wanglab/gogpt-training-data huggingface dataset:
Protein: O-acyltransferase (Q960U8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|PIRNR:PIRNR000439}.
Interaction partners:
- Acyltransferase
- phosphatidate phosphatase
- Acyltransferase
- Acyltransferase
- RE35159p
- RH32172p
- GH04282p
- Membrane-bound acylglycerophosphatidylinositol O-acyltransferase frj
- FI20175p1
- Dehydrogenase/reductase 4
Sequence:
MTTNKDPQDKEPGKAEQPTKNSGSSGVGIMKRLRRSASATEHNLSSLRNRKSTQNLFDQHGNPIDLRQYRKVLDKDENGNGTNGSEKKLRYRRTQSVTRAEEISNKEEKQRRAQPGRPIHRPRDSLFSWSSGFTNFSGLVNWGFLLLCIGGLRLGLENLLKYGIRINPLDWFFFISGHNEGEGHNALILSIYSLVHISLCLAVEKGLAMEIIAEGLGLFIQIVNIVVLVCLPVVTIHLKGHAFSLMGASTVCFFYSVLFLKLWSYVQTNMWCRQTYYQKNPRERRPSITLAELKKGVLNGGEEDEDVSKLVQYPDNLTYKDLLYFLCAPTLCYELNFPRTSRVRKRFLLKRLLEVVIGVNVVMALFQQWIIPSVRNSLIPFSNMDVALATERLLKLALPNHLCWLCFFYLMFHSFLNAVGELLNFADRNFYCDWWNANNIDTFWRTWNMPVHRWCVRHLYIPVVQMGYSSRQASTIVFLFSAVFHEYLVSVPLQIYKIWAFMGMMGQIPLSAISKSIEKKLGPRMGNIIVWASIILGQPLCIMAYYHDYVVQHFKNSLNGTDYSS
Protein: UPF0056 inner membrane protein YhgN (P67143)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Putative aminopeptidase FrvX
Sequence:
MNEIISAAVLLILIMDPLGNLPIFMSVLKHTEPKRRRAIMVRELLIALLVMLVFLFAGEKILAFLSLRAETVSISGGIILFLIAIKMIFPSASGNSSGLPAGEEPFIVPLAIPLVAGPTILATLMLLSHQYPNQMGHLVIALLLAWGGTFVILLQSSLFLRLLGEKGVNALERLMGLILVMMATQMFLDGIRMWMKG
Protein: Tetraspanin (Q9W4X6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361218}.
Interaction partners:
Sequence:
MSNYRYQGAGLGGVGMAGGRGYSGIEVHEVMHPHHFTYVSQCVKYMIFLLNFVFWLFGGLLLGIGVYAFRDKWEDANGSVRLENFYDVFLNISLVMILAGTVIFLVSFSGCVGALRENTFLLKFYSMCLLLFFLLEMAIAIVCFVCPQYMNTFLEKQFTHKIIHSYRDDPDLQNFIDFAQQEFKCCGLSNSGYQDWSKNEYFNCSSPSVEKCGVPYSCCINATDISSGLVNIMCGYGVQNAPVPEATKLIWTSGCIEIVRVWAEHNLYVIAGNALGIALIQLLVIYLAKTLEGQIELQKSRWLA
Protein: Ubiquitin-conjugating enzyme E2 22 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme 22) (Ubiquitin carrier protein 22) (Q9FF66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins.
Interaction partners:
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 6
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 7
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 11 RING-H2 finger protein
Sequence:
MASNENLPPNVIKQLAKELKSLDESPPDGIKVVVNDEDFSQICADIEGPVGTPYENGLFRMKLALSHDFPHSPPKGYFMTKIFHPNVASNGEICVNTLKKDWNPSLGLRHVLSVVRCLLIEPFPESALNEQAGKMLLENYDEYARHARLYTGIHAKPKPKFKTGAISESTTALNVGQTNNETPGAATAIPSSMTDIKRVTTSAQDQQHVANVVVAASASVVTTTQKREAGLAKVQADKKKVDARKKSLKRL
Protein: Glutathione S-transferase U21 (AtGSTU21) (EC 2.5.1.18) (GST class-tau member 21) (F4IA73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase DHAR3, chloroplastic
- Glutathione S-transferase F8, chloroplastic
- Glutathione S-transferase L2, chloroplastic
- Glutathione S-transferase DHAR2
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase F14
- Glutathione S-transferase F7
- Glutathione synthetase, chloroplastic
- Glutathione S-transferase F13
Sequence:
MAAEVILLGFWPSMFGMRTMIALEEKGVKYEYREEDVINNKSPLLLEMNPIHKTIPVLIHNGKPVLESLIQIQYIDEVWSDNNSFLPSDPYHRAQALFWADFIDKKEQLYVCGRKTWATKGEELEAANKEFIEILKTLQCELGEKPYFGGDKFGFVDIVLIGFYSWFPAYQKFGNFSIEPECLKLIAWGKRCMQRESVAKALPDSEKVVGYVLQLKKLYGIE
Protein: Protein myomixer (P0DP88)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Myoblast-specific protein that mediates myoblast fusion, an essential step for the formation of multi-nucleated muscle fibers. Involved in membrane fusion downstream of the lipid mixing step mediated by mymk. Acts by generating membrane stresses via its extracellular C-terminus, leading to drive fusion pore formation (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:29078404}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q2Q5T5}.
Interaction partners:
Sequence:
MPAVFLLLRSLVVRLFGSRLAASGVQLLRRILTTATGHLGTVLRNIWERISSQQSKEAILGCVLCLLNMHKKVDN
Protein: 23S rRNA (guanine(745)-N(1))-methyltransferase (EC 2.1.1.187) (23S rRNA m1G745 methyltransferase) (Ribosomal RNA large subunit methyltransferase A) (P36999)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates the guanosine in position 745 of 23S rRNA.
Interaction partners:
- 23S rRNA
- tRNA
- tRNA
- Peptidoglycan D,D-transpeptidase FtsI
- Cold shock-like protein CspC
Sequence:
MSFSCPLCHQPLSREKNSYICPQRHQFDMAKEGYVNLLPVQHKRSRDPGDSAEMMQARRAFLDAGHYQPLRDAIVAQLRERLDDKATAVLDIGCGEGYYTHAFADALPEITTFGLDVSKVAIKAAAKRYPQVTFCVASSHRLPFSDTSMDAIIRIYAPCKAEELARVVKPGGWVITATPGPRHLMELKGLIYNEVHLHAPHAEQLEGFTLQQSAELCYPMRLRGDEAVALLQMTPFAWRAKPEVWQTLAAKEVFDCQTDFNIHLWQRSY
Protein: Meiotically up-regulated gene 112 protein (O74981)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Meiotically up-regulated gene 133 protein
- Meiotic fizzy-related protein 2
- Serine/threonine-protein kinase ppk33
- Meiotically up-regulated gene 8 protein
- Meiotically up-regulated gene 24 protein
Sequence:
MEVQKIWKSFLNAISKVFSKGKKLRCTCFPKRKKEASERSCFPFLDTETISSCDLSDDVLSPKLFAKNSYRCSLKETKCIDVIVSHNSLAPQFTEIRYTDGISAKAENTDEMTMHIALAPLTENQ
Protein: Serrate RNA effector molecule homolog (Arsenite-resistance protein 2) (Q9BXP5)
Organism: Homo sapiens (Human)
Function: Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Predominantly nuclear. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent way (By similarity). {ECO:0000250}.
Interaction partners:
- Nuclear cap-binding protein subunit 1
- Nuclear cap-binding protein subunit 2
- THO complex subunit 4
- Phosphorylated adapter RNA export protein
- Spliceosome RNA helicase DDX39B
- Granulysin
- Neurogenic locus notch homolog protein 1
- Exosome RNA helicase MTR4
- RNA-binding protein 39
- RNA-binding protein 7
Sequence:
MGDSDDEYDRRRRDKFRRERSDYDRSRERDERRRGDDWNDREWDRGRERRSRGEYRDYDRNRRERFSPPRHELSPPQKRMRRDWDEHSSDPYHSGYEMPYAGGGGGPTYGPPQPWGHPDVHIMQHHVLPIQARLGSIAEIDLGVPPPVMKTFKEFLLSLDDSVDETEAVKRYNDYKLDFRRQQMQDFFLAHKDEEWFRSKYHPDEVGKRRQEARGALQNRLRVFLSLMETGWFDNLLLDIDKADAIVKMLDAAVIKMEGGTENDLRILEQEEEEEQAGKPGEPSKKEEGRAGAGLGDGERKTNDKDEKKEDGKQAENDSSNDDKTKKSEGDGDKEEKKEDSEKEAKKSSKKRNRKHSGDDSFDEGSVSESESESESGQAEEEKEEAEEALKEKEKPKEEEWEKPKDAAGLECKPRPLHKTCSLFMRNIAPNISRAEIISLCKRYPGFMRVALSEPQPERRFFRRGWVTFDRSVNIKEICWNLQNIRLRECELSPGVNRDLTRRVRNINGITQHKQIVRNDIKLAAKLIHTLDDRTQLWASEPGTPPLPTSLPSQNPILKNITDYLIEEVSAEEEELLGSSGGAPPEEPPKEGNPAEINVERDEKLIKVLDKLLLYLRIVHSLDYYNTCEYPNEDEMPNRCGIIHVRGPMPPNRISHGEVLEWQKTFEEKLTPLLSVRESLSEEEAQKMGRKDPEQEVEKFVTSNTQELGKDKWLCPLSGKKFKGPEFVRKHIFNKHAEKIEEVKKEVAFFNNFLTDAKRPALPEIKPAQPPGPAQILPPGLTPGLPYPHQTPQGLMPYGQPRPPILGYGAGAVRPAVPTGGPPYPHAPYGAGRGNYDAFRGQGGYPGKPRNRMVRGDPRAIVEYRDLDAPDDVDFF
Protein: Growth/differentiation factor 8 (GDF-8) (Myostatin) (O42220)
Organism: Gallus gallus (Chicken)
Function: Acts specifically as a negative regulator of skeletal muscle growth.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Activin receptor type-2B
- Follistatin
- TGF-beta receptor type-1
- Receptor protein serine/threonine kinase
- Follistatin like 3.
- Activin receptor type-2A
- Myogenin
- Myoblast determination protein 1 homolog
- Myogenic factor 5
- Mothers against decapentaplegic homolog
Sequence:
MQKLAVYVYIYLFMQIAVDPVALDGSSQPTENAEKDGLCNACTWRQNTKSSRIEAIKIQILSKLRLEQAPNISRDVIKQLLPKAPPLQELIDQYDVQRDDSSDGSLEDDDYHATTETIITMPTESDFLVQMEGKPKCCFFKFSSKIQYNKVVKAQLWIYLRQVQKPTTVFVQILRLIKPMKDGTRYTGIRSLKLDMNPGTGIWQSIDVKTVLQNWLKQPESNLGIEIKAFDETGRDLAVTFPGPGEDGLNPFLEVRVTDTPKRSRRDFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
Protein: Hypersensitive to pore-forming toxin protein 40 (Q23647)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:32338603}. Note=Localizes to perinuclear foci in germ cells (PubMed:32338603). Its localization at perinuclear foci is either adjacent to or co-localized with mutator complex protein mut-16 (PubMed:32338603). {ECO:0000269|PubMed:32338603}.
Interaction partners:
- Protein F37C4.5
- Non-specific serine/threonine protein kinase
- Cyclin-dependent kinase 12
- Cyclin-T1.1
- Zc3h12a-like Ribonuclease NYN domain-containing protein
- Zc3h12a-like Ribonuclease NYN domain-containing protein
Sequence:
MNSQQEWEHAYSLAERMYNKQAPTKREELNPTERVICSRFETIFDYDPFKDEYTFRDQALLFSTPVQPKCRTVAEADLHELKENTAKLNIPMPSYINICPIYALLPFTVLVFNNSQHAHKSLSDDMERAAATFRNPHESEIVPGAMYIFKQKHGKAYRCIILSEDGDMNIPDAERKYLVAFIDNVQIVSVKQKTLFVSDQFSIKDYPCALHCARIVGISAIRKSYVSGMNQFILNFYDAKEKRKAGMFAFIYKLDKEEKKLVIDYPSLLGTPKTTSTEIRTAVGHQIVASKDPVSLTFEQLNKKEVPEFKYLNSTDDDSDVELDLIEHDTKSVNPVASSHPTSSSMDDCPYGRASIARAKDYQLRLPPHSQKGLSSSSLLGSSYPVSNSIKNDITKQSESNRADATNISFSSFESTKSDISPQNNQNVEETSTPTVPPNSTIQENEEDEIMSPASIIRAPSRLAGSLNKVSIERPNTPLPTSSKNSEHNMSEISTYEASSISSHHLVPQSPSVPKTNYTVPVVQRPLTAPEKFRDPFGGPGSSDILNTKMLCSEKNIVPSNKFGRQISPGKDDKNENYQYSRMETKPQTLFAPVLDENQRQSSSSNMMCQIPDISSVAQGSNAPKTAPNDSVNSVAPDDIHETDKRGNHCKSVTEDPKDNKDPTAVTTLEDPDINDENFSVQSICSETFVETDQKLMEVETGADAFTESITDQFAQMSEGLKKLAINLADSVRTAAIEKNHDAFIANIHAMEIISKKVPDDIDKRFWKMKIVEARKLEAAFD
Protein: Tenomodulin (TeM) (hTeM) (Chondromodulin-1-like protein) (ChM1L) (hChM1L) (Chondromodulin-I-like protein) (Myodulin) (Tendin) (Q9H2S6)
Organism: Homo sapiens (Human)
Function: May be an angiogenesis inhibitor.
Subcellular location: [Isoform 1]: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Nucleus envelope.; SUBCELLULAR LOCATION: [Isoform 2]: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Nucleus envelope.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.
Interaction partners:
- Basic helix-loop-helix transcription factor scleraxis
- Homeobox protein Mohawk
- Decorin
- Collagen alpha-1
- Fibromodulin
- Thrombospondin-4
- Growth/differentiation factor 7
Sequence:
MAKNPPENCEDCHILNAEAFKSKKICKSLKICGLVFGILALTLIVLFWGSKHFWPEVPKKAYDMEHTFYSNGEKKKIYMEIDPVTRTEIFRSGNGTDETLEVHDFKNGYTGIYFVGLQKCFIKTQIKVIPEFSEPEEEIDENEEITTTFFEQSVIWVPAEKPIENRDFLKNSKILEICDNVTMYWINPTLISVSELQDFEEEGEDLHFPANEKKGIEQNEQWVVPQVKVEKTRHARQASEEELPINDYTENGIEFDPMLDERGYCCIYCRRGNRYCRRVCEPLLGYYPYPYCYQGGRVICRVIMPCNWWVARMLGRV
Protein: 14-3-3 protein epsilon (14-3-3E) (P62258)
Organism: Homo sapiens (Human)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner (By similarity). Positively regulates phosphorylated protein HSF1 nuclear export to the cytoplasm.
Subcellular location: Nucleus {ECO:0000269|PubMed:12917326, ECO:0000269|PubMed:37599448}. Cytoplasm {ECO:0000269|PubMed:12917326}. Melanosome {ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:12042314, ECO:0000269|PubMed:17081065}.
Interaction partners:
- M-phase inducer phosphatase 3
- 14-3-3 protein zeta/delta
- M-phase inducer phosphatase 2
- Serine/threonine-protein kinase B-raf
- RAF proto-oncogene serine/threonine-protein kinase
- 14-3-3 protein gamma
- WW domain-containing transcription regulator protein 1
- Myeloid leukemia factor 1
- 14-3-3 protein theta
- Bcl2-associated agonist of cell death
Sequence:
MDDREDLVYQAKLAEQAERYDEMVESMKKVAGMDVELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEENKGGEDKLKMIREYRQMVETELKLICCDILDVLDKHLIPAANTGESKVFYYKMKGDYHRYLAEFATGNDRKEAAENSLVAYKAASDIAMTELPPTHPIRLGLALNFSVFYYEILNSPDRACRLAKAAFDDAIAELDTLSEESYKDSTLIMQLLRDNLTLWTSDMQGDGEEQNKEALQDVEDENQ
Protein: SLIT and NTRK-like protein 2 (Q810C0)
Organism: Mus musculus (Mouse)
Function: It is involved in synaptogenesis. Promotes excitatory synapse differentiation (By similarity). Suppresses neurite outgrowth.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:Q9H156}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9H156}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase delta
- Neuroligin-1
- Receptor-type tyrosine-protein phosphatase S
Sequence:
MLSGVWFLSVLTVAGILQTESRKTAKDICKIRCLCEEKENVLNINCENKGFTTVSLLQPPQYRIYQLFLNGNLLTRLYPNEFVNYSNAVTLHLGNNGLQEIRPGAFSGLKTLKRLHLNNNKLEVLREDTFLGLESLEYLQADYNYISTIEAGAFSKLNKLKVLILNDNLLLSLPSNVFRFVLLTHLDLRGNRLKVMPFAGVLEHIGGIMEIQLEENPWNCTCDLLPLKAWLDTITVFVGEIVCETPFRLHGKDVTQLTRQDLCPRKSASGDSSQRSSHSDTHVQRLTPTTNPALNPTRAPKASRPPKMRNRPTPRVTVSKDRQSFGPIMVYQTKSPVALTCPSSCVCTSQSSDNGLNVNCQERKFTNISDLQPKPTSPKKLYLTGNYLQTVYKNDLLEYSSLDLLHLGNNRIAVIQEGAFTNLTSLRRLYLNGNYLEVLYPSMFDGLQSLQYLYLEYNVIKEIKPLTFDALINLQLLFLNNNLLRSLPDNIFGGTALTRLNLRNNHFSHLPVKGVLDQLPAFIQIDLQENPWDCTCDIMGLKDWTEHANSPVIINEVTCESPAKHAGEILKFLGREAICPENPNLSDGTILSMNHNTDTPRSLSVSPSSYPELHTEVPLSVLILGLLVVFILSVCFGAGLFVFVLKRRKGVPNVPRNATNLDVSSFQLQYGSYNTETNDKADGHVYNYIPPPVGQMCQNPIYMQKEGDPVAYYRNLQDFSYGNLEEKKEEPATLAYTISATELLEKQATPREPELLYQNIAERVKELPSAGLVHYNFCTLPKRQFAPSYESRRQNQDRINKTVLYGTPRKCFVGQSKPDHPLLQAKPQSEPDYLEVLEKQTAISQL
Protein: Adenosine deaminase (EC 3.5.4.4) (Adenosine aminohydrolase) (P56658)
Organism: Bos taurus (Bovine)
Function: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine (By similarity). Plays an important role in purine metabolism and in adenosine homeostasis (By similarity). Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events (By similarity). Acts as a positive regulator of T-cell coactivation, by binding DPP4 (By similarity). Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion (By similarity). Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion. Enhances CD4+ T-cell differentiation and proliferation (By similarity). Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change (By similarity). Stimulates plasminogen activation (By similarity). Plays a role in male fertility (By similarity). Plays a protective role in early postimplantation embryonic development (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P00813}; Peripheral membrane protein {ECO:0000250}; Extracellular side {ECO:0000250}. Cell junction {ECO:0000250|UniProtKB:P00813}. Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P03958}. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000250|UniProtKB:P00813}. Note=Colocalized with DPP4 at the cell surface. {ECO:0000250|UniProtKB:P00813}.
Interaction partners:
- Dipeptidyl peptidase 4
- Adenosine kinase
- Purine nucleoside phosphorylase
- 5'-nucleotidase
- Adenosine deaminase 2
- Deoxycytidine kinase
- 5', 3'-nucleotidase
- 5',3'-nucleotidase
- Cytosolic purine 5'-nucleotidase
- Adenine phosphoribosyltransferase
Sequence:
MAQTPAFNKPKVELHVHLDGAIKPETILYYGRKRGIALPADTPEELQNIIGMDKPLSLPEFLAKFDYYMPAIAGCREAVKRIAYEFVEMKAKDGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVSLVNQGLQEGERDFGVKVRSILCCMRHQPSWSSEVVELCKKYREQTVVAIDLAGDETIEGSSLFPGHVKAYAEAVKSGVHRTVHAGEVGSANVVKEAVDTLKTERLGHGYHTLEDATLYNRLRQENMHFEVCPWSSYLTGAWKPDTEHPVVRFKNDQVNYSLNTDDPLIFKSTLDTDYQMTKNEMGFTEEEFKRLNINAAKSSFLPEDEKKELLDLLYKAYGMPSPASAEQCL
Protein: Growth hormone receptor (GH receptor) (Somatotropin receptor) [Cleaved into: Growth hormone-binding protein (GH-binding protein) (GHBP) (Serum-binding protein)] (P16310)
Organism: Rattus norvegicus (Rat)
Function: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to, and activates the JAK2/STAT5 pathway.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P10912}; Single-pass type I membrane protein {ECO:0000255}. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway. {ECO:0000250|UniProtKB:P19941}.; SUBCELLULAR LOCATION: [Growth hormone-binding protein]: Secreted {ECO:0000250|UniProtKB:P10912}. Note=Complexed to a substantial fraction of circulating GH. {ECO:0000250|UniProtKB:P10912}.
Interaction partners:
- Tyrosine-protein kinase JAK2
- Somatotropin
- Insulin-like growth factor 1
- Prolactin
- Prolactin-6A1
- Signal transducer and activator of transcription 5B
- Tyrosine-protein kinase
- Suppressor of cytokine signaling 2
- Signal transducer and activator of transcription 5A
- Tyrosine-protein kinase JAK3
Sequence:
MDLWRVFLTLALAVSSDMFPGSGATPATLGKASPVLQRINPSLRESSSGKPRFTKCRSPELETFSCYWTEGDDHNLKVPGSIQLYYARRIAHEWTPEWKECPDYVSAGANSCYFNSSYTSIWIPYCIKLTTNGDLLDEKCFTVDEIVQPDPPIGLNWTLLNISLPGIRGDIQVSWQPPPSADVLKGWIILEYEIQYKEVNETKWKTMSPIWSTSVPLYSLRLDKEHEVRVRSRQRSFEKYSEFSEVLRVTFPQMDTLAACEEDFRFPWFLIIIFGIFGVAVMLFVVIFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILGIHDNYKPDFYNDDSWVEFIELDIDDADEKTEESDTDRLLSDDQEKSAGILGAKDDDSGRTSCYDPDILDTDFHTSDMCDGTSEFAQPQKLKAEADLLCLDQKNLKNSPYDASLGSLHPSITLTMEDKPQPLLGSETESTHQLPSTPMSSPVSLANIDFYAQVSDITPAGGVVLSPGQKIKAGLAQGNTQLEVAAPCQENYSMNSAYFCESDAKKCIAAAPHMEATTCVKPSFNQEDIYITTESLTTTARMSETADTAPDAEPVPDYTTVHTVKSPRGLILNATALPLPDKKKFLSSCGYVSTDQLNKIMQ
Protein: Immunoglobulin lambda variable 3-19 (Ig lambda chain V-III region SH) (P01714)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MAWTPLWLTLLTLCIGSVVSSELTQDPAVSVALGQTVRITCQGDSLRSYYASWYQQKPGQAPVLVIYGKNNRPSGIPDRFSGSSSGNTASLTITGAQAEDEADYYCNSRDSS
Protein: Disintegrin and metalloproteinase domain-containing protein 11 (ADAM 11) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein) (MDC) (Q9R1V4)
Organism: Mus musculus (Mouse)
Function: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Required for localization of the potassium channel subunit proteins KCNA1/KV1.1 and KCNA2/KV1.2 at cerebellar cortex basket cell distal terminals, is thereby involved in ephaptic inhibitory synchronization of Purkinje cell firing and response to stress. Plays a role in spatial learning and motor coordination. Involved in the nociceptive pain response to chemical-derived stimulation.
Subcellular location: Presynaptic cell membrane {ECO:0000269|PubMed:26269648}; Single-pass type I membrane protein. Perikaryon {ECO:0000269|PubMed:26269648}. Cell projection, axon {ECO:0000269|PubMed:26269648}. Note=Localizes to basket cell terminals and pinceaux. {ECO:0000269|PubMed:26269648}.
Interaction partners:
- Leucine-rich glioma-inactivated protein 1
- Leucine-rich repeat LGI family member 4
Sequence:
MRRLRRWAIAALLLLPLLPPPGLGALGPRGALHWRSSAHVGSPESPEGSEVTEPSRLVRQSSGGEVRKPQLDTRVRQDPPRGTPVHLAQVSFVIPAFDSNFTLDLELNHHLLSSQYVERHFSREGTRQHSTGAGDHCYYHGKLRGNPQSFAALSTCQGLHGVFSDGNLTYIVEPKEIAGPWGPPQGPLPHLIYRTPLLPAPLGCREPGCLFAVPAQSALPNWPKLRRKRQVRRGHPTVHSETKYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRREGLPEPSDATHLFSGRTFQSTSSGAAYVGGICSLSRGGGVNEYGNMGAMAVTLAQTLGQNLGMMWNKHRSSAGDCKCPDIWLGCIMEDTGFYLPRKFSRCSIDEYNQFLQEGGGSCLFNKPLKLLDPPECGNGFVEAGEECDCGSVQECSRAGGNCCKKCTLTHDAMCSDGLCCRRCKYEPRGVSCREAVNECDIAETCTGDSSQCPPNLHKLDGYYCDHEQGRCYGGRCKTRDRQCQALWGHAAADRFCYEKLNVEGTERGNCGRKGSGWVQCSKQDVLCGFLLCVNISGAPRLGDLGGDISSVTFYHQGKELDCRGGHVQLADGSDLSYVEDGTACGPNMLCLDHRCLPASAFNFSTCPGSGERRICSHHGVCSNEGKCICQPDWTGKDCSIHNPLPTSPPTGETERYKGPSGTNIIIGSIAGAVLVAAIVLGGTGWGFKNIRRGRSGGA
Protein: SLIT and NTRK-like family, member 2 (D3ZK41)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase delta
- Receptor-type tyrosine-protein phosphatase S
- Interleukin-1 receptor accessory protein-like 1
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L2
- Neuroligin-1
Sequence:
MLSGVWFLSVFTVAGILQIESRKTAKDICKIRCLCEEKENVLNINCENKGFTTVSLLQPPQYRIYQLFLNGNLLTRLYPNEFVNYSNAVTLHLGNNGLQEIRPGAFSGLKTLKRLHLNNNKLEVLREDTFLGLESLEYLQADYNYISTIEAGAFSKLNKLKVLILNDNLLLSLPSNVFRFVLLTHLDLRGNRLKVMPFAGVLEHIGGIMEIQLEENPWNCTCDLLPLKAWLDTITVFVGEIVCETPFRLHGKDVTQLTRQDLCPRKSASGDSSQRSSHSDTHVQRLSPTMNPALNPTRAPKASRPPKMRNRPTPRVTVSKDRQSFGPIMVYQTKSPVALTCPSSCVCTSQSSDNGLNVNCQERKFTNISDLQPKPTSPKKLYLTGNYLQTVYKNDLLEYTSLDLLHLGNNRIAVIQEGAFTNLTSLRRLYLNGNYLEVLYPSMFDGLQSLQYLYLEYNVIKEIKPLTFDALINLQLLFLNNNLLRSLPDNIFGGTALTRLNLRNNHFSHLPVKGVLDQLPAFIQIDLQENPWDCTCDIMGLKDWTEHANSPVIINEVTCESPAKHAGEILKFLGREAICPDNPNLSDGTVLSMNHNTDTPRSLSVSPSSYPELHTEVPLSVLILGLLVVFILSVCFGAGLFVFVLKRRKGVPSVPRSATNLDVSSFQLQYGSYNTETNDKTDGHVYNYIPPPVGQMCQNPIYMQKEGDPVAYYRNLQDFSYGNLEEKKEEPATLAYTISATELLEKQATPKEPELLYQNIAERAKELPSAGLVHYNFCTLPKRQFAPSYESRRQNQDRINKTVLYGTPRKCFVGQSKPDHPLLQAKPQSEPDYLEVLEKQTAISQL