wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized AAA domain-containing protein C16E9.10c (O14325)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ribosome biogenesis protein nsa1
- Uncharacterized RNA-binding protein C4F6.14
- Ribosome biogenesis protein ytm1
- ATP-dependent RNA helicase mak5
- Ribosome assembly protein 4
- Pescadillo homolog
- Ribosome biogenesis protein erb1
- Probable nucleolar GTP-binding protein 1
- Nucleolar complex-associated protein 3
- Nucleolar GTP-binding protein 2
Sequence:
MRRSGTSLSRDLERKIHERLVSLKDTIQQTEIEEWPVSTRRAIQFVQERDMSLRRIKKPILEKVVEKVLDTLKAEVEEKLASSQDLVLVDSDMEEQSDSNLMEVKDTNVINKSITSLWSSPNLKEIDGEDEKKSVGQESITGSAKRKDRRSKTNGSKRQKAEANREPPSDISLSDIGGLDDCINELLELVAMPIKHPEVYQYTGIHPPRGVLLHGPPGCGKTMLANALANELGVPFISISAPSIVSGMSGESEKKVREVFEEAKSLAPCLMFIDEIDAVTPKRESAQREMERRIVAQFLTCMDELSFEKTDGKPVLVIGATNRPDSLDSALRRAGRFDREICLTVPSQDAREKILRTMAKGLKLSGDFDFRQLAKQTPGYVGADLKALTAAAGIIAIKRIFNEISPLNKLDLNSDPRFNELDSDMALDSNDSLPLDHSSIIQRYLNAHPDPLSPEELEPLAICPQDFIEALAKVQPSSKREGFATVPGVSWNNIGALKSIRVELQMAIVQPIKRPELYQSVGISAPTGVLLWGPPGCGKTLLAKAVANESKANFISIRGPELLNKYVGESERAVRQVFLRARASSPCVIFFDELDAMVPRRDDSLSEASSRVVNTLLTELDGLSDRSGVYVIAATNRPDIIDPAMLRPGRLDKTLLVDLPDAHERVEILKTLTKQTPLHEEVNLDVLGRDERCSNFSGADLAALVREAAVTALRSAVFADIASNEPEITQHSALEPIRVTNADFELAFKNIKPSVSDRDRQKYQRLAKRWSSASTNDAD
Protein: Group IID secretory phospholipase A2 (GIID sPLA2) (sPLA2-IID) (EC 3.1.1.4) (PLA2IID) (Phosphatidylcholine 2-acylhydrolase 2D) (Secretory-type PLA, stroma-associated homolog) (Q9WVF6)
Organism: Mus musculus (Mouse)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular lipids, exerting anti-inflammatory and immunosuppressive functions. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines (By similarity). In draining lymph nodes, selectively hydrolyzes diacyl and alkenyl forms of phosphatidylethanolamines, releasing omega-3 polyunsaturated fatty acids (PUFAs) such as eicosapentaenoate and docosahexaenoate that are precursors of the anti-inflammatory lipid mediators, resolvins. During the resolution phase of acute inflammation drives docosahexaenoate-derived resolvin D1 synthesis, which suppresses dendritic cell activation and T-helper 1 immune response. May act in an autocrine and paracrine manner. Via a mechanism independent of its catalytic activity, promotes differentiation of regulatory T cells (Tregs) and participates in the maintenance of immune tolerance. May contribute to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane.
Subcellular location: [Isoform 1]: Secreted {ECO:0000269|PubMed:10455175}. Cell membrane {ECO:0000269|PubMed:19564598}. Note=Localizes to cell membrane likely through binding to heparan sulfate proteoglycans. {ECO:0000269|PubMed:19564598}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
Interaction partners:
- Group XIIA secretory phospholipase A2
- Group XIIB secretory phospholipase A2-like protein
- Group 3 secretory phospholipase A2
- Cytochrome P450 2E1
- Phospholipase A and acyltransferase 3
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Group 10 secretory phospholipase A2
- Phospholipase A2
- Group IIE secretory phospholipase A2
- Phospholipase A2 group V
Sequence:
MRLALLCGLLLAGITATQGGLLNLNKMVTHMTGKKAFFSYWPYGCHCGLGGKGQPKDATDWCCQKHDCCYAHLKIDGCKSLTDNYKYSISQGTIQCSDNGSWCERQLCACDKEVALCLKQNLDSYNKRLRYYWRPRCKGKTPAC
Protein: Ras-specific guanine nucleotide-releasing factor RalGPS2 (Ral GEF with PH domain and SH3-binding motif 2) (RalA exchange factor RalGPS2) (Q86X27)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor for the small GTPase RALA. May be involved in cytoskeletal organization. May also be involved in the stimulation of transcription in a Ras-independent fashion (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Note=Associates with membranes through the PH domain. {ECO:0000250}.
Interaction partners:
- Testis-expressed protein 35
- Regulator of G-protein signaling protein-like
- 14-3-3 protein zeta/delta
- Leukocyte-specific transcript 1 protein
- Ras-related protein Ral-A
- Glutamate receptor-interacting protein 1
Sequence:
MDLMNGQASSVNIAATASEKSSSSESLSDKGSELKKSFDAVVFDVLKVTPEEYAGQITLMDVPVFKAIQPDELSSCGWNKKEKYSSAPNAVAFTRRFNHVSFWVVREILHAQTLKIRAEVLSHYIKTAKKLYELNNLHALMAVVSGLQSAPIFRLTKTWALLSRKDKTTFEKLEYVMSKEDNYKRLRDYISSLKMTPCIPYLGIYLSDLTYIDSAYPSTGSILENEQRSNLMNNILRIISDLQQSCEYDIPMLPHVQKYLNSVQYIEELQKFVEDDNYKLSLKIEPGTSTPRSAASREDLVGPEVGASPQSGRKSVAAEGALLPQTPPSPRNLIPHGHRKCHSLGYNFIHKMNTAEFKSATFPNAGPRHLLDDSVMEPHAPSRGQAESSTLSSGISIGSSDGSELSEETSWPAFERNRLYHSLGPVTRVARNGYRSHMKASSSAESEDLAVHLYPGAVTIQGVLRRKTLLKEGKKPTVASWTKYWAALCGTQLFYYAAKSLKATERKHFKSTSNKNVSVIGWMVMMADDPEHPDLFLLTDSEKGNSYKFQAGNRMNAMLWFKHLSAACQSNKQQVPTNLMTFE
Protein: Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) (P83780)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: In the cytoplasm, catalyzes the conversion of glucose-6-phosphate to fructose-6-phosphate, the second step in glycolysis, and the reverse reaction during gluconeogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15378761}.
Interaction partners:
- Phosphoglycerate kinase
- Triosephosphate isomerase
- Enolase 1
- Pyruvate kinase
- ATP-dependent 6-phosphofructokinase
- phosphoglucomutase
- Phosphoglycerate mutase
- Fructose-bisphosphate aldolase
- Glucose-6-phosphate 1-dehydrogenase
- Transketolase
Sequence:
MASFKLATDLPEWKKLEETYKSVGEKFSVRDAFAKDPKRFEEFSWIYKNYDDSKILFDFSKNLVNKEILDQLVTLAKEAGVEKLRDAMFAGDHINTTEDRAVYHVALRNRALRKMPVDGKDTAQEVDDVLKHMKEFSDSIRDGSWTGYTGKSITDVVNIGIGGSDLGPVMVTEALKAYSKPGLNVHFISNIDGTHTAETLKNLNPETTLFLIASKTFTTAETITNATSAKNWFLATAKDSKHIAKHFAALSTNEKEVVAFGIDAKNMFGFESWVGGRYSVWSAIGLSVAIYIGFENFNDFLKGAEAMDQHFLTTPLENNIPVIGGLLSVWYNNFFGAQTHLVVPFDQYLHRFPAYLQQLSMESNGKSVTRANVFTNYQTGTILFGEPATNAQHSFFQLVHQGTKLIPADFILAAQSHNPIEKNLHQRMLASNFFAQSEALMVGKDEAKVKAEGATGGLVPHKEFSGNRPTTSILAQKITPATLGSLIAYYEHLTFTEGAIWNINSFDQWGVELGKVLAKVIGKELDDKKAVATHDASTNGLINQFKEWEE
Protein: SR-CI (Q5ELS5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEFFWTLAVIVIYCIGHIHGRCERSLDLDNGSINYRPRNIVRFRCNRGYTLQGTVMQTCDRDGRLRGEKPFCASRGCAKPEDPENGHVENLSLRADVVCHDGYVLVGGRTAYCDGERWSTQLGSCRRSNHTRDHSCDFESEDQCGWEAETTFRRPWKRVSTVSDIHSLRTGPRHDHTFKNESGGHYMRMETQMGAYGSYHLLSPIYPRSLTLKTACCFRFHYFMFGAGVDTLVVSVKPVSMPMATMWNRFRANCSKFEISGQQGTQWLEHTISIDEMQEDFQVIFTATDARSQFGDIAIDDVKLMTGSECGTNGFSTTTEPTAPTGSNEQPLVYDMMSCSGRCGTSISASNITNNGIVMGCGCNDECLSDETCCLNYLEECTKEMLTTTEDDISSVPPTVTSTSTSTTRKSTTTTTTSTTSTSTTTTKRPTTTTTTTKATTTKRTTTTKKPTTTSTTPKPTTTTSTTPKSTTSTTSTTSTTPTTTTTINVFTTKKTTIMIPTSSTEKTTGINTTMKTRKRITWNVDPQDIEGHMDTSGSTPNPALVVLYLLLAIVLVVVLANVVNRWIIPITGSKTSSEKAVRFKKAFDSLKKQRKRNSMDDQPLCDSDNDDVEYFEEMGVDIRHRTDL
Protein: Membrane-associated phosphatidylinositol transfer protein 1 (Phosphatidylinositol transfer protein, membrane-associated 1) (PITPnm 1) (Pyk2 N-terminal domain-interacting receptor 2) (NIR-2) (Q5U2N3)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of phosphatidylinositol (PI) between membranes (By similarity). Binds PI, phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding affinity order of PI > PA > PC (By similarity). Regulates RHOA activity, and plays a role in cytoskeleton remodeling (By similarity). Necessary for normal completion of cytokinesis (By similarity). Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus (By similarity). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus (By similarity). Required for protein export from the endoplasmic reticulum and the Golgi (By similarity). Binds calcium ions (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O00562}. Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:O00562}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00562}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00562}; Peripheral membrane protein {ECO:0000250|UniProtKB:O00562}. Lipid droplet {ECO:0000250|UniProtKB:O00562}. Cleavage furrow {ECO:0000250|UniProtKB:O00562}. Midbody {ECO:0000250|UniProtKB:O00562}. Note=Peripheral membrane protein associated with Golgi stacks in interphase cells. A minor proportion is associated with the endoplasmic reticulum. Associated with lipid droplets. Dissociates from the Golgi early on in mitosis and localizes to the cleavage furrow and midbody during cytokinesis. {ECO:0000250|UniProtKB:O00562}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein B
- Protein-tyrosine kinase 2-beta
- Vesicle-associated membrane protein-associated protein A
- Oxysterol-binding protein
Sequence:
MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGNGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRLYRSVKTGRGPLADDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWIELSMADIRALEEETARMLAQRMAKCNTGSEGPEAQTPGKPSTETQPGTRTAGTPDGPEAPPGPDASPDASFGKQWSSSSRSSYSSQHGGGVSPQSLSEWRMQNIARDSENSSEEEFFDAHEGFSDSDEVFPKEMTKWNSNDFIDAFASPTEVEGVPDPAIMATKGIEDEARAPRDSEGLDGTGDLGVEACSVHALFLILHSGSILDSGPGDTNSKQADVQTLSTAFEAVTRVHFPEALGHVALRLVPCPPICAAAYALVSNLSPYSHDGDSLSRSQDHIPLAALPLLATSSSRYQGAVATVIARTNQAYAAFLRSSEGTGFCGQVVLIGDGVGGILGFDALCHSASAGTGSRGSSRRGSMNNEMLSPEVGPVRDPLADGVEVLGRASPEPSALPAQRTSSDMANPDPDGSQNSLQVAPTVTSGEPRRASTASCPPASSEAPDGPTNAARLDFKVSGFFLFGSPLGLVLALRKTVMPALEVAQMRPACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLAVPRYQKFPLGDGSSLLLADTLQTHSSLFLEELEMMVPSTPTSASGAFWKGNELGNEPAAQPAAPSTTSEVVKILDRWWGNKRIDYSLYCPEALTAFPTVTLPHLFHASYWESADVVAFILRQVIEKERPQLTECEEPSIYSPAFPREKWQRKRTQVKIRNVTSNHRASDTVVCEGRPQVLNGRFMYGPLDVVTLTGEKVDVYVMTQPLSGKWIHFGTEVTNSSGRLTFPVPSERALGIGVYPVRMVVRGDHTYAECCLTVVSRGTEAVVFSIDGSFTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWLSQHNFPHGVVSFCDGLTHDPLRQKAMFLQSLVQEVELNIVAGYGSPKDVAVYAALGLSPSQTYIVGRAVRKLQAQCQFLSDGYVAHLGQLEAGSHSHAPSGPPRAALAKSSYAVAAPVDFLRKQSQLLRSRGPSQVDLEGPGTPPTTLARGKTRSISLKLDSEE
Protein: Mitochondrial import inner membrane translocase subunit TIM54 (P47045)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential component of the TIM22 complex, a complex that mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. The TIM22 complex forms a twin-pore translocase that uses the membrane potential as external driving force. Its precise function within the TIM22 complex is unclear.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10397776, ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9412462}; Single-pass membrane protein {ECO:0000269|PubMed:10397776, ECO:0000269|PubMed:10637294, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9412462}. Note=Import into inner membrane protein requires TOM70 function.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM9
- Mitochondrial import inner membrane translocase subunit TIM22
- Mitochondrial import inner membrane translocase subunit TIM18
- Mitochondrial import inner membrane translocase subunit TIM12
- Mitochondrial import inner membrane translocase subunit TIM10
- Succinate dehydrogenase cytochrome b subunit
- Mitochondrial import inner membrane translocase subunit TIM44
- Mitochondrial import inner membrane translocase subunit TIM23
- Mitochondrial import inner membrane translocase subunit TIM17
- Mitochondrial import inner membrane translocase subunit TIM50
Sequence:
MSSESGKPIAKPIRKPGYTNPALKALGIPALRLPSRNWMIFWSVLTVSIGGIAYDKYKQRQILSHATDLVKPLAEESMEVDKVPRKITVFIAPPPNDYLESSLKVWRRYVKPVLYYAGLDYELVQEDRQGIIRTNVANRIRELRKEILASTDGQPVKEPNQTVAKPSGSSTSKISSLLPFNKIIQDPAEEDDSFDPEIGKKFKENFDWRNVIGIFYTMPKPKHIISEDALTKDPILSGGVICLGRGAYKEYIAGIHEGLLGPIEKTEKTGSTEPKMTGVVEANQIESKVSESGATELVDAEKETALEEAKVQDDLKVDEENSSEDSQKFLKPFISSDQYPDLQIASELQTPNGEFIRNPNTNIPLLINQPLLVIPIPNLIGFTTIPRRIHRFYQKRFYVEDVCSSVVNCVRQTRIRPFDIAKDIDLAKDEEKDWPQNWVKQGKEKNSEWTQELVCDPRITKHMFVYEKPPKEEPESDI
Protein: Eukaryotic translation initiation factor 4E (eIF-4E) (eIF4E) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) (P48597)
Organism: Xenopus laevis (African clawed frog)
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. In addition to its role in translation initiation, also acts as a regulator of translation and stability in the cytoplasm (By similarity). Maternal RNA in oocytes remain in a dormant state as tacc3/maskin outcompetes eif4g to bind eif4e, thereby preventing translation. During oocyte maturation this complex dissolves and eif4g binds eif4e to allow translation of maternal RNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10635326}. Nucleus {ECO:0000250|UniProtKB:P06730}. Note=Cytoplasmic when interacting with tacc3/maskin. {ECO:0000269|PubMed:10635326}.
Interaction partners:
Sequence:
MAAVEPENTNPQSTEEEKETGQEIVSPDQYIKHPLQNRWALWFFKNDKSKTWQANLRLISKFDTVEDFWALYNHIQLSSNLMSGCDYSLFKDGIEPMWEDEKNKRGGRWLITLNKQQRRNDLDRFWLETLMCLIGESFDEHSDDVCGAVVNVRAKGDKIAIWTTEFENKDAVTHIGRVYKERLGLPAKVVIGYQSHADTATKSGSTTKNRFVV
Protein: adenine phosphoribosyltransferase (EC 2.4.2.7) (H3BQZ9)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDYIAGECPVAASRALPPLRAPRAELEIQKDALEPGQRVVVVDDLLATGGTMNAACELLGRLQAEVLECVSLVELTSLKGREKLAPVPFFSLLQYE
Protein: DNA polymerase IV (Pol IV) (EC 2.7.7.7) (Q8Y5T0)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Function: Poorly processive, error-prone DNA polymerase involved in untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity. May be involved in translesional synthesis, in conjunction with the beta clamp from PolIII.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01113}.
Interaction partners:
- Beta sliding clamp
- LexA repressor
- NifJ protein
- Protein RecA
- Lmo0162 protein
- DNA polymerase I
- DNA polymerase III PolC-type
- 3'-5' exonuclease DinG
- Lmo0418 protein
Sequence:
MDTSRKIIHIDMDAFYASVEQRDHPEFRGKPLIIGGDPNKRGVVATCSYEARKFGVHSAMPTRQAAKLCPNGIFIHGNMAHYVEVSNQIREIFSRYTDIIEPLSLDEAYLDVTENKKGMKSATMVAREIQQTIYQELGLTASAGVSFNKFIAKIASDFKKPAGITVVTPEEAEAFLEQIPVTKFYGVGKVTAEKLHRLGIETGADLKKWSEWDLIRELHKHGYHLYRHVRGRSNNIVNPHRDRKSVGKETTFEFNVLDSRVLEQSLMQFAKKVEERLIKLQKHGKTVVLKLRYSDFTTITKRLTLNEYTNDASQIYQAAALLLIESYTGQDSIRLIGLTVTNLKPVYFENLRLEGL
Protein: Bone morphogenetic protein 3 (A0JML2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MDRCQRLFVLLLGCGYLCCGYCAVLKTPVMGFSKDVQLGQKAEEPEKQHVKKSEQDTLSEHMQMLYAKYTSAGFPLKDGNTVRSFKGHLGTINNRQLQIFNLTSLTKSEDVLSATLHYYIGDLHNSSHRCSKHKSCAQHNLRRQAHVHLDVWSFSLVKNTTRTIGHFPINISTMHWDFISWQWKDITRVVNQAKHHDQLLIGININSRGHQPWKKLLSDRSPYILVYANDSAISEPESVVSTLQRHKSRLLPNLHMLESHNRNASAQHRSRRSTNILLPLQNNELPGPEYPYEIPTWDEASPYDPMESKTVKRPRKKPRKNPRHKNPLLQFDEQTIKKARKKQWNEPRNCARRYLKVDFADIGWSEWIISPKSFDAYYCSGSCQFPMPKSLKPSNHATIQSIVRAVGVVPGIPEPCCVPEKMSSLSILFFDEDKNVVLKVYPNMTVDSCACR
Protein: Sensor histidine kinase MtrB (EC 2.7.13.3) (P9WGK9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Member of the two-component regulatory system MtrA/MtrB. Probably functions as a membrane-associated protein kinase that phosphorylates MtrA in response to environmental signals. Autophosphorylates and transfers phosphate to MtrA in vitro. Overexpression of MtrA alone decreases bacterial virulence in mouse infection; co-expression of MtrA and MtrB restores normal bacterial growth, suggesting that bacterial growth in macrophages requires an optimal ratio of MtrB to MtrA. Probably plays a role in cell division.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20233304, ECO:0000269|PubMed:22610443}; Multi-pass membrane protein {ECO:0000269|PubMed:20233304, ECO:0000269|PubMed:22610443}. Note=Found at the septa or mid-cell, independent of phosphorylation state.
Interaction partners:
- DNA-binding response regulator MtrA
- Lipoprotein LpqB
- Transcriptional regulatory protein PrrA
- Sensory transduction protein RegX3
- Response regulator MprA
- Possible two component system response transcriptional positive regulator PhoP
- Transcriptional regulatory protein TrcR
- Probable transcriptional regulatory protein TcrX
- Transcriptional regulatory protein TcrA
- Transcriptional regulatory protein KdpE
Sequence:
MIFGSRRRIRGRRGRSGPMTRGLSALSRAVAVAWRRSLQLRVVALTLGLSLAVILALGFVLTSQVTNRVLDIKVRAAIDQIERARTTVSGIVNGEETRSLDSSLQLARNTLTSKTDPASGAGLAGAFDAVLMVPGDGPRAASTAGPVDQVPNALRGFVKAGQAAYQYATVQTEGFSGPALIIGTPTLSRVANLELYLIFPLASEQATITLVRGTMATGGLVLLVLLAGIALLVSRQVVVPVRSASRIAERFAEGHLSERMPVRGEDDMARLAVSFNDMAESLSRQIAQLEEFGNLQRRFTSDVSHELRTPLTTVRMAADLIYDHSADLDPTLRRSTELMVSELDRFETLLNDLLEISRHDAGVAELSVEAVDLRTTVNNALGNVGHLAEEAGIELLVDLPAEQVIAEVDARRVERILRNLIANAIDHAEHKPVRIRMAADEDTVAVTVRDYGVGLRPGEEKLVFSRFWRSDPSRVRRSGGTGLGLAISVEDARLHQGRLEAWGEPGEGACFRLTLPMVRGHKVTTSPLPMKPIPQPVLQPVAQPNPQPMPPEYKERQRPREHAEWSG
Protein: Growth hormone receptor (GH receptor) (Somatotropin receptor) [Cleaved into: Growth hormone-binding protein (GH-binding protein) (GHBP) (Serum-binding protein)] (P19941)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to, and activates the JAK2/STAT5 pathway (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12403792}; 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:0000269|PubMed:11418602}.; SUBCELLULAR LOCATION: [Growth hormone-binding protein]: Secreted {ECO:0000269|PubMed:12403792}. Note=Complexed to a substantial fraction of circulating GH. {ECO:0000269|PubMed:12403792}.
Interaction partners:
- Tyrosine-protein kinase
- Somatotropin
- Prolactin
- Tyrosine-protein kinase
- Suppressor of cytokine signaling 2
- Insulin-like growth factor 1
- Signal transducer and activator of transcription
- Leptin
- Somatoliberin
- Erythropoietin
Sequence:
MDLWQLLLTVALAGSSDAFSGSEATPATLGRASESVQRVHPGLGTNSSGKPKFTKCRSPELETFSCHWTDGVHHGLKSPGSVQLFYIRRNTQEWTQEWKECPDYVSAGENSCYFNSSYTSIWIPYCIKLTNNGGMVDQKCFSVEEIVQPDPPIGLNWTLLNVSLTGIHADIQVRWEPPPNADVQKGWIVLEYELQYKEVNETQWKMMDPVLSTSVPVYSLRLDKEYEVRVRSRQRSSEKYGEFSEVLYVTLPQMSPFTCEEDFRFPWFLIIIFGIFGLTVMLFVFIFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKLEEVNTILAIQDSYKPEFYNDDSWVEFIELDIDDPDEKTEGSDTDRLLSNSHQKSLSVLAAKDDDSGRTSCYEPDILENDFNASDGCDGNSEVAQPQRLKGEADLLCLDQKNQNNSPYHDVSPAAQQPEVVLAEEDKPRPLLTGEIESTLQAAPSQLSNPNSLANIDFYAQVSDITPAGSVVLSPGQKNKAGNSQCDAHPEVVSLCQTNFIMDNAYFCEADAKKCIAVAPHVDVESRVEPSFNQEDIYITTESLTTTAERSGTAEDAPGSEMPVPDYTSIHLVQSPQGLVLNAATLPLPDKEFLSSCGYVSTDQLNKILP
Protein: Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) (Leukocyte common antigen) (L-CA) (T200) (CD antigen CD45) (P08575)
Organism: Homo sapiens (Human)
Function: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:22174689}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:12676959}. Synapse {ECO:0000269|PubMed:35767951}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000269|PubMed:12676959}.
Interaction partners:
- Tyrosine-protein kinase Lck
- B-cell receptor CD22
- Leukosialin
- Dipeptidyl peptidase 4
- Protein tyrosine phosphatase receptor type C-associated protein
- Tyrosine-protein kinase Fyn
- Galectin-3
- Tyrosine-protein kinase Lyn
- T-cell surface glycoprotein CD4
- Leukocyte surface antigen CD47
Sequence:
MTMYLWLKLLAFGFAFLDTEVFVTGQSPTPSPTGLTTAKMPSVPLSSDPLPTHTTAFSPASTFERENDFSETTTSLSPDNTSTQVSPDSLDNASAFNTTGVSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDPVSPLTTTLSLAHHSSAALPARTSNTTITANTSDAYLNASETTTLSPSGSAVISTTTIATTPSKPTCDEKYANITVDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTLILDVPPGVEKFQLHDCTQVEKADTTICLKWKNIETFTCDTQNITYRFQCGNMIFDNKEIKLENLEPEHEYKCDSEILYNNHKFTNASKIIKTDFGSPGEPQIIFCRSEAAHQGVITWNPPQRSFHNFTLCYIKETEKDCLNLDKNLIKYDLQNLKPYTKYVLSLHAYIIAKVQRNGSAAMCHFTTKSAPPSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGNTLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGDYPGEPFILHHSTSYNSKALIAFLAFLIIVTSIALLVVLYKIYDLHKKRSCNLDEQQELVERDDEKQLMNVEPIHADILLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEYNQFGETEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEMSKESEHDSDESSDDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTYPAQNGQVKKNNHQEDKIEFDNEVDKVKQDANCVNPLGAPEKLPEAKEQAEGSEPTSGTEGPEHSVNGPASPALNQGS
Protein: Fanconi anemia complementation group d2 (Fanconi anemia group D2 protein) (Q6WAS6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MMRKKKRSSVTVDEDPTLDVSKAKKSKSSGRSTKSSVQDSCQDSVFVQFLKESGVTLTPGSTANEIAVDQVIFQKRLQQRLRKSPRFPNIIQEFISALETYIEDPERFRNCLLPCVPAPTSQQDTNSSSYQESLVRLLLGIEMLQTLVINTLFEKLPEFMFEGASEDGLNVPRLIVNQLKWLDRIVDGKDLSSKLMQMVSVAPVEIQRDIITSLPEILEDSQHGDMAKELNGLLQQNTQLAVPILDALSSLNLSSTLLSEVREAVMGTLSAVQLEDLPVVVKFVLHSISASDANEVVCDLRKKLELEQCVLPAVLQASQSRMKNKTVSRSSSVPSCSSGQDSVALILDVIKSAIRFQKTISEAWLKAIENIDESEDHKVVDLLVLFILHSTNANHSRRGAERVLKVKVRKGLIQESLLQKTFKGHAQVMRGYFPSILALAQGLLRSPDCCVVPFGGHMYKQAFTAFDSYCQQEVVGSLVTHACSGVSGEVDVALELLCELVSQKPAEMSQFTVFVKGILDYMDNLTSQQIRRLFHLLSRLAFGQEQHGGHIQDDMHIVIRKQLSSTVPKYKRIGIIGAVMMVGSMGACRNKHDGSQGGTLPKETNRQVMALLELVRSCSESSPEAAALCYDELANLLQTCKLDPLVQAWIGKSVLEDFQDDFVVDLGPDISGAFMFPTSVLYNLDEEESEGGIAVNLLPLMALDQQHKTDTSQPAGVKRERRVSPLCLSPFFRLLRLCEEVQHEGDLEEIDALLGCPLILTDMEVVEKVDSLSKSEREFLCSLLFHTINWFREVVNAFCRQNDPEMKMKVVTRIQNITYLQSLLQTCLAATPGYIPPQANFDGESADVMIPSSSVVQQKKGKKESSGRKRKASASKNSSGDKSQLEGAADAEESQPDPPEKESEKEKEKDGKSGVSLSSYWPFFRELDVEALSVLQCGLLSRTLLDTELHSKLREEVQLGPAELLFLLEDMWRKLDFSLTSAPAKKAPFLKGKMDKAVGFAHLQQKNAKEIATCCSDLLPTLCTHLENCHNHFQTLLTENQGVVDAPNVDVKENQLMCSAYQLLLQVLHTMFSWSGFSIPEHRGLLKSALGILAGRLKEDQADLTLDQLSRHAFEYLQNFRSTVPSLNTALCLTQLLIVLPQYGGSNHRTYREQITSLTKHFLCQEWVTASGEKERGNKYNETLQTLLSIYLEHTDDVLKAVEEIAGEGVPELLNAAKDANSRSWPTLNRQTFLVYYKCMMSELEKAVRKIPPSKQMDNQEMQSEKLLTRNLAVRDFHILINLVKMFDSRPVLTVCLKYGRLFLESFLKLGMPLLDYSFKKHKEDVQGLLKTFQLSTRQLHHMCGHSKIRQDTGLTNHVPALKKSLEQFVYRVKAMLTLNHCQEAFWLGNLKNRDLKGEEILSQRSQAADEEEEESSQLQSEAEESDSDERNDGQEEVEESDESD