wanglab/gogpt-training-data huggingface dataset:
Protein: Glucosaminyl (N-acetyl) transferase 1 (Q64165)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- ST3 beta-galactoside alpha-2,3-sialyltransferase 1
- alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase
- C1GALT1-specific chaperone 1
- Hexosyltransferase
- Beta-1,4-galactosyltransferase
- Polypeptide N-acetylgalactosaminyltransferase.
- Polypeptide N-acetylgalactosaminyltransferase 5
- Polypeptide N-acetylgalactosaminyltransferase
- Polypeptide N-acetylgalactosaminyltransferase 1
Sequence:
MLRNLFRRRLFSYPTKYYFMVLVLSLITFSVVRIHQKPEFVSVSHLELSGDDPNSNVNCTKVLQGDPEEIQKVKLEILTVQFKKRPRRTPHDYINMTRDCASFIRTRKYIMEPLTKEEVGFPIAYSIVVHHKIDMLDRLLRAIYMPQNFYCIHVDRKAEESFLAAVQGIASCFDNVFVASQLESVVYASWSRVKADLNCMKDLYRMNANWKYLINLCGMDFPIKTNLEIVRKLKSFTGENSLETEKMPPNKEERWKKRYTVVDGKLTNTGVVKAQPPLKTPLFSGSAYFVVTREYVGYVLENKNIQKFMEWAQDTYSPDEFLWATIQRIPEVPGSLPSSHKYDLSDMNAVARFVKWQYFEGDVSNGAPYPPCSGVHVRSVCVFGVGDLSWMLRKHHFFANKFDMDVDPFALQCLEEHLRHKALETLER
Protein: Speriolin (Spermatogenesis and centriole-associated protein 1) (Spermatogenesis-associated protein 15) (Spermatogenic cell-specific Cdc20-binding protein) (Q76KD6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Colocalizes with the centrosomal pericentrin protein PCNT1 (By similarity). Located in the connecting piece of sperm. {ECO:0000250, ECO:0000269|PubMed:20542897}.
Interaction partners:
- Outer dense fiber protein 1
- Cell division cycle protein 20 homolog
- Centlein
- Cell division cycle protein 27 homolog
- Pericentrin
- Nuclear pore complex protein Nup85
Sequence:
MSLLTNYEGLRHQIERLVRENEELKKLVRLIRENHELKSAIKTQAGGLGISGFTSGLGEATAGLSSRQNNGVFLPPSPAVANERVLEEVGIMALAPLAEMLTSLQPSATPGSLMSPLTGTLSTLLSGPAPTSQSSPLTSFLTSPIAGPLTGTLASSLGLPSTGTLTPSSLVAGPVAMSQSSPLIAPVMGTVAVSLSSPLLSSTATPPGVSQNLLANPMSNLVLPEAPRLRLAEPLRGGPTGPQSPACVVPTATTKVPLSTEPPQSTQDPEPLSMAFAGAPLQTSTPIGAMGTPAPKTAFSFNTSDTQAQPSAAQEQVVPASVPTSPTTSPTVTVLASAPALAPQVATSYTPSSTTHIAQGAPHPPSRMHNSPTQNLPVPHCPPHNAHSPPRTSSSPASVNDSRGPRTTEPSTKSMMEVERKLAHRKTSKFPENPRESKQLAWERLVGEIAFQLDRRILSSIFPERVRLYGFTVSNIPEKIIQASLNPSDHKLDEKLCQRLTQRYVSVMNRLQSLGYNGRVHPALTEQLVNAYGILRERPELAASEGGPYTVDFLQRVVVETVHPGMLADALLLLSCLSQLAHDDGKPMFIW
Protein: Lnk, isoform E (A0A0B4LHS0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGGNSTGANTSAFSAGGYIGPTSASSHHSLGTSSAAAAAAAGSDLIPAPIGTGNAMGVSSYAYGGTSWEEFCERHARVAASDFAKACITYINGNLPPEEARNIQHRSFAQKFVESFSAHYDTEFFKRRSTLKSGAGSLDFEEEHEVPKLLSKSLLRRLSFKGLRKGKISLLQAFFHKNSDDLDGSGGSGKQSKTKLAKIVVECRKEGTVNNLTPESLDQPTGSQKWEKCRLVLVKAVGGYMLEFYTPHKATKPRSGVFCFLISEARETTALEMPDRLNTFVLKADNNMEYVIEAESAEEMRSWLATIRYCMRTPPTQQPTIESDGVMASAMQTSPTLPSPNPIGGIQNPQYQQQRGSNGNLVGGGAPLTSSLSADSALGQGGATSASELNVINELGTSPTSGPPDIPVRPHRGEQRLSASSNFDGIEGTENDADVADLTAEMSVFPWFHGTLTRSEAARMVLHSDAAGHGYFLVRQSETRRGEFVLTFNFQGRAKHLRLTISEKGQCRVQHLWFPSIQEMLEHFRHNPIPLESGGTSDVTLTEWVHSHSRLNDPTTAANHDSGQLNDLSTNGNGNGNGNGYDNGQGSSTASNAAGGTASGAAGGGHPSPRHVR
Protein: Large ribosomal subunit protein eL18 (60S ribosomal protein L18) (P12001)
Organism: Rattus norvegicus (Rat)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q07020}. Cytoplasm {ECO:0000250|UniProtKB:Q07020}. Rough endoplasmic reticulum {ECO:0000250|UniProtKB:Q95342}. Note=Detected on cytosolic polysomes (By similarity). Detected in ribosomes that are associated with the rough endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q07020, ECO:0000250|UniProtKB:Q95342}.
Interaction partners:
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL27
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL13
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MGVDIRHNKDRKVRRKEPKSQDIYLRLLVKLYRFLARRTNSTFNQVVLKRLFMSRTNRPPLSLSRMIRKMKLPGRENKTAVVVGTITDDVRILEVPKLKVCALRVSSRARSRILKAGGKILTFDQLALESPKGRGTVLLSGPRKGREVYRHFGKAPGTPHSHTKPYVRSKGRKFERARGRRASRGYKN
Protein: Ribosomal protein S6 kinase (EC 2.7.11.1) (D4AE24)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Serine/threonine-protein kinase mTOR
- Regulatory-associated protein of mTOR
- 3-phosphoinositide-dependent protein kinase 1
- RAC-gamma serine/threonine-protein kinase
- Small ribosomal subunit protein eS6
- RAC-beta serine/threonine-protein kinase
- RAC-alpha serine/threonine-protein kinase
- Ribosomal protein S6 kinase beta-1
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Target of rapamycin complex subunit LST8
Sequence:
MAAVFDLDLETEEGSEGEGEPEFNPADVCPLGELRAAGLETVGHYEEVELTESSVNLGPERIGPHCFELLSVLGKGGYGKVRKVQGTNLGKIYAMKVLRKAKIVCSAKDTAHTRAERNILESVKHPFIVELAYAFQTGGKLYLILECLSGGELFTHLEREGIFLEDTACFYLAEITLALGHLHSQGIIYRDLKPENIMLNSQGHIKLTDFGLCKESIHEGAITHTFCGTIEYMAPEILVRIGHNRAVDWWSLGALMYDMLTGSPPFTAENRKKTMDKIIKGKLVLPPYLTPDARDLAKKFLKRNPTHRIGGGPGDAADVQRHPFFRHINWDDLLAHRVDPPFRPSLQSEEDVSQFDVRFTRQTPVDSPDDTALSESANQAFLGFTYVAPSVLDSIKEGFSFQPKLRSPRRLNSSPRTPISPLKFSPFEGFRPSPGPPEPMEPSLPPLLPPPSSPPPTSTAPLPIRPPSGTKKSKKGRGRPGR
Protein: One cut domain family member (Q6NYT7)
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:
MNAQLSMENIGDLHGVSHEPVHSAADLMTGDSAHHRSHRSSLSAHARSMGMASILDSGDYHHHRPPEHPGLATHLHPAMSMACEAPPGMSMSSTYTTLTPLQPLPPISTVSDKFPHHHHHHHHHHHHPHQRIPGNVSGSFTLMRDDRGLAPMNNLYSPYHKDVASMGQSLSPLSGSGLSGIHNSQQGLPPYAHPGATMPAEKMLTPNGFEAHHPAMLARHGEQHMSASSASMVPINVIHHHPHAHLNAQGHGQVLGSTREQNHSSVPGSQLNNGSSSGQMEEVNTKEVAQRITTELKRYSIPQAIFAQRVLCRSQGTLSDLLRNPKPWSKLKSGRETFRRMWKWLQEPEFQRMSALRLAACKRKEQEHGKGERGNISKKPRLVFTDVQRRTLHAIFKENKRPSKELQITISQQLGLELATVSNFFMNARRRSLDKWLDDGSSNSANSSSSSTCTKA
Protein: Zinc finger CCCH domain-containing protein 2 (AtC3H2) (Protein SOMNUS) (SOM) (Tandem CCCH Zinc Finger protein 4) (AtTZF4) (Q9ZWA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription repressor that functions as negative regulator of phytochrome-mediated promotion of seed germination. Inhibits seed germination by regulating the expression of gibberellic acid (GA) and abscisic acid (ABA) metabolic genes. Does not regulate the expression of the DELLA genes RGA and RGA1. Activated by PIL5, a phytochrome-interacting basic helix-loop-helix transcription factor. Represses directly JMJ20 and JMJ22 expression in the absence of red light (R) and in far-red (FR) conditions.
Subcellular location: Nucleus {ECO:0000269|PubMed:18487351}.
Interaction partners:
- tRNA-dihydrouridine
- Zinc finger CCCH domain-containing protein 17
- Zinc finger CCCH domain-containing protein 36
- Zinc finger CCCH domain-containing protein 14
- Zinc finger CCCH domain-containing protein 15
- Zinc finger CCCH domain-containing protein 59
- GDSL esterase/lipase At5g45920
- Zinc finger CCCH domain-containing protein 37
- Zinc finger CCCH domain-containing protein 43
- Zinc finger CCCH domain-containing protein 68
Sequence:
MDVVCTEHQMRKPTVEIPPRKLLLSSKSFPSDSSSPRSPRKHNWNKSNKITSEHEEDNEDNNRENKEYCYDSDSDDPYASDHFRMFEFKIRRCTRSRSHDWTDCPFAHPGEKARRRDPRRFQYSGEVCPEFRRGGDCSRGDDCEFAHGVFECWLHPIRYRTEACKDGKHCKRKVCFFAHSPRQLRVLPPENVSGVSASPSPAAKNPCCLFCSSSPTSTLLGNLSHLSRSPSLSPPMSPANKAAAFSRLRNRAASAVSAAAAAGSMNYKDVLSELVNSLDSMSLAEALQASSSSPVTTPVSAAAAAFASSCGLSNQRLHLQQQQPSSPLQFALSPSTPSYLTNSPQANFFSDDFTPRRRQMNDFTAMTAVRENTNIEDGSCGDPDLGWVNDLLT
Protein: High-affinity choline transport protein (P0ABC9)
Organism: Escherichia coli (strain K12)
Function: High-affinity uptake of choline driven by a proton-motive force.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- HTH-type transcriptional regulator BetI
- Oxygen-dependent choline dehydrogenase
- Betaine aldehyde dehydrogenase
- Proline/betaine transporter
Sequence:
MTDLSHSREKDKINPVVFYTSAGLILLFSLTTILFRDFSALWIGRTLDWVSKTFGWYYLLAATLYIVFVVCIACSRFGSVKLGPEQSKPEFSLLSWAAMLFAAGIGIDLMFFSVAEPVTQYMQPPEGAGQTIEAARQAMVWTLFHYGLTGWSMYALMGMALGYFSYRYNLPLTIRSALYPIFGKRINGPIGHSVDIAAVIGTIFGIATTLGIGVVQLNYGLSVLFDIPDSMAAKAALIALSVIIATISVTSGVDKGIRVLSELNVALALGLILFVLFMGDTSFLLNALVLNVGDYVNRFMGMTLNSFAFDRPVEWMNNWTLFFWAWWVAWSPFVGLFLARISRGRTIRQFVLGTLIIPFTFTLLWLSVFGNSALYEIIHGGAAFAEEAMVHPERGFYSLLAQYPAFTFSASVATITGLLFYVTSADSGALVLGNFTSQLKDINSDAPGWLRVFWSVAIGLLTLGMLMTNGISALQNTTVIMGLPFSFVIFFVMAGLYKSLKVEDYRRESANRDTAPRPLGLQDRLSWKKRLSRLMNYPGTRYTKQMMETVCYPAMEEVAQELRLRGAYVELKSLPPEEGQQLGHLDLLVHMGEEQNFVYQIWPQQYSVPGFTYRARSGKSTYYRLETFLLEGSQGNDLMDYSKEQVITDILDQYERHLNFIHLHREAPGHSVMFPDA
Protein: Trace amine-associated receptor 8 (TaR-8) (Trace amine receptor 8) (G-protein coupled receptor 102) (Trace amine receptor 5) (TaR-5) (Q969N4)
Organism: Homo sapiens (Human)
Function: Orphan receptor. Could be a receptor for trace amines. Trace amines are biogenic amines present in very low levels in mammalian tissues. Although some trace amines have clearly defined roles as neurotransmitters in invertebrates, the extent to which they function as true neurotransmitters in vertebrates has remained speculative. Trace amines are likely to be involved in a variety of physiological functions that have yet to be fully understood.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25391046}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTSNFSQPVVQLCYEDVNGSCIETPYSPGSRVILYTAFSFGSLLAVFGNLLVMTSVLHFKQLHSPTNFLIASLACADFLVGVTVMLFSMVRTVESCWYFGAKFCTLHSCCDVAFCYSSVLHLCFICIDRYIVVTDPLVYATKFTVSVSGICISVSWILPLTYSGAVFYTGVNDDGLEELVSALNCVGGCQIIVSQGWVLIDFLLFFIPTLVMIILYSKIFLIAKQQAIKIETTSSKVESSSESYKIRVAKRERKAAKTLGVTVLAFVISWLPYTVDILIDAFMGFLTPAYIYEICCWSAYYNSAMNPLIYALFYPWFRKAIKLILSGDVLKASSSTISLFLE
Protein: Candida glabrata strain CBS138 chromosome A complete sequence (Q6FXZ1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
Sequence:
MTLSFSIFLLLLATIQAFPVYRKREIVTRMHTASTTNTVTDFYSTTTEVIIAPTVEFIVSGSVTFTTTLYPEGVNPTAVASTITTIQKNVAPTPQPDNSGDNNSKNNSNNSDGNSASQNNSENSSNSNNNSDNNNSDNNNSDNNNSDNNNSDNSNGNNSNNSNNSNNSNNSNNSNNSNNSNNSNNSNNSNNSNNNNNDNSNNNNNNNNNNNNSGSQSSKMSSSTSSSSSKTITLSPTASSLKSSSSSTTTSSVSSVSNTVTFSKSSSAESTSTTTITTTEWDTSYTTTFTTISGSSGINSATKTVSSSSKVSNSDSPTSSTSPSGLLKGVPHSLTYSPYNNDGSCKSADQVFSDLSQIKAKGVSNVRIYGTDCNSLGTVQPAAAKLGIKINQGLWITAAGVDSLDAGLQLLINYGKTNGWDIFNYITIGNEAIHSDYCSVEQLIAKIKSVKQALKDAGYSGQVTTSEPPVVFENSPDLCTQSGIDFVGINAHAYFDQYASAQTAGSFVKGQVQLIQNVCGTNNVVVTETGYPSAGKQNGNNIPSPENQRIAIQQILDEMNGQVTVLSSFDDMWKNPGPYGIEQSFGIIDILA
Protein: Basigin, isoform G (Q7KTJ7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Astrocytic leucine-rich repeat molecule
- G-protein coupled receptor moody
Sequence:
MEAKFLASALSFLSIFLAIYAQSLANDLSKESTEFEESPTIYYGDPVVNLGQPFSITCIIPITDQIHWLKNGEPITRHNLRHGRDDHAYVLSESAIEGEKHKIEAHLSVRHALKVHEGRYQCNRRRGSYILHVRDPKGVGAGAGEPTESGYQTIDELTPNSADDFFTRAWLEQQQQQQQLPHQSHKLHKSHLGYGNASLSGSQPWHPSAGGGGIHRVYSATPPDFPPPRLNLLEQTVAPPEPPTILYNPNPTHPTASATATETSVLLTTAHHHAHHQQQLQQQSQHTLNAFQLPLPPRPNPGQNERYQTYAPHYVPPVVVSGAGAGAGADPGAGASGEQTTISAATSTRAMMGGGGGVAGAGFSAGASGPMLGAGGHMLMGGQGHQVHLQHQTLLPVKMDKLVPNYDNAEHQMKFYDIRSPLVLSCNVKDGTPGGVLIWKKNGTAVTDVPSLRGRFKLIADENKFIIDKTDTNDDGKYSCEFDGVSKEIEVIARVVVRVPSNTAVVEGEKMSVTCSVVGTKPELTWTFANVTLTNATDRFILKPDDNGVPNAILTLDNVTLDDRGEYKCIGRNAANVYGGNTTTPASDVTTVRVKGKFAALWPFLGICAEVLILCIIILIYEKRRNKSELEESDTDPQEQKKKRRNYD
Protein: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase) (GFAT) (Glucosamine-6-phosphate synthase) (Hexosephosphate aminotransferase) (L-glutamine--D-fructose-6-phosphate amidotransferase) (P17169)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source.
Subcellular location: Cytoplasm.
Interaction partners:
- Bifunctional protein GlmU
- Phosphoglucosamine mutase
- Glucosamine-6-phosphate deaminase
- Glucose-6-phosphate isomerase
- N-acetylglucosamine-6-phosphate deacetylase
- Glutamate synthase large chain
- RNase adapter protein RapZ
- Glutamine synthetase
- Carbamoyl phosphate synthase large chain
- Carbamoyl phosphate synthase small chain
Sequence:
MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAEEHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFVSETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLVIGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQYDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILACGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGLRLSKELGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKLSRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIALEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRARGGQLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPRNLAKSVTVE
Protein: Hyaluronidase (EC 3.2.1.35) (Q76HN0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
LCLIKYNLAVNLKVFQMVGSPRLKDRRQNVVIFYANKLGSYPWYTSEGVPINGGLPQNTSLQVHLEKAYQDINYYIPSENFSGLAVIDWEYWRPQWARNWNTKDIYRQKSRTLISDMKENISTADIEYLAKATFEKSAKAFMEETIKLGIKSRPKGFWGYYLYPDCHNYNFYATNYTGSCPEEEVLRNNDLSWLWNSSTALYPAVSIRKSFADSENTLHFSQFRVRESLRISTMTSHDYALPVFVYTRLGYKEEPLLFLSKQDLIS
Protein: Heat shock protein SSA4 (P22202)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm.
Interaction partners:
- Heat shock protein SSA3
- Protein SIS1
- ATP-dependent molecular chaperone HSP82
- Heat shock protein 104
- Mitochondrial protein import protein MAS5
- J domain-containing protein APJ1
- Heat shock protein STI1
- Heat shock protein 26
- ATP-dependent molecular chaperone HSC82
- Heat shock protein 78
Sequence:
MSKAVGIDLGTTYSCVAHFANDRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQAAMNPHNTVFDAKRLIGRKFDDPEVTNDAKHYPFKVIDKGGKPVVQVEYKGETKTFTPEEISSMILTKMKETAENFLGTEVKDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKSQKEHNVLIFDLGGGTFDVSLLSIDEGVFEVKATAGDTHLGGEDFDSRLVNFLAEEFKRKNKKDLTTNQRSLRRLRTAAERAKRTLSSSAQTSIEIDSLFEGIDFYTSITRARFEELCADLFRSTLEPVEKVLADSKLDKSQIDEIVLVGGSTRIPKVQKLVSDFFNGKEPNRSINPDEAVAYGAAVQAAILTGDQSSTTQDLLLLDVAPLSLGIETAGGIMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERTRTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVSAVEKGTGKSNKITITNDKGRLSKEDIDKMVAEAEKFKAEDEQEAQRVQAKNQLESYAFTLKNSVSENNFKEKVGEEDARKLEAAAQDAINWLDASQAASTEEYKERQKELEGVANPIMSKFYGAAGGAPGAGPVPGAGAGPTGAPDNGPTVEEVD
Protein: Manganese-exporting P-type ATPase (EC 7.2.2.22) (Cation-transporting P-type ATPase CtpC) (Metal-transporting ATPase Mta72) (P9WPT5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: High affinity, slow turnover Mn(2+) transporting ATPase, which is required for virulence. Controls the Mn(2+) cytoplasmic quota and is involved in the uploading of Mn(2+) into secreted metalloproteins. Required for tolerance to Zn(2+) and oxidative stress. Plays a crucial role in the ability to resist zinc poisoning in human macrophages. Shows a preference for Mn(2+), but Zn(2+), Co(2+) and Cu(2+) can act as alternative substrates although at slower turnover rates.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23482562}; Multi-pass membrane protein {ECO:0000305|PubMed:23482562}.
Interaction partners:
- Conserved protein
- Conserved protein
Sequence:
MTLEVVSDAAGRMRVKVDWVRCDSRRAVAVEEAVAKQNGVRVVHAYPRTGSVVVWYSPRRADRAAVLAAIKGAAHVAAELIPARAPHSAEIRNTDVLRMVIGGVALALLGVRRYVFARPPLLGTTGRTVATGVTIFTGYPFLRGALRSLRSGKAGTDALVSAATVASLILRENVVALTVLWLLNIGEYLQDLTLRRTRRAISELLRGNQDTAWVRLTDPSAGSDAATEIQVPIDTVQIGDEVVVHEHVAIPVDGEVVDGEAIVNQSAITGENLPVSVVVGTRVHAGSVVVRGRVVVRAHAVGNQTTIGRIISRVEEAQLDRAPIQTVGENFSRRFVPTSFIVSAIALLITGDVRRAMTMLLIACPCAVGLSTPTAISAAIGNGARRGILIKGGSHLEQAGRVDAIVFDKTGTLTVGRPVVTNIVAMHKDWEPEQVLAYAASSEIHSRHPLAEAVIRSTEERRISIPPHEECEVLVGLGMRTWADGRTLLLGSPSLLRAEKVRVSKKASEWVDKLRRQAETPLLLAVDGTLVGLISLRDEVRPEAAQVLTKLRANGIRRIVMLTGDHPEIAQVVADELGIDEWRAEVMPEDKLAAVRELQDDGYVVGMVGDGINDAPALAAADIGIAMGLAGTDVAVETADVALANDDLHRLLDVGDLGERAVDVIRQNYGMSIAVNAAGLLIGAGGALSPVLAAILHNASSVAVVANSSRLIRYRLDR
Protein: Hematopoietic progenitor cell antigen CD34 (CD antigen CD34) (Q64314)
Organism: Mus musculus (Mouse)
Function: Possible adhesion molecule with a role in early hematopoiesis by mediating the attachment of stem cells to the bone marrow extracellular matrix or directly to stromal cells. Could act as a scaffold for the attachment of lineage specific glycans, allowing stem cells to bind to lectins expressed by stromal cells or other marrow components. Presents carbohydrate ligands to selectins (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- L-selectin
- Fibronectin
- Endoglin
- Myeloid cell surface antigen CD33
- Platelet endothelial cell adhesion molecule
- E-selectin
- Receptor-type tyrosine-protein phosphatase C
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- Thy-1 membrane glycoprotein
- 5'-nucleotidase
Sequence:
MQVHRDTRAGLLLPWRWVALCLMSLLHLNNLTSATTETSTQGISPSVPTNESVEENITSSIPGSTSHYLIYQDSSKTTPAISETMVNFTVTSGIPSGSGTPHTFSQPQTSPTGILPTTSDSISTSEMTWKSSLPSINVSDYSPNNSSFEMTSPTEPYAYTSSSAPSAIKGEIKCSGIREVRLAQGICLELSEASSCEEFKKEKGEDLIQILCEKEEAEADAGASVCSLLLAQSEVRPECLLMVLANSTELPSKLQLMEKHQSDLRKLGIQSFNKQDIGSHQSYSRKTLIALVTSGVLLAILGTTGYFLMNRRSWSPTGERLGEDPYYTENGGGQGYSSGPGASPETQGKANVTRGAQENGTGQATSRNGHSARQHVVADTEL
Protein: Phosphatidylcholine transfer protein (PC-TP) (START domain-containing protein 2) (StARD2) (StAR-related lipid transfer protein 2) (P53809)
Organism: Rattus norvegicus (Rat)
Function: Lipid transfer protein that promotes intermembrane transfer of phosphatidylcholines but no other phospholipids. Binds a single lipid molecule. May play a role in hepatocellular selection and transport of phosphatidylcholines during bile formation.
Subcellular location: Cytoplasm.
Interaction partners:
- Acyl-coenzyme A thioesterase 13
- StAR-related lipid transfer protein 4
- STAR-related lipid transfer
- StAR-related lipid transfer protein 3
Sequence:
MAGPAAHFSDEQFREACAELQKPALTGADWQLLVEASGITIYRLLDQSTGLYEYKVFGVLESCIPSLLADVYMDLDYRKKWDQYVKELYEKSFDGQMVAYWEVKYPFPLSNRDYVYTRQRRDLDVDGRKIYVVLAQNISVPQFPEKSGVIRVKQYKQSLAIESDGKKGSRVFMYYFDNPGGQIPSWLINWAAKNGVPSFLKDMVKACQNYHKKT
Protein: Crk-like protein (P47941)
Organism: Mus musculus (Mouse)
Function: May mediate the transduction of intracellular signals.
Interaction partners:
- E3 ubiquitin-protein ligase CBL
- CRK SH3-binding GNRP
- Breast cancer anti-estrogen resistance protein 1
- Paxillin
- Dedicator of cytokinesis protein 1
- Signal transducer and activator of transcription
- GRB2-associated-binding protein 1
- Epidermal growth factor receptor
- Fibroblast growth factor receptor substrate 2
- Tyrosine-protein kinase ABL1
Sequence:
MSSARFDSSDRSAWYMGPVTRQEAQTRLQGQRHGMFLVRDSSTCPGDYVLSVSENSRVSHYIINSLPNRRFKIGDQEFDHLPALLEFYKIHYLDTTTLIEPAPRYPSPPVGSVSAPNLPTAEENLEYVRTLYDFPGNDAEDLPFKKGELLVIIEKPEEQWWSARNKDGRVGMIPVPYVEKLVRSSPHGKHGNRNSNSYGIPEPAHAYAQPQTTTPLPTVASTPGAAINPLPSTQNGPVFAKAIQKRVPCAYDKTALALEVGDIVKVTRMNINGQWEGEVNGRKGLFPFTHVKIFDPQNPDDNE
Protein: Phosphoinositide 3-phosphatase (EC 3.1.3.64) (O13819)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Lipid phosphatase which dephosphorylates phosphatidylinositol 3-monophosphate (PI3P). Involved in the control of PI3P-dependent signaling and in the maintenance of endosomal system integrity (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C3C7.01c
- Uncharacterized protein C19F5.03
- Polyphosphoinositide phosphatase
- 1-phosphatidylinositol 3-phosphate 5-kinase fab1
- Phosphatidylinositol 3-kinase pik3
- Phosphatidylinositol 4-kinase lsb6
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phosphatidylinositol 4-kinase stt4
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1
- Phosphatidylinositol 4-kinase pik1
Sequence:
MENIKVAKVGNVKFVNKGNELNGTLHLTAYHSIFSISENGKEIWTAYSMINNVKLCSNEKSFCIRIQCRDFMFFCWRFQSTEDAMDVYDTLQELMSINSINMLYAFYYMPSGDEEKLPSSWKSFLLENEYRRMGVGDSTQADGAGGNWRITKINENYSECHSYPQALAVPASISDSVIYYGCKYRSKNRFPTLTYLHKNSFSITRASQPLVGIRQNRSAQDEKLVEAIFATSIIPGKENLIVDARPSTNAMANIAVGAGSENMDHYRFAKKIYLGIDNIHVMRDSLNKIVNALKNTDISAAPPLIELLNRSSWLKHLANILQGAVLIVKTVHFRHAHVLVHCSDGWDRTSQLCALPQLCLDPYYRTIEGFFALVEKDWLSFGHRFAERCCHLPGKRIFTIDSSYSEEPPQSSPSSTLQYTFSTVRSALSGFSIDHSEKMMSPVFHQFLDCVWQIMDQFPNCFEFNERFLRRLLYHLYSCQYGSFLYNSERERAQASVSTHTRCIWDYFLSRKDEFKNPNYVPYDDVIMPDPSSLRWWSASFAQPDENMNIPSPSESPSL
Protein: Aorsin (EC 3.4.21.-) (Q8NK92)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Serine endopeptidase which hydrolyzes a range of fluorogenic peptide substrates containing the basic residues arginine or lysine at the P1 position and prefers paired basic resides. Also hydrolyzes clupeine and salmine, activates plasminogen and converts trypsinogen to trypsin.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:12519073}.
Interaction partners:
- FK506-binding protein 1
Sequence:
MRPLSHLSFFNGLLLGLSALSAATSVVHERREATSSNWVKRARVNPSDKHVVRIGLTQSSLEEAHDLLMDVSNPSSPNYARFYSADEVAAKFAPSTETVNEVQNWLTEKGINASRVAQTQNHGWLVFHATSKEIENLFDTTYYEYHNRKTGKKAIACEQYHVPASVQKHIDYVHPGVNLNPSSGKPSSIRRRAAASKKTKLPARGPRPIQQHDVKGLNVTNCDQLITPECIRALYKIPSARAAPHPNNSLGIFEEGDYYAQEDLDLFFKTFAKDIPQGTHPIPAFIDGAEAPVPVTKAGGESDLDFELAYPIVHPQSITLYQTDDANWASNTTGFLNTFLDALDGSYCTYCAYGECGNDPSLDPVYPDDAGYDGQLMCGVFKPTNVISVSYGEQENDLPANYQQRQCMEFLKLGLQGVSVLFASGDNGVAGPPGDGNSVNGCLNNGTVFSPAFPNSCPYITNVGATKVYPGYTVSQPESAVYDPDGLYSYASGGGFSNIYPIPDYQAEAVATYFKDHNPPYPYYEGAENLGKNGGLYNRLGRGYPDVAANGDNIAVFNGGEFGSSGGTSASTPIFASIINRIIDERLAVGKGPVGFINPVLYKNPSVLNDITNGTNPGCGTDGFSTAPGWDPATGLGTPNYPKMLKLWLDLP
Protein: Peptide YYb (E7F0L6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Neuropeptide Y receptor type 2
- Proenkephalin a
- Prepronociceptin a.
- Motilin-like
- Galanin peptides
- Somatostatin 1, tandem duplicate 1.
- Prodynorphin.
Sequence:
MASALRSWTVPLALALCVIVCLSSLAEAYPPKPEPPAGDVGPEEMAKYHTALRHYINLITRQRYGKRSTPEAAVAELLFGDDEQDIRPRVEDLLW
Protein: Regulator of microtubule dynamics protein 1 (RMD-1) (hRMD-1) (Protein FAM82B) (Q96DB5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18070910}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18070910}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:18070910}. Note=In interphase localizes in the cytoplasm, and during mitosis localizes to the spindle microtubules and spindle poles.
Interaction partners:
Sequence:
MALAARLWRLLPFRRGAAPGSRLPAGTSGSRGHCGPCRFRGFEVMGNPGTFKRGLLLSALSYLGFETYQVISQAAVVHATAKVEEILEQADYLYESGETEKLYQLLTQYKESEDAELLWRLARASRDVAQLSRTSEEEKKLLVYEALEYAKRALEKNESSFASHKWYAICLSDVGDYEGIKAKIANAYIIKEHFEKAIELNPKDATSIHLMGIWCYTFAEMPWYQRRIAKMLFATPPSSTYEKALGYFHRAEQVDPNFYSKNLLLLGKTYLKLHNKKLAAFWLMKAKDYPAHTEEDKQIQTEAAQLLTSFSEKN
Protein: Glutathione S-transferase 4 (EC 2.5.1.18) (GST class-phi member 4) (GST-27) (GST-IV) (P46420)
Organism: Zea mays (Maize)
Function: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the detoxification of certain herbicides. Most active with substrates possessing a chloroacetamide structure. Trans-cinnamic acid and 1-chloro-2,4-dinitrobenzene are not effective substrates. May play an important role in the benoxacor-mediated protection of maize from metolachlor injury.
Interaction partners:
- methionine--tRNA ligase
- methionine--tRNA ligase
- methionine--tRNA ligase
- ARF-related protein
- Glutathione reductase
- glutathione transferase
Sequence:
MATPAVKVYGWAISPFVSRALLALEEAGVDYELVPMSRQDGDHRRPEHLARNPFGKVPVLEDGDLTLFESRAIARHVLRKHKPELLGGGRLEQTAMVDVWLEVEAHQLSPPAIAIVVECVFAPFLGRERNQAVVDENVEKLKKVLEVYEARLATCTYLAGDFLSLADLSPFTIMHCLMATEYAALVHALPHVSAWWQGLAARPAANKVAQFMPVGAGAPKEQE