLPDYKPYPMYPATTSLVNVVPKLSSTGRDLLQNLLKCNPVQRISAEEALQHPYFADFCPP
Protein: Euchromatic histone lysine methyltransferase 1 (A0A8I6ABS0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
Interaction partners:
Sequence:
MAAADAEQAVLAKQETKQDCCMKTELLREDTLMAADEGSTEKQAGETPMAADGETNGSCEKSGDISHPNAPKHTQENTRASPQEGTNRVSRVAENGVSERDTEVGKQNHVTADDFMQTSVIGSNGYFLNKPALQGQPLRTPNTLNSSLPGHAAKTLPGGASKCRTPSALPQTPTTAPTVPGEGSADTEDRKPTASGTDVRVHRARKTMPKSILGLHAASKDHREVQDHKEPKEDINRNISECGRQQLLPTFPALHQSLPQNQCYMATTKSQTAAAVSRKKKRRMGTYSLVPKKKTKVLKQRTVIEMFKSITHSTVGAKGEKVLDDSALHVNGESLEMDSEEEDSEELEDEEDRGAEQAAAFPTEDSRTSKESMSETDRAAKMDGDSEEEQESPDTGEDEDGGDESDLSSESSIKKKFLKRRGKTDSPWIKPARKRRRRSRKKPSSMLGLANGPDVLETDGLHEVPLCSCRMETPKSREISTLANNQCMATESVDHELGRCTNSVVKYELMRPSNKAPLLVLCEDHRGRMVKHQCCPGCGYFCTAGNFMECQPESSISHRFHKDCASRVNNASYCPHCGEETSKAKEVTIAKADTTSTVTLAPGQEKSLAAEGRADTTTGSIAGAPEDEKSQSTVTQAPECFDPAGPAGFVRPTSGFSQGPGKETLESALIALDSEKPKKLRFHPKQLYFSARQGELQKVLLMLVDGIDPNFKMEHQSKRSPLHAAAEAGHVDICHMLVQAGANIDTCSEDQRTPLMEAAENNHLDAVKYLIKAGAQVDPKDAEGSTCLHLAAKKGHYDVVQYLLSNGQMDVNCQDDGGWTPMIWATEYKHVDLVKLLLSKGSDINIRDNEENICLHWAAFSGCVDIAEILLAAKCDLHAVNIHGDSPLHIAARENRYDCVVLFLSRDSDVTLKNKEGETPLQCASLNSQVWSALQMSKALQDSAPDKPVAVEKTVSRDIARGYERIPIPCVNAVDSELCPTNYKYVSQNCVTSPMNIDRNITHLQYCVCVDDCSSSTCMCGQLSMRCWYDKDGRLLPEFNMAEPPLIFECNHACSCWRNCRNRVVQNGLRARLQLYRTQDMGWGVRSLQDIPLGTFVCEYVGELISDSEADVREEDSYLFDLDNKDGEVYCIDARFYGNVSRFINHHCEPNLVPVRVFMSHQDLRFPRIAFFSTRLIQAGEQLGFDYGERFWDVKGKLFSCRCGSPKCRHSSAALAQRQASAAQEAQENGLPDTSSAAAADPL
Protein: Tyrosine 2,3-aminomutase (MfTAM) (EC 5.4.3.6) (Tyrosine ammonia-lyase) (EC 4.3.1.23) (B8ZV93)
Organism: Myxococcus fulvus
Function: Has aminomutase and, to a much lesser extent, ammonia-lyase activity. Primarily, catalyzes the rearrangement of L-tyrosine to S-beta-tyrosine, which is probably incorporated into secondary metabolite myxovalargin. The aminomutase activity exclusively produces S-beta-tyrosine.
Interaction partners:
Sequence:
MDIYAVAVGRVGVELDAAQLERVRATHLRVQGWGMEKYPMYGVNTGFGELINVIIPPQFKSDLQHNLLRSHAAGGGEPFPDEVVRAIMTVRINCLMKGYSGISPEALQLLATMLNRGIHPVIPMQGSLGASGDLAPLSHMALPLIGDGHVRKNGVTRPTMEVFQEEGLTPLKLGFKEGLALVNGTSAMTGAASLALYRARHLLRLSLLASADIVQAMNASTRPFSHTGNALKNHPGQVVIARLMRDLTQGTGLMRDHQDIMRAISERTSHSNDVEETEIYLQNAYSLRCMPQVLGVVLETLQMCQRFIEEEANSVNDNPVILDTPAETYHGANFHGQYVAMACDYLSIAVAEMGVLAERQLNRLLDPHINKPLPGFLAHAKTGLFCGFEGGQYLATSIASENLDLAAPSSIKSIPSNGQNQDIVSMGLIAARKTLALCENVGTILSVLMAALNQASHFTEAAKYSAPIRSIHEKLGKVAPRYEDERPMSTVIAQVRGVLLQEQGLALAQSLVNLDLTPDLSLEPRA
Protein: SH2B adapter protein 2 (C9JK89)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNGAGPGPAAAAPVPVPVPVPDWRQFCELHAQAAAVDFAHKFCRFLRDNPAYDTPDAGASFSRHFAANFLDVFGEEVRRVLVAGPTTRGAAVSAEAMEPELADTSALKAAPYGHSRSSEDVSTHAATKARVRKGFSLRNMSLCVVDGVRDMWHRRASPEPDAAAAPRTAEPRDKWTRRLRLSRTLAAKVELVDIQREGALRFMVADDAAAGSGGSAQWQKCRLLLRRAVAEERFRLEFFVPPK
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (D3ZTG5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MLSHGALLALWIALSVLQTGVAEQVKCNFTVLESKVSSLSASIQWRTFGSPCNFSLIYSSDTSGPLWCHPILIDNFTYGCDPKDLQAGTIYNFRIVSLDGEERSLVLQTDPLPPARLEVNPERTTSTTLQVRWTPSSGKVTWYEVQLFDQNNQKIQEVQVQESATWSQYTFLNLTAGSSYKIGITAVSGGKRSFPVYTNGSTGPSPVEDIGISPNPNSLLISWSRGPGNVEQFRLMLMDKGAIVQDTNVDKRDTSYAFRGLTPGHLYNVTIVTMASGLQNSRWKLGRTAPMEVSNLKVTSGGSLTSLNVKWQKPLGVIDSYSITLSHQGTVKESKTLPPRATEIQFKDLVPGRFYQVTIRCVSGELSAEKSAMGRTVPEKVSNLVSYNEIWMKSFAVNWTPPAGDWDHYRILLFNDSLVLLNTTVGKEETHFALEGLELIPGRQYEVEVIVESGNLRNSERCQGRTVPLAVLQLRIKQANETSLGITWRAPLGEWEKYTISLMDRELFVIHKSLSKDAKEYTFTNLMPGRNYKATVTSMSGDLKQSASIQGRTVPAQVTDLEVSNQGMTSSLFTNWTKALGDVEFYQVLLIHENVVVKNESVSSDSSWYSFRALRSGSLYSVVVTTVSGGIPSRQVVAEGRTVPSSVSGVTVNNSGRNDYLSVSWLPAPGEVHHYVVTLSHDSKVVQSLITAKFVSECSFSSLTPGRLYNVTITTKSGNYESHSFSEERTVPDKVQGISVSNSARSDYLKVSWVHATGDFDHYEVTIKNRDSFIQTKSIPKSENECVFARLVPGRLYSITVTTKSGQYEASEQGTGRTIPEPVKNLTLLNRSTEDLHVTWSRANGDVDQYEVQLLFNDMKVFPPIYLVNTATEYQFSALTPGRHYKILVLTISGDVQQPAFIEGLTVPSTVKNIHISANGATDRLTVTWSPGGGDVDSYVVSAFRQDEKVESHTLPKHGSEHTFHRLEAGATYRIAIVSVSGSLRNQIDVLGQTVPASVHGVVADNAYSSNSLTVSWQKALGMAERYDILLLSENGVLLSNTSEPATVKQHKFEDLTPGKKYKMQILTVSGGLFSKEVETEGRTVPAAVTNLRITENSSRHLSFSWTASEGELSWYNIFLYNPDKTLQERAQVDPLVQSFSFQNLLQGRMYKMVIVTHSGELSNESFIFGRTVPAAVNHLKGSNRNMTDSLWFSWSPASGDFDFYELILYNPNGTKKENWREKDVTEWRFQGLIPGRKYTLYVVTHSGDLSNKVTGEGRTAPSPPSLLSFADVANTSLAITWKGPPDWTDYNDFELQWLPGDALTVFNPYSSKKSEGRIVNGLRPGRSYQFSVKTVSGDSWKTYSKPISGSVRTKPDKIQNLHCRPQNSTAIACSWIPPDSDFDGYSIECRKMDTQEIEFSRKLEKEKSLLNIMMLVPHRRYLVSIKVQSAGVTSEVVEDSTITMIDRPPPPPPHIRVNEKDVLISKSSINFTVNCSWFSDTNGAVKYFAVVVREADSMDELRPEQQHPLPSYLEYRHNASIRVYQTNYFASKCAESPDPDRSSKSFNIKLGGEMDSLGGKCDPSQQKFCDGPLKPHTAYRISIRAFTQLFDEGLKEFTKPLYSDTFFSMPITTESEPLFGVIEGVSAGLFLIGMLVALVAFFICRQKASHSRERSSARLSIRRDRPLSVHLNLGQKGNRKTSCPIKINQFEGHFMKLQADSNYLLSKEYEDLKDVGRSQSCDIALLPENRGKNRYNNILPYDASRVKLCNVDDDPCSDYINASYIPGNNFRREYIATQGPLPGTKDDFWKMAWEQNVHNIVMVTQCVEKGRVKCDHYWPADQDPLYYGDLILQMVSESVLPEWTIREFKICSEEQLDAHRLLRHFHYTVWPDHGVPETTQSLIQFVRTVRDYINRSPGAGPTVVHCSAGVGRTGTFVALDRILQQLDSKDSVDIYGAVHDLRLHRVHMVQTECQYVYLHQCVRDVLRARKLRNEQENPLFPIYENVNPEYHRVHSLTLIPWGR
Protein: Collagen type XI alpha 2 chain (A0A8I6AUU9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MERCSRCHRLLLLLPLVLGLSAAPGWAGAPSVDVLRALRFPSLPDGVRKSKGVCPADVAYRVARPAQLSAPTRQLFPGGFPKDFSLLTVVRTRSGLQAPLLTLYSAQGVQQLGLELGRPVRFLYEDQRGRPQASAQPIFRGLSLADGKWHHVAVAVKGQSVTLIVDCKKRVTRPLPRSVHPVLDTHGVVIFGAHVLDDEVFEGDVQELLIVPGVQAAYQSCGQKDLECEREQRDGPQTQKPHRAQRSPKKEPARLHKPQNQEPQQQEQTDLQVPPTADSFQAEEYGEGGTEPPAGFYDYTYGYGDDYREETELGPALSAETDHTGAVAHGPRGLKGEKGEPAVLEPGMFVEGPPGPEGPAGLAGPPGIQGNPGPVGDPGERGPPGRAGLPGSDGPPGPPGTSLMLPFRFGSSGGDKGPVVAAQEAQAQAILQQARLALRGPPGPMGYTGRPGPLGQPGSPGLKGESGDLGPQGPRGPQGLTGPPGKAGRRGRAGADGARGMPGEPGVKGDRGFDGLPGLPGEKGQRGDTGAQGLPGPPGEDGERGDDGEIGPRGLPGESGPRGLLGPKGPPGIPGPPGVRGMDGPHGPKGSLGPQGEPGPPGQQGTPGTQGLPGPQGAIGPHGEKGPRGKPGLPGMPGSDGLPGHPGKEGPPGTKGNQGPSGPQGPLGYPGPRGVKGVDGIRGLKGHKGEKGEDGFPGFKGDIGVKGDRGEVGVPGSRGEDGPEGPKGRTGPTGDPGPTGLMGEKGKLGVPGLPGYPGRQGPKGSLGFPGFPGASGEKGARGLSGKSGPRGERGPTGPRGQRGPRGATGKSGAKGTSGGDGPHGPPGERGLPGPQGPNGFPGPKGPPGPAGKDGLPGHPGQRGEVGFQGKTGPPGPPGVVGPQGAAGESGPMGERGHPGPPGPPGEQGLPGTAGKDGTKGDPGPPGAPGKDGPAGLRGFPGERGLPGTAGGPGLKGNEGPAGPPGPAGSPGERGAAGSGGPIGPPGRPGPQGPPGAAGEKGVPGEKGPIGPTGRDGVQGPVGLPGPAGPPGVAGEDGDKGEVGDPGQKGTKGNKGEHGPPGPPGPIGPVGQPGAAGADGEPGARGPQGHFGAKGDEGTRGFNGPPGPIGLQGLPGPFGEKGETGDVGPMGPPGPPGPRGPAGPNGADGPQGPPGGVGNLGPPGEKGEPGESGSPGVQGEPGVKGPRGERGEKGESGQAGEAGPPGPKGPTGDDGPKGNPGPVGFPGDPGPPGEAGPRGQDGAKGSQGEDGEPGQPGSPGPTGENGPPGPLGKRGPAGTPGPEGRQGEKGAKGDPGAVGAPGKTGPVGPAGPAGKPGPDGLRGLPGSVGQQGRPGATGQAGPPGPVGPPGLPGLRGDAGAKGEKGHPGLIGLIGPTGEQGEKGDRGLPGPQGSPGQKGETGIPGASGPIGPGGPPGLPGPSGPKGAKGATGPAGPKGEKGVQGPPGHPGPPGEVIQPLPIQMPKKTRRSVDGSKLMQDEEATPTGGAPGSPAGLEEIFGSLDSLREEIEQMRRPTGTQDSPARTCQDLKLCHPELPDGEYWVDPNQGCARDAFRVFCNFTAGGETCVTPRDDVTQFSYVDSEGSPVGVVQLTFLRLLSVSAHQDVSYPCSGVSQDGPLKLRGANEDELSPETSPYVKEFRDGCQTQQGRTVLEVRTPVLEQLPVLDASFSDLGAPTRRGGVLLGPVCFMG
Protein: Histidinol-phosphate aminotransferase (EC 2.6.1.9) (Histidine transaminase) (EC 2.6.1.38) (Imidazole acetol-phosphate transaminase) (Q8R5Q4)
Organism: Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis)
Interaction partners:
- Imidazoleglycerol-phosphate dehydratase
- Histidine biosynthesis bifunctional protein HisIE
- Histidinol dehydrogenase
- Imidazole glycerol phosphate synthase subunit HisF
- Imidazole glycerol phosphate synthase subunit HisH
- 1-
- ATP phosphoribosyltransferase
- Prephenate dehydrogenase
- ATP phosphoribosyltransferase regulatory subunit
- Prephenate dehydratase
Sequence:
MIENLLREEIKGFKNYEVENVPYKYKMDANETPFELPEEVMKNIGDIVKSIHVNIYPDPTAEKLREELARYCSVTPKNIFVGNGSDEIIHLIMLAFVDKGDTVLYPHPSFAMYSIYSKIAGANEIAVNLNEDYTYNVERFAEAVERYKPKLVFLCNPNNPTGSVIDEEDIIRIIEKARGIVIVDEAYFEFYGKTLVPYIDRFENLIVLRTLSKAFGIAGLRVGYALSNGEIVKYLNLVKSPYNLNSLSQRIALEVLKSGVLKERVNYIINEREKLVKELNKINGIKVYPSHANFVLCKFENANDVHKRLVERGILVRNFSNVKGLEGTLRITVSSSDANDYLINALREILS
Protein: Sodium/myo-inositol cotransporter 2 (Na(+)/myo-inositol cotransporter 2) (Sodium-dependent glucose cotransporter) (Sodium/glucose cotransporter KST1) (Sodium/myo-inositol transporter 2) (SMIT2) (Solute carrier family 5 member 11) (Q8K0E3)
Organism: Mus musculus (Mouse)
Function: Involved in the sodium-dependent cotransport of myo-inositol (MI) with a Na(+):MI stoichiometry of 2:1. Exclusively responsible for apical MI transport and absorption in intestine. Can also transport D-chiro-inositol (DCI) but not L-fucose (By similarity). Exhibits stereospecific cotransport of both D-glucose and D-xylose (By similarity). May induce apoptosis through the TNF-alpha, PDCD1 pathway (By similarity). May play a role in the regulation of MI concentration in serum, involving reabsorption in at least the proximal tubule of the kidney (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9Z1F2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z1F2}. Apical cell membrane {ECO:0000250|UniProtKB:Q9Z1F2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Z1F2}. Note=Located on apical membrane of enterocytes (By similarity). Located on membrane of kidney brush border membrane vesicles (BBMVs) and apical membrane of proximal convoluted tubules (By similarity). {ECO:0000250|UniProtKB:Q28728, ECO:0000250|UniProtKB:Q9Z1F2}.
Interaction partners:
- Solute carrier family 2, facilitated glucose transporter member 5
Sequence:
MESATISPQPPQSDSLEAFPQKSMEPADIAVLVLYFLFVLAVGLWSTVRTKRDTVKGYFLAGGDMVWWPVGASLFASNVGSGHFIGLAGSGAAVGISVAAYELNGLFSVLMLAWVFLPIYIAGQVTTMPEYLRRRFGGNRISITLAVLYLFIYIFTKISVDMYAGAIFIQQSLHLDLYLAIVGLLAITALYTVAGGLAAVIYTDALQTVIMLIGAFILMGYSFAAVGGMEGLKDQYFLALASNRSENSSCGLPREDAFHIFRDPLTSDLPWPGILFGMSIPSLWYWCTDQVIVQRSLAAKNLSHAKGGSLMAAYLKVLPLFLMVFPGMVSRVLFPDQVACAHPDICQRVCSNPSGCSDIAYPKLVLELLPTGLRGLMMAVMVAALMSSLTSIFNSASTIFTMDLWNHIRPRASERELMIVGRIFVFALVLVSILWIPIVQASQGGQLFIYIQSISSYLQPPVAMVFIMGCFWKRTNEKGAFSGLILGLLLGLVRLILDFVYAQPRCDQPDDRPAVVKDVHYLYFSMILSFTTLITVVTVSWFTETPSKEMVSRLTWFTRHEPVAQKDSAPPETPLSLTLSQNGTTEAPGTSIQLETVQESTTKACGDGVSPRHSKVVRAILWLCGMEKNKEEPPSKAEPVIVSLEENPLVKTLLDVNCIVCISCAIFLWGYFA
Protein: Uncharacterized protein (Q38AC3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDRSETFKVFCERVEAFLGKGVGIDLVLKCMLGLTRLRMVNASDEATKEVYAGFAMAVINGRMLGNHFRYPSSFSLALRTFKAKEGPLFHWFLFGLSFLLRTFEQMTGDLNYYQMIIMRHWSRSRLSHTYWFFKSLSLTCLLLDEVLLLRLELRSPQWREKTSEERSSFLRRKVISVMRCLLDMCMYYQWVPWYNPYKTLQYCCVTASGFLGVYSGWGDVCDSLAASKARRVDSIKAD
Protein: CD209 antigen (C-type lectin domain family 4 member L) (Dendritic cell-specific ICAM-3-grabbing non-integrin 1) (DC-SIGN) (DC-SIGN1) (CD antigen CD209) (Q9NNX6)
Organism: Homo sapiens (Human)
Function: Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 6]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 7]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 8]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 9]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 10]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 11]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 12]: Secreted {ECO:0000305}.
Interaction partners:
- Intercellular adhesion molecule 2
- Intercellular adhesion molecule 3
- Inter-alpha-trypsin inhibitor heavy chain H4
- C-type lectin domain family 4 member M
- Lymphocyte-specific protein 1
- Butyrophilin subfamily 2 member A1
- Syncytin-1
- Mucin-1
- Integrin alpha-M
- Kinase suppressor of Ras 1
Sequence:
MSDSKEPRLQQLGLLEEEQLRGLGFRQTRGYKSLAGCLGHGPLVLQLLSFTLLAGLLVQVSKVPSSISQEQSRQDAIYQNLTQLKAAVGELSEKSKLQEIYQELTQLKAAVGELPEKSKLQEIYQELTRLKAAVGELPEKSKLQEIYQELTWLKAAVGELPEKSKMQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTRLKAAVGELPEKSKQQEIYQELTQLKAAVERLCHPCPWEWTFFQGNCYFMSNSQRNWHDSITACKEVGAQLVVIKSAEEQNFLQLQSSRSNRFTWMGLSDLNQEGTWQWVDGSPLLPSFKQYWNRGEPNNVGEEDCAEFSGNGWNDDKCNLAKFWICKKSAASCSRDEEQFLSPAPATPNPPPA
Protein: PRELI/MSF1 domain-containing protein (Q5A107)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Mitochondrial distribution and morphology protein 35
- PRELI/MSF1 domain-containing protein
Sequence:
MKLFESEHSFNYPWDQVTAANWQKYPNELASHVISVDILQREMINNNTTLRTERLIGCKQPIPKWLSFVVGGATVSYVREVSEVDLVNRTLVMKSMNLTMNNLLLVKETVIYKPDDELPHNKTVFHQSAEITAFASLSRLCDKLEDWSVERFGQNAKSGRLAFENVLNKLTLKWEENGIFENNKILQEVKNLSI
Protein: Transmembrane protein 223 (Q9CQE2)
Organism: Mus musculus (Mouse)
Function: Mitochondrial ribosome-associated protein involved in the first steps of cytochrome c oxidase complex (complex IV) biogenesis. Stimulates the translation of MT-CO1 mRNA and is a constituent of early MT-CO1 assembly intermediates.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:A0PJW6}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MVASVPLRNVSHLLSVLRSQNVPRYLQNGVPRDVLLFRHERGRFFAILGLFCAGQGIFWTSLAVAALSRPLSRVPAEAPNRSYQDLRSALWRYGLAVGCGTMGVLVLGAGLLYSLRSVRSVMLLAGGQQVTLTTYAPFGLGTCFTVPLNQISCMAHRGEVPAMLPLKVKGRRFYFLLDKAGHFPNTQLFDNTVGAYRSL
Protein: Cold-inducible RNA-binding protein (BFCIRP) (Glycine-rich RNA-binding protein CIRP) (Q9PTX2)
Organism: Aquarana catesbeiana (American bullfrog) (Rana catesbeiana)
Function: Cold-inducible mRNA binding protein. Acts cooperatively with elavl1/elrA to stabilize AU-rich element (ARE)-containing mRNAs by binding to them and inhibiting their deadenylation. Essential for embryonic gastrulation and neural development, acting to maintain the expression of a set of adhesion molecules, and cell movement during embryogenesis. Required for pronephros development (By similarity). May play a role in hibernation.
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9DED4}. Cytoplasm {ECO:0000250|UniProtKB:Q9DED4}. Note=Shuttles between the nucleus and cytoplasm. Predominantly cytoplasmic in oocytes. Translocates from the nucleus to the cytoplasm upon arginine methylation (By similarity). {ECO:0000250|UniProtKB:Q9DED4}.
Interaction partners:
Sequence:
MSCDEGKLFVGGLSFDTDEQCLETVFSKYGQIQEVVVVKDRETKRSRGFGFVTFENCEDAKDAMAGMNGKTVDGRQIRVDQAGKSSNDRRGGYRGGSSGGGRGFFRGGRGRGGGGYGGSSRFDNRSGGGYGGWIPDYYSSGRESSYGDRSAGGRSYRDSYDSYG
Protein: Secretin/TonB short N-terminal domain-containing protein (Q9I0P7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}.
Interaction partners:
- Major facilitator superfamily
- Probable major facilitator superfamily
- Probable sigma-70 factor, ECF subfamily
- Probable oxidoreductase
- Probable transcriptional regulator
- AAA family ATPase
- DNA-binding protein
- Probable sigma-70 factor, ECF subfamily
- Secretin/TonB short N-terminal domain-containing protein
- Transporter
Sequence:
MPDVRLSSRSLTPVLCAVGLACALQGEVQAADGGPRDVATAPRVFDIAPGELAEVLLNIVRQGHVPIAFDQRLVAGLRGPDIRGRLSVEDALRRALAGSGLAYAQDESGAFVLRRGQAPVQETRGAAVAPTLSTVVVTGTRKSDVRAQDSLSPIDVVSATQLRSSGAVDLRDALVKLLPSLTRQAQPFNASALTHTQSLRGLSPNHVLVLVNGKRRHETANLNISGGLEKGSTGVDLDTIPINAIERVEVLRDGASAQYGSDAIAGVINVILKSADSGGSAAADVGQTGDGDGFTHGGGGNIGLAFGDSGFVNLTAEYREQERTMRSGIDERTGRRDNISMGDPAFHRQSLALNSGFGLGDDIEVYGFGTYTRRKASSAANYRLASVAPTLYPDGFTPRPNSDEDDYAFLAGVRGERLLDAWHWDLSSGYGADRPDIGMTQSVNAAIYRETGNSPRSFDLARYRNSQWTSNLDLGREFELDFLAAPLALSLGAEYRRESYRIDAGDPASYYSGGAESLAGLSPLSEGQWSRHAWASYLDLGTSLTPAWEVDVAVRHEKFSDFGSTTNGKFATRYQFDPRVALRASVSSGFRAPSLVQEHYTGLSVGPTIALGLLAANSPAAKMLGADELQPEKSTSFNLGLVLSPWENVGLNIDAYQISIRDRIVDSATYSGQEAIDALAAAGISLPASASTVSTHYLANGADTRTRGVDITGHYLVALGEYGQVDWELSANFNRTTLRKNHRGANGEPLLNAQQVAWITSSTPRSQVSLGGTWSRQDWEVSLRLTRYGRTSSELDYTVGPDAWSTEKFNHFVNDPKYITDIAARYRLSADLTLTAGADNLFDVRPDKLPAQNTTYGDVLRYDTYASQIGFNGAFYYLRAAYRF
Protein: Sodium/myo-inositol cotransporter (Na(+)/myo-inositol cotransporter) (Sodium/myo-inositol transporter 1) (SMIT1) (Solute carrier family 5 member 3) (P53794)
Organism: Homo sapiens (Human)
Function: Electrogenic Na(+)-coupled sugar symporter that actively transports myo-inositol and its stereoisomer scyllo-inositol across the plasma membrane, with a Na(+) to sugar coupling ratio of 2:1 (By similarity). Maintains myo-inositol concentration gradient that defines cell volume and fluid balance during osmotic stress, in particular in the fetoplacental unit and central nervous system (By similarity). Forms coregulatory complexes with voltage-gated K(+) ion channels, allosterically altering ion selectivity, voltage dependence and gating kinetics of the channel. In turn, K(+) efflux through the channel forms a local electrical gradient that modulates electrogenic Na(+)-coupled myo-inositol influx through the transporter. Associates with KCNQ1-KCNE2 channel in the apical membrane of choroid plexus epithelium and regulates the myo-inositol gradient between blood and cerebrospinal fluid with an impact on neuron excitability (By similarity). Associates with KCNQ2-KCNQ3 channel altering ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation. Provides myo-inositol precursor for biosynthesis of phosphoinositides such as PI(4,5)P2, thus indirectly affecting the activity of phosphoinositide-dependent ion channels and Ca(2+) signaling upon osmotic stress.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q9JKZ2}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q9JKZ2}; Multi-pass membrane protein {ECO:0000255}. Note=Colocalizes with KCNQ1 at the apical membrane of choroid plexus epithelium. {ECO:0000250|UniProtKB:Q9JKZ2}.
Interaction partners:
- Sodium- and chloride-dependent betaine transporter
- Nuclear factor of activated T-cells 5
- Aldo-keto reductase family 1 member B1
- Proton myo-inositol cotransporter
Sequence:
MRAVLDTADIAIVALYFILVMCIGFFAMWKSNRSTVSGYFLAGRSMTWVAIGASLFVSNIGSEHFIGLAGSGAASGFAVGAWEFNALLLLQLLGWVFIPIYIRSGVYTMPEYLSKRFGGHRIQVYFAALSLILYIFTKLSVDLYSGALFIQESLGWNLYVSVILLIGMTALLTVTGGLVAVIYTDTLQALLMIIGALTLMIISIMEIGGFEEVKRRYMLASPDVTSILLTYNLSNTNSCNVSPKKEALKMLRNPTDEDVPWPGFILGQTPASVWYWCADQVIVQRVLAAKNIAHAKGSTLMAGFLKLLPMFIIVVPGMISRILFTDDIACINPEHCMLVCGSRAGCSNIAYPRLVMKLVPVGLRGLMMAVMIAALMSDLDSIFNSASTIFTLDVYKLIRKSASSRELMIVGRIFVAFMVVISIAWVPIIVEMQGGQMYLYIQEVADYLTPPVAALFLLAIFWKRCNEQGAFYGGMAGFVLGAVRLILAFAYRAPECDQPDNRPGFIKDIHYMYVATGLFWVTGLITVIVSLLTPPPTKEQIRTTTFWSKKNLVVKENCSPKEEPYKMQEKSILRCSENNETINHIIPNGKSEDSIKGLQPEDVNLLVTCREEGNPVASLGHSEAETPVDAYSNGQAALMGEKERKKETDDGGRYWKFIDWFCGFKSKSLSKRSLRDLMEEEAVCLQMLEETRQVKVILNIGLFAVCSLGIFMFVYFSL