wanglab/gogpt-training-data huggingface dataset:
Protein: Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes) (Glycine cleavage system L protein) (P0A9P0)
Organism: Escherichia coli (strain K12)
Function: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16079137}. Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex
- Pyruvate dehydrogenase E1 component
- 2-oxoglutarate dehydrogenase E1 component
- Glycine dehydrogenase
- Aminomethyltransferase
- Glycine cleavage system H protein
- Formate acetyltransferase 1
- Serine hydroxymethyltransferase
- PFL-like enzyme TdcE
Sequence:
MSTEIKTQVVVLGAGPAGYSAAFRCADLGLETVIVERYNTLGGVCLNVGCIPSKALLHVAKVIEEAKALAEHGIVFGEPKTDIDKIRTWKEKVINQLTGGLAGMAKGRKVKVVNGLGKFTGANTLEVEGENGKTVINFDNAIIAAGSRPIQLPFIPHEDPRIWDSTDALELKEVPERLLVMGGGIIGLEMGTVYHALGSQIDVVEMFDQVIPAADKDIVKVFTKRISKKFNLMLETKVTAVEAKEDGIYVTMEGKKAPAEPQRYDAVLVAIGRVPNGKNLDAGKAGVEVDDRGFIRVDKQLRTNVPHIFAIGDIVGQPMLAHKGVHEGHVAAEVIAGKKHYFDPKVIPSIAYTEPEVAWVGLTEKEAKEKGISYETATFPWAASGRAIASDCADGMTKLIFDKESHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTIHAHPTLHESVGLAAEVFEGSITDLPNPKAKKK
Protein: Osteopontin precursor (Spp1) (Q6IVB9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MKSIIVLTLLVATVFCVPVKRSASSSESSEELVIVQRPPPILRKAAANVFQVEPTQTTPTESNESTDSADDTEEADEESETDEKEEENETDSSESESGESDTTIIPVTVDPTLGPIINTGRGDSLGYPSDYKKSIVYVDAKDFEKLPSPYKSYSSDKLGGLTFVSKKTSAYDDQSINDVEKEITLYKALQVHDLEDGNTSTSEIDNIEANERQAALGAQEIVPVGDQAATEEGASARDSPSDSASASASQEENEEESDSEETTATPGAADSESNSSQSTESTESQESDSDEETTQTTEASIIIVK
Protein: GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (Glutamine amidotransferase) (P49915)
Organism: Homo sapiens (Human)
Function: Catalyzes the conversion of xanthine monophosphate (XMP) to GMP in the presence of glutamine and ATP through an adenyl-XMP intermediate.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:8089153}.
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase 1
- Inosine-5'-monophosphate dehydrogenase 2
- Ubiquitin carboxyl-terminal hydrolase 7
- Adenine phosphoribosyltransferase
- GMP reductase 1
- Guanylate kinase
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- CTP synthase 1
- Thiopurine S-methyltransferase
Sequence:
MALCNGDSKLENAGGDLKDGHHHYEGAVVILDAGAQYGKVIDRRVRELFVQSEIFPLETPAFAIKEQGFRAIIISGGPNSVYAEDAPWFDPAIFTIGKPVLGICYGMQMMNKVFGGTVHKKSVREDGVFNISVDNTCSLFRGLQKEEVVLLTHGDSVDKVADGFKVVARSGNIVAGIANESKKLYGAQFHPEVGLTENGKVILKNFLYDIAGCSGTFTVQNRELECIREIKERVGTSKVLVLLSGGVDSTVCTALLNRALNQEQVIAVHIDNGFMRKRESQSVEEALKKLGIQVKVINAAHSFYNGTTTLPISDEDRTPRKRISKTLNMTTSPEEKRKIIGDTFVKIANEVIGEMNLKPEEVFLAQGTLRPDLIESASLVASGKAELIKTHHNDTELIRKLREEGKVIEPLKDFHKDEVRILGRELGLPEELVSRHPFPGPGLAIRVICAEEPYICKDFPETNNILKIVADFSASVKKPHTLLQRVKACTTEEDQEKLMQITSLHSLNAFLLPIKTVGVQGDCRSYSYVCGISSKDEPDWESLIFLARLIPRMCHNVNRVVYIFGPPVKEPPTDVTPTFLTTGVLSTLRQADFEAHNILRESGYAGKISQMPVILTPLHFDRDPLQKQPSCQRSVVIRTFITSDFMTGIPATPGNEIPVEVVLKMVTEIKKIPGISRIMYDLTSKPPGTTEWE
Protein: Sperm acrosome membrane-associated protein 3 (Cancer/testis antigen 54) (CT54) (Lysozyme-like acrosomal sperm-specific secretory protein ALLP-17) (Lysozyme-like protein 3) (Sperm lysozyme-like protein 1) (Sperm protein reactive with antisperm antibodies) (Sperm protein reactive with ASA) [Cleaved into: Sperm acrosome membrane-associated protein 3, membrane form; Sperm acrosome membrane-associated protein 3, processed form] (Q8IXA5)
Organism: Homo sapiens (Human)
Function: Sperm surface membrane protein that may be involved in sperm-egg plasma membrane adhesion and fusion during fertilization. It could be a potential receptor for the egg oligosaccharide residue N-acetylglucosamine, which is present in the extracellular matrix over the egg plasma membrane. The processed form has no detectable bacteriolytic activity in vitro.
Subcellular location: [Isoform 1]: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Note=Anterior acrosome in non-capacitated spermatozoa and retained in the equatorial segment and in the luminal face of both the inner and outer acrosomal membranes following capacitation and the acrosome reaction. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
Interaction partners:
- Sperm acrosome membrane-associated protein 1
Sequence:
MVSALRGAPLIRVHSSPVSSPSVSGPRRLVSCLSSQSSALSQSGGGSTSAAGIEARSRALRRRWCPAGIMLLALVCLLSCLLPSSEAKLYGRCELARVLHDFGLDGYRGYSLADWVCLAYFTSGFNAAALDYEADGSTNNGIFQINSRRWCSNLTPNVPNVCRMYCSDLLNPNLKDTVICAMKITQEPQGLGYWEAWRHHCQGKDLTEWVDGCDF
Protein: ATP-dependent Clp protease proteolytic subunit (EC 3.4.21.92) (Endopeptidase Clp) (Q6ENE9)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Subcellular location: Plastid, chloroplast stroma {ECO:0000255|HAMAP-Rule:MF_00444}.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit
- Clp ATPase C-terminal domain-containing protein
- ATP-dependent Clp protease proteolytic subunit
- Clp ATPase C-terminal domain-containing protein
- Clp ATPase C-terminal domain-containing protein
- Clp ATPase C-terminal domain-containing protein
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease proteolytic subunit
Sequence:
MPIGVPKVPYRIPGDEEATWVDLYNVMYRERTLFLGQEIRCEVTNHITGLMVYLSIEDGISDIFLFINSPGGWLISGMAIFDTMQTVTPDIYTICLGIAASMASFILLGGEPTKRIAFPHARIMLHQPASAYYRARTPEFLLEVEELHKVREMITRVYALRTGKPFWVVSEDMERDVFMSADEAKAYGLVDIVGDEMLDEHCDTDPVWFPEMFKDW
Protein: Luc7-like protein 3 (Cisplatin resistance-associated-overexpressed protein) (Luc7A) (Okadaic acid-inducible phosphoprotein OA48-18) (cAMP regulatory element-associated protein 1) (CRE-associated protein 1) (CREAP-1) (O95232)
Organism: Homo sapiens (Human)
Function: Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:10631324, ECO:0000269|PubMed:12565863}. Note=The subnuclear localization is affected by cisplatin.
Interaction partners:
- Arginine/serine-rich protein PNISR
- RNA-binding protein 25
- RNA-binding protein 39
- U1 small nuclear ribonucleoprotein 70 kDa
- Pre-mRNA-processing factor 39
- Serine/arginine-rich splicing factor 11
- U4/U6.U5 tri-snRNP-associated protein 1
- Pre-mRNA-processing factor 40 homolog A
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein F
Sequence:
MISAAQLLDELMGRDRNLAPDEKRSNVRWDHESVCKYYLCGFCPAELFTNTRSDLGPCEKIHDENLRKQYEKSSRFMKVGYERDFLRYLQSLLAEVERRIRRGHARLALSQNQQSSGAAGPTGKNEEKIQVLTDKIDVLLQQIEELGSEGKVEEAQGMMKLVEQLKEERELLRSTTSTIESFAAQEKQMEVCEVCGAFLIVGDAQSRVDDHLMGKQHMGYAKIKATVEELKEKLRKRTEEPDRDERLKKEKQEREEREKEREREREERERKRRREEEEREKERARDRERRKRSRSRSRHSSRTSDRRCSRSRDHKRSRSRERRRSRSRDRRRSRSHDRSERKHRSRSRDRRRSKSRDRKSYKHRSKSRDREQDRKSKEKEKRGSDDKKSSVKSGSREKQSEDTNTESKESDTKNEVNGTSEDIKSEGDTQSN
Protein: Interferon regulatory factor 6 (G0Z349)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MALHPRRVRLKPWLVAQVDSGLYPGLIWLHRDSKRFQIPWKHATRHSPQQEEENTIFKAWAVETGKYQEGVDDPDPAKWKAQLRCALNKSREFNLMYDGTKEVPMNPVKIYQVCDIPQPQGSIINPGSTGSAPWDEKDNDVDEEDEEDELDQSQHHVPIQDTFPFLNINGSPMAPASVGNCSVGNCSPEAVWPKTEPLEMEVPQAPIQPFYSSPELWISSLPMTDLDIKFQYRGKEYGQTMTVSNPQGCRLFYGDLGPMPDQEELFGPVSLEQVKFPGPEHITNEKQKLFTSKLLDVMDRGLILEVSGHAIYAIRLCQCKVYWSGPCAPSLVAPNLIERQKKVKLFCLETFLSDLIAHQKGQIEKQPPFEIYLCFGEEWPDGKPLERKLILVQVIPVVARMIYEMFSGDFTRSFDSGSVRLQISTPDIKDNIVAQLKQLYRILQTQESWQPMQPTPSMQLPPALPPQ
Protein: Envelope protein P10 (P11127)
Organism: Pseudomonas phage phi6 (Bacteriophage phi-6)
Function: Involved in cell lysis.
Subcellular location: Virion membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDNILDPLKAPFSSEAAAKTTAAKIAVVYALVGLVGGLLLTK
Protein: Exonuclease domain-containing protein (Q57WZ1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRACVHFARAIKATQNLTHLEVFTQLQLGIHPPLSTQRQFLQQHFDVEMERRGITETKLLAMDGHLCTQLLRQLLFERYLSVPFRLFTFDLEFTGPPVFGPDGPTEDIMEFGFYSPAHDKVFSCLVRPSNGRCVSPEVTTLTHITQKMLEEDGLPFRDAWAKVLDFLNTPEPQELPGAEKRLLVLSHGGKLADVSLIKWTLEASGMELPSNIIFGDTFHLIRDAHRRRPVTLDKHPPTWGLSDLVQWLRIPPTLPAHRAGNDAKMTWDALYHTLERYGDEDLTPREQLVSRFFDVEAKQVMSQAGIRSHAQPDGTLENDTSYMEASVSDSLDLDFDEIFTPDGKQRPEVSEDRTDDVPDGSKGESHSGASRGKVRSGKRNGRSSSSGGDRGEEFII
Protein: Prickle-like protein 1a (Prickle1) (Q6WGK5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MELENHGGLHMGSKVNKLTLGFQRSSTSDDDSGCALEEYAWVPPGLRPEQVALYFSCLPEDKVPYVNSPGEKQRIKQLLYQLPPHDNEVRYCQSLSEEEKKELHMFSIQRKKEALGRGTLKILPRTVHHAACEHCGERLSGGEMAVCVSRAAAAGQCWHPACFTCSTCSELLVDLIYFYHDGKVHCGRHHAELLKPRCSSCDEIIFADECTEAEGRHWHMKHFSCSECEVILGGQRYIMKDGRPFCCGCFQSLYAEYCQACAQHIGVDHAQMTYDGLHWHATDACFSCAQCKSSLLGCPFLPRQGRIYCSKACSLGEDVQASDSSDSAFQSARSRESRRSVKMGKSSRSADQCRQSLLFSPASNYKFPGLSGNADDTLSKRLSQLNFADNHFWRNREDQEAPEDHEEWAEHDDYMTQLLLKFGEHGMFQDTRTDLSIWTDSELKNKTCSGGNSSLASKKYKADMYWTQSQDGLGDSAYGSHPGPASSRKLQDLDLEHGASFKHEDNKQWFNDSLECITDQLKEADLNIRDSMDSLALSNITGASVDGDIKDKPLLFSLQKFSDLDRCENTSNMGTLNSSMKSLTSDLDRTQVIEEQQEQGVPSPEVHPKPPRLPVLRRSKSQSKTQQVKFSDDVIDNGRYDELKVRQPPMSERTRRRAFQFDEQDHQRPRHHHRRRRSRMSRSDNALHLAPKEEKPRVCFKDDRRKHGLGHNGAQYGDGLRTERFTRLYEDDWCSTCSSSSSESEEEGFFLGQPIPQPRQPRYQYYASDEAAFSTRTKSKQKRGRKGKNCIIS
Protein: HIG1 hypoxia inducible domain family member 1A (C9JNU6)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
Sequence:
MSTDTGVSLPSYEEDQGSKLIRKAKEAPFVPVGIAGFAAIVAYGLYKLKSRGNTKMSIHLIHMRVAAQGFVVGAMTVAFFFFRYGLFHVSGILGKT
Protein: Vomeronasal type-1 receptor 54 (Pheromone receptor VN7) (Vomeronasal receptor 7) (Vomeronasal type-1 receptor A9) (Q9EPB8)
Organism: Mus musculus (Mouse)
Function: Putative pheromone receptor implicated in the regulation of social and reproductive behavior.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MNKMNRLSHNTEIRNAIYSGVGIGISGNSFLLLFHIFKYIRGQRSRHIDLPIGLLSLIHLVMLIAMSLVATDIFMPWGRWGDTTCKCVISLYRFCRSLSLCATSLLSILQAVTLNPRNSCLEKFKRKSPHYMLGCLLFLSVFYTFISSPLATYITAKSNLTSPSFTYITTSCSLAPMSYSFHLTVFILLTSRDVIFVGLMLLSSGYMVTFLGRHKKQSQFLHITSFSLKPSAEKRAMRTILCLMSFFVLMYTLDSIVSYIRSIDDGQIFYCVHIFTAHGYATVSPFLILSTEKYIINIFRSTFGRMVTIILLRNR
Protein: Cardiac troponin I (D5M8S7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MPEQVQEKRKSKISASRKLMLKSLMVAKAKEEIEQEIVDKEEEKERYLAERAPTLQTGGMSFAELQELCRELHAKVDVVDEERYDIEAKVMHNTREIKDLNIKVLDLRGKFKRPSLRRVRVSADAILRSLLGSKHKVSMDLRANLKSVKKEDTEKEKTVEVSDWRKNVEAMSGMEGRKKMFDAAKGTPQ
Protein: Ubiquitin-like-conjugating enzyme ATG10 (EC 2.3.2.-) (Autophagy-related protein 10) (AtATG10) (Q8VZ52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E2-like enzyme involved in autophagy. Acts as an E2-like enzyme that catalyzes the conjugation of ATG12 to ATG5. The ATG12-ATG5 conjugates is required for the formation of autophagic vesicles and for the timely progression of senescence and programmed cell death (PCD). Likely serves as an ATG5-recognition molecule. Confers some resistance to nitrogen and carbon starvation. Is also involved in the formation of anthocyanic vacuolar inclusions (AVI). Promotes an autophagic process that constitutes a pro-survival mechanism by controlling the containment of host tissue-destructive microbial infections during necrotrophic pathogen infection, but negatively controls SA-dependent defenses and basal immunity to bacterial infection during biotrophic infection.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ubiquitin-like protein ATG12A
- Ubiquitin-like modifier-activating enzyme atg7
- Ubiquitin-like protein ATG12B
- Autophagy-related protein 3
- Autophagy protein 5
- Autophagy-related protein 16
- Autophagy-related protein 9
- Autophagy-related protein 101
- Phosphatidylinositol 3-kinase VPS34
- Serine/threonine-protein kinase VPS15
Sequence:
MDSAREVSDGRLTVEGFSVASRAFADKWKIHNQSFPPWSWVPLINRTLLVSKKEEGYLSLEKIIILSSLEEEIPEDESLNVATDCLEKEETVDHTILVPTMENEAHYYDFHIVYSASYKVPVLYFRGYCSGGEPLALDVIKKDVPSCSVSLLLESKWTFITQEEHPYLNRPWFKLHPCGTEDWIKLLSQSSSSSGCQMPIVLYLVSWFSVVGQVVGLRIPLEMLN
Protein: Cutinase (EC 3.1.1.74) (Poly(ethylene terephthalate) hydrolase) (PET hydrolase) (PETase) (EC 3.1.1.101) (Q47RJ7)
Organism: Thermobifida fusca (strain YX)
Function: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters). Also hydrolyzes the triglyceride triolein. Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world.
Subcellular location: Secreted {ECO:0000250|UniProtKB:G8GER6}. Periplasm {ECO:0000250|UniProtKB:G8GER6}.
Interaction partners:
Sequence:
MPPHAARPGPAQNRRGRAMAVITPRRERSSLLSRALRFTAAAATALVTAVSLAAPAHAANPYERGPNPTDALLEARSGPFSVSEERASRFGADGFGGGTIYYPRENNTYGAVAISPGYTGTQASVAWLGERIASHGFVVITIDTNTTLDQPDSRARQLNAALDYMINDASSAVRSRIDSSRLAVMGHSMGGGGTLRLASQRPDLKAAIPLTPWHLNKNWSSVRVPTLIIGADLDTIAPVLTHARPFYNSLPTSISKAYLELDGATHFAPNIPNKIIGKYSVAWLKRFVDNDTRYTQFLCPGPRDGLFGEVEEYRSTCPF
Protein: Lipid droplet assembly factor 1 (Promethin) (Transmembrane protein 159) (Q96B96)
Organism: Homo sapiens (Human)
Function: Plays an important role in the formation of lipid droplets (LD) which are storage organelles at the center of lipid and energy homeostasis. In association with BSCL2/seipin, defines the sites of LD formation in the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30901948, ECO:0000269|PubMed:31708432}; Multi-pass membrane protein {ECO:0000255}. Lipid droplet {ECO:0000269|PubMed:30901948, ECO:0000269|PubMed:31708432}. Note=Co-localizes with BSCL2/seipin in the ER, upon LD formation dissociates from BSCL2/seipin and relocalizes to LD surfaces during LD maturation. {ECO:0000269|PubMed:31708432}.
Interaction partners:
- Seipin
Sequence:
MAKEEPQSISRDLQELQKKLSLLIDSFQNNSKVVAFMKSPVGQYLDSHPFLAFTLLVFIVMSAVPVGFFLLIVVLTTLAALLGVIILEGLVISVGGFSLLCILCGLGFVSLAMSGMMIASYVVVSSLISCWFSPRPLTQQNTSCDFLPAMKSAEFEGLYQE
Protein: Recombination signal binding protein for immunoglobulin kappa J region (D6RF98)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAWIKRKFGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNADLCIASGTKVALFNRLRSQTVSTRYLHVEGGNFHASSQQWGAFFIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLVRNDGIIYSTSLTFTYTPEPGPRPHCSAAGAILRANSSQVPPNESNTNSEGSYTNASTNSTSVTSSTATVVS
Protein: High affinity Ca2+/Mn2+ P-type ATPase (Eurofung) (Q5AW66)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 4
Sequence:
MSRSATPALPFHNGQATGSISPLAAPAGGRSNAAPSVSTSTYSQLSPQETADRLQTSLTHGLTPAEAEIRYIRDGPNELPHEEPEPLWLRFLKQFKETLILLLLASAAVSFFMGNLDDAVSITLAVTIVVTVGFVQEYRSEKSLEALNRLVPHHAHLIRDVPSNSPPIVHPTTAIPDDEFELRELRSKSPSSGSVSAAVKASTTVPAAELVPGDLVLFTVGDRIPADIRITAATDLTLDESNLTGENEPVVKYPDAICNQKNIPTSKIVTPPRSPFYDAPASGTVGADLRLNEQHNIAFMGTLVRSGYGQGIVIGTGAKTEFGSISASLQEIESPRTPLQLSMDRLGQELSYISFGVIALIVVVGLIQGRKLLDMFTIGVSLAVAAIPEGLPIIVTVTLALGVLRMASRGAIMRRLPSVETLGSVNVVCSDKTGTLTLNHMTVTKMWHFDCAEPFEVHHDIASLTPGPAARTVLRIGNIANNARLSRVHANSPASASSAAVLSSTDDDASGSMKSRWVGQPTDVAILDLLDAFGEDDVRDRISARVAETPFSSERKWMGVVIGSGVPGDSTAPIGGPSMAYIKGALEQVLARCDTYLTKDGQEVILDERRRQVVRQAAEQMASEGLRVLSFASGAVRESRGRALGSRSGTPSSKVSSGDEDDRYSGLVFAGLVGMNDPPRKDVHKAIRRLMAGGVRVIMITGDAETTAVAIAKKLGMPIVETPGVRNVLCGQEIDRMGTSELSQALSSVSIFARTSPDHKMKIVRALQSRGDVVAMTGDGVNDAPALKKADIGIAMGKLGTDVAKEAADMILTDDDFSTILRAIEQGKGIFYNIQNFITFQLSTSVAALSLVLLSTMFGFKNPLNAMQILWINILMDGPPAQSLGVEPVDPSIMGRPPRPKSARVLTKPLIQRVLTSAFMIMMGTLAIYIYEMGDDDDVLTGKRSRVVTAHDTTMTFTCFVLFDMFNALTCRSEGKSVLRGEISLFGNKMFNYAVLGSLAGQACVIYLPFLQRVFQTEPLNAAHLFKLVCIASTVFWVDEGRKYYQSLQRRRAVGVGYSVNV
Protein: Somatotropin (Growth hormone) (GH) (GH-N) (Growth hormone 1) (Pituitary growth hormone) (P01241)
Organism: Homo sapiens (Human)
Function: Plays an important role in growth control. Its major role in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. It stimulates both the differentiation and proliferation of myoblasts. It also stimulates amino acid uptake and protein synthesis in muscle and other tissues.
Subcellular location: Secreted {ECO:0000269|PubMed:5279046, ECO:0000269|PubMed:5810834}.
Interaction partners:
- Growth hormone receptor
- Prolactin receptor
- Chorionic somatomammotropin hormone 1
- Chorionic somatomammotropin hormone 2
- Somatoliberin
- Erythropoietin
- Appetite-regulating hormone
- Leptin
- Prolactin
- Albumin
Sequence:
MATGSRTSLLLAFGLLCLPWLQEGSAFPTIPLSRLFDNAMLRAHRLHQLAFDTYQEFEEAYIPKEQKYSFLQNPQTSLCFSESIPTPSNREETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEGIQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFRKDMDKVETFLRIVQCRSVEGSCGF
Protein: Putative lipoprotein LpqE (P9WK63)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
Interaction partners:
- Cytochrome bc1 complex cytochrome c subunit
- Cytochrome bc1 complex Rieske iron-sulfur subunit
- Uncharacterized protein Rv2876
- Cytochrome bc1 complex cytochrome b subunit
- Probable cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 2
- Probable cytochrome c oxidase polypeptide 4
- Probable cytochrome c oxidase subunit 3
- Superoxide dismutase
- DNA integrity scanning protein DisA
Sequence:
MNRCNIRLRLAGMTTWVASIALLAAALSGCGAGQISQTANQKPAVNGNRLTINNVLLRDIRIQAVQTSDFIQPGKAVDLVLVAVNQSPDVSDRLVGITSDIGSVTVAGDARLPASGMLFVGTPDGQIVAPGPLPSNQAAKATVNLTKPIANGLTYNFTFKFEKAGQGSVMVPISAGLATPHE
Protein: Dickkopf-related protein 2 (Dickkopf-2) (Dkk-2) (hDkk-2) (Q9UBU2)
Organism: Homo sapiens (Human)
Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity).
Subcellular location: Secreted.
Interaction partners:
- Low-density lipoprotein receptor-related protein 5
- Low-density lipoprotein receptor-related protein 6
- Kremen protein 1
- Dickkopf-related protein 3
- Protein Wnt-6
- Protein Wnt-2b
- Dickkopf-related protein 1
- Protein Wnt-3a
- Dickkopf-related protein 4
- Protein Wnt-2
Sequence:
MAALMRSKDSSCCLLLLAAVLMVESSQIGSSRAKLNSIKSSLGGETPGQAANRSAGMYQGLAFGGSKKGKNLGQAYPCSSDKECEVGRYCHSPHQGSSACMVCRRKKKRCHRDGMCCPSTRCNNGICIPVTESILTPHIPALDGTRHRDRNHGHYSNHDLGWQNLGRPHTKMSHIKGHEGDPCLRSSDCIEGFCCARHFWTKICKPVLHQGEVCTKQRKKGSHGLEIFQRCDCAKGLSCKVWKDATYSSKARLHVCQKI
Protein: Phosphodiesterase (EC 3.1.4.-) (A0A0S2Z4T6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGSGSSSYRPKAIYLDIDGRIQKVIFSKYCNSSDIMDLFCIATGLPRNTTISLLTTDDAMVSIDPTMPANSERTPYKVRPVAIKQLSAGVEDKRTTSRGQSAERPLRDRRVVGLEQPRREGAFESGQVEPRPREPQGCYQEGQRIPPEREELIQSVLAQVAEQFSRAFKINELKAEVANHLAVLEKRVELEGLKVVEIEKCKSDIKKMREELAARSSRTNCPCKYSFLDNHKKLTPRRDVPTYPKYLLSPETIEALRKPTFDVWLWEPNEMLSCLEHMYHDLGLVRDFSINPVTLRRWLFCVHDNYRNNPFHNFRHCFCVAQMMYSMVWLCSLQEKFSQTDILILMTAAICHDLDHPGYNNTYQINARTELAVRYNDISPLENHHCAVAFQILAEPECNIFSNIPPDGFKQIRQGMITLILATDMARHAEIMDSFKEKMENFDYSNEEHMTLLKMILIKCCDISNEVRPMEVAEPWVDCLLEEYFMQSDREKSEGLPVAPFMDRDKVTKATAQIGFIKFVLIPMFETVTKLFPMVEEIMLQPLWESRDRYEELKRIDDAMKELQKKTDSLTSGATEKSRERSRDVKNSEGDCA
Protein: Translation initiation factor eIF-2B alpha subunit, putative (Q585B9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Elongation initiation factor 2 alpha subunit, putative
- Translation initiation factor eIF2B subunit gamma
- Glucose-1-phosphate adenylyltransferase/Bifunctional protein GlmU-like C-terminal hexapeptide domain-containing protein
- Translation initiation factor eIF2B subunit delta
- protein-synthesizing GTPase
- Translation initiation factor, putative
- Translation initiation factor eIF2B subunit beta
- Selenocysteine-specific elongation factor
- mannose-1-phosphate guanylyltransferase
Sequence:
MEVPHDDYDISIMIRVVKEVQELLTSKQFSTYSELDKEITNMLKGYKSIGDGFERFRIDLTKDAANSPDLRSSLVDMNARCESRLRDFECSQKDQINDMLPFIRSTSRILVHGCGDLLALAIACAIQEREGVHFYICEGRPATAKYPQGTGEALLRKASATHEGLKLKEKLQQYCTIIPDAGVGAVMSKVDFVVTGAYCVTEHGGLVHSTGSLQIATVASAMNVPFYVLCETFKFAHIFPLSTADLRQPEGSSDVPLVEFVPPSMVTLVFSEQGIMPPSAVTYEMFRYHTALFAPGKCQ
Protein: Dead end protein homolog 1 (RNA-binding motif, single-stranded-interacting protein 4) (Q8IYX4)
Organism: Homo sapiens (Human)
Function: RNA-binding factor that positively regulates gene expression by prohibiting miRNA-mediated gene suppression. Relieves miRNA repression in germline cells (By similarity). Prohibits the function of several miRNAs by blocking the accessibility of target mRNAs. Sequence-specific RNA-binding factor that binds specifically to U-rich regions (URRs) in the 3' untranslated region (3'-UTR) of several mRNAs. Does not bind to miRNAs. May play a role during primordial germ cell (PGC) survival (By similarity). However, does not seem to be essential for PGC migration (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18155131}. Cytoplasm {ECO:0000269|PubMed:18155131}. Note=Perinuclear germ granules, also called germ plasm or chromatoid body. Colocalizes in perinuclear sites with APOBEC3 (By similarity). {ECO:0000250}.
Interaction partners:
- Nanos homolog 3
- Tudor domain-containing protein 7
- Nanos homolog 2
- Nanos homolog 1
- Deleted in azoospermia-like
- Eukaryotic translation initiation factor 2 subunit 2
Sequence:
MQSKRDCELWCERVNPENKAALEAWVRETGIRLVQVNGQRKYGGPPPGWVGSPPPAGSEVFIGRLPQDVYEHQLIPLFQRVGRLYEFRLMMTFSGLNRGFAYARYSSRRGAQAAIATLHNHPLRPSCPLLVCRSTEKCELSVDGLPPNLTRSALLLALQPLGPGLQEARLLPSPGPAPGQIALLKFSSHRAAAMAKKALVEGQSHLCGEQVAVEWLKPDLKQRLRQQLVGPFLRSPQPEGSQLALARDKLGFQGARATLQLLCQRMKLGSPVFLTKCLGIGPAGWHRFWYQVVIPGHPVPFSGLIWVVLTLDGRDGHEVAKDAVSVRLLQALSESGANLLWSAGAEAGTMVKQ