wanglab/gogpt-training-data huggingface dataset:
Protein: Klingon (P91670)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNIISRSIRTGALAPPTTAHASANASGLRKSSQRRNRAPLQMNCPILIVISLGWLLHAHAGSGGFAVEAAISNRGSNSRSIATCNSRRCRLHADRHPAPFPLQRTHLPRRRRGHAGLPCQVENLGNFVLLWRRGTNVLTASNIMVTRDERVRLIDGYNLEISDLEPQDAGDYVCQISDKINRDQVHTVEILVPPSVRAIPTSGQLQARKGGPITLECKGSGNPVPSIYWTKKSGANKSTARIGDGPILTLEKLERQQAGVYQCTADNGVGDPVTVDMRLDVLYPPDIQVEKSWIHSGEGFEAKLVCIVFADPVATVSWYQNSFPIQSTDRRIMATRANRHMLTIRHIQQEDFGNYSCVADNSLGRSRKYMELSGRPGAAEFYSPKWGRSPDSYNLTWKIDSYPPLEEVRLLYRRVQMNETYQQPGRWHDFILTPEHRPASEPLTHIMSYTIKNLHPGGYYEAIVQAKNRYGWNEVSDIFQFVVATNSQDIGPEDAEVVASSKSRSNSASIGSLPGSTVLHTALLLALA
Protein: Histone H2B type 1-K (Q8CGP1)
Organism: Mus musculus (Mouse)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H3.1
- Histone H3.2
- Histone H3.3
- Histone H4
- Plasminogen
- E3 ubiquitin-protein ligase BRE1A
- E3 ubiquitin-protein ligase BRE1B
- Histone H2AX
- Histone H2A type 1-B
- Histone H3-like centromeric protein A
Sequence:
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
Protein: MAL2A (Mal, T-cell differentiation protein 2) (Q7TPB7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSAGGAAVPPPPNPAVSFPAPRITLPAGPDILRTYSGAFVCLEIVLGGLVWILVASSNVPLPLLQGWVMFVSVTAFFFSLLFLGLFLSGMVTQIDANWNFLDFAYHFIVFVFYFGAFLLEAAATSLHDLQCNTTMVVKPLLNDNQYNINVAATVFAFMTTACYGCSLCLALRRWRP
Protein: H/ACA ribonucleoprotein complex subunit nhp2 (H/ACA snoRNP protein NHP2) (High mobility group-like nuclear protein 2) (P17-nhp2) (Q9P7H0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Non-catalytic component of the H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP), which catalyzes pseudouridylation of rRNA and is required for ribosome biogenesis. This involves the isomerization of uridine such that the ribose is subsequently attached to C5, instead of the normal N1 (By similarity). Pseudouridine ('psi') residues may serve to stabilize the conformation of rRNAs (By similarity). The H/ACA snoRNP complex also mediates pseudouridylation of other types of RNAs (By similarity). The H/ACA snoRNP complex mediates pseudouridylation at position 93 in U2 snRNA (By similarity). Directly binds H/ACA snoRNAs (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10502409}.
Interaction partners:
- H/ACA ribonucleoprotein complex subunit nop10
- H/ACA ribonucleoprotein complex subunit gar1
- H/ACA ribonucleoprotein complex subunit cbf5
- rRNA 2'-O-methyltransferase fibrillarin
- mRNA export factor elf1
- Nucleolar protein 56
- Nucleolar protein 58
- Elongation factor 3
- H/ACA ribonucleoprotein complex non-core subunit NAF1
- Ribosome production factor 2 homolog
Sequence:
MAKDKKDHKHSGSTEDEYDSYLPALMPIAKPLAPKKLNKKMMKTVKKASKQKHILRGVKEVVKAVRKGEKGLVILAGDISPMDVISHIPVLCEDNNVPYLYTVSKELLGEASNTKRPTSCVMIVPGGKKKDMSKVEEYKESYEEIIKEVPALEV
Protein: Coronin-2A (Q8C0P5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSWHPQYRSSKFRHVYGKPASKENCYDSVPITRSVHDNHFCAVNPHFIAVVTECAGGGAFLVIPLHQTGKLDPHYPKVCGHRGNVLDIKWNPFNDFEIASCSEDATIKIWNIPKQLLTRNLTTYRKELIGHARRVGLVEWHPTTANILFSAGYDYKVMVWNLDTKDSVIAGPVKTINCHQDVILSMSFNTNGSLLATTCKDRKIRIVDPRLGIVLQEASYKGHRANKVLFLGSLKKLLSTGTSRWNNRQMALWDQENLSVPLTEEDLDGSSGVLFPFFDSDTSMLYIVGKGDGNIRYYEVSMEKPHLTYLTEYRSYNPQKGIGIMPKRGLDVSSCEIFRFYKLITTKSLIEPVSMIVPRRSESYQEDIYPPTAAAQPSLTAHEWLSGMNRGPIMMSLRPGSELLDSQTLPPERPLSNSMVQVSPQPLEPMKQPAEDGDQAPFSLLEEKLAKWTAEHHLGEKSCLTNGFDVFECSPPKTENELLQMFYRQQEEIRRLRELLIQREVQTKQLELEIKNLRMALGQL
Protein: Glucose 1-dehydrogenase (GDH) (GlcDH) (EC 1.1.1.47) (Q703W7)
Organism: Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)
Function: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. To a lesser extent, is also active with xylose as substrate, but mannose, arabinose, galactose, fructose 6-phosphate, glucose 6-phosphate, glycerinaldehyde 3-phosphate, ribose, sorbitol, ethanol, erythritol, or lactose are not oxidized by the enzyme. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a marked preference for NADP(+). Is involved in the degradation of glucose through a non-phosphorylative variant of the Entner-Doudoroff pathway.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase
- NAD
- ATP-dependent hexokinase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase class 1
- Triosephosphate isomerase
- Enolase
- Pyruvate kinase
- pyruvate synthase
- pyruvate synthase
Sequence:
MRAVTVTPGVPESLRLREVPEPKPGPGQVLLKPLLVGVCGTDKEIIEGRYGKAPEGSDYLILGHEALAEVAALGKGVDNVSEGDLVVPTVRRPLDCQLPVDYCPPGKYLEHGIWGLHGHAAELSITDAAYLVKVPKELRDIAVLTEPLSVVEKGVELGVESYKARLGSPPKTALVLGAGPVGLLASMVLRLMGVSITAVATRPHDSLKARLVEELGGRYIDAVHERLEGEFDLVIEATGAPSLAVQGLERLAPGGVEVLLGVYPPTGELKGLGSLLTDAVLKNKLVVGSVNAGLRHFERALAHLKEANDSLNGFPKRLITKVVPLERYQEAYVWTHDDIKVVLQVQT
Protein: C-type lectin domain family 2 member D (Lectin-like NK cell receptor) (Lectin-like transcript 1) (LLT-1) (Osteoclast inhibitory lectin) (Q9UHP7)
Organism: Homo sapiens (Human)
Function: Receptor for KLRB1 that protects target cells against natural killer cell-mediated lysis. Inhibits osteoclast formation. Inhibits bone resorption. Modulates the release of interferon-gamma. Binds high molecular weight sulfated glycosaminoglycans.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15104121, ECO:0000269|PubMed:20843815, ECO:0000305|PubMed:16339513}; Single-pass type II membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000269|PubMed:20843815}.; SUBCELLULAR LOCATION: [Isoform 4]: Endoplasmic reticulum {ECO:0000269|PubMed:20843815}.
Interaction partners:
- Killer cell lectin-like receptor subfamily B member 1
- NKG2-A/NKG2-B type II integral membrane protein
Sequence:
MHDSNNVEKDITPSELPANPGCLHSKEHSIKATLIWRLFFLIMFLTIIVCGMVAALSAIRANCHQEPSVCLQAACPESWIGFQRKCFYFSDDTKNWTSSQRFCDSQDADLAQVESFQELNFLLRYKGPSDHWIGLSREQGQPWKWINGTEWTRQFPILGAGECAYLNDKGASSARHYTERKWICSKSDIHV
Protein: Glutathione S-transferase 3, mitochondrial (GST-3) (EC 2.5.1.-) (Glutathione peroxidase MGST3) (EC 1.11.1.-) (LTC4 synthase MGST3) (EC 4.4.1.20) (O14880)
Organism: Homo sapiens (Human)
Function: Catalyzes oxydation of hydroxy-fatty acids. Also catalyzes the conjugation of a reduced glutathione to leukotriene A4 in vitro. May participate in the lipid metabolism.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:27184847}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Microsomal glutathione S-transferase 1
- Cytochrome P450 2E1
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Epoxide hydrolase 1
- Glutathione reductase, mitochondrial
- Peroxiredoxin-6
- Cytochrome P450 1A1
- Thioredoxin domain-containing protein 12
- Cytochrome P450 3A4)
- Cytochrome P450 1B1
Sequence:
MAVLSKEYGFVLLTGAASFIMVAHLAINVSKARKKYKVEYPIMYSTDPENGHIFNCIQRAHQNTLEVYPPFLFFLAVGGVYHPRIASGLGLAWIVGRVLYAYGYYTGEPSKRSRGALGSIALLGLVGTTVCSAFQHLGWVKSGLGSGPKCCH
Protein: Protein disulfide isomerase-like 1-1 (AtPDIL1-1) (EC 5.3.4.1) (Protein disulfide-isomerase 1) (PDI 1) (Protein disulfide-isomerase 5) (AtPDI5) (Q9XI01)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein disulfide isomerase that associates with RD21A protease for trafficking from the ER through the Golgi to lytic and protein storage vacuoles of endothelial cells in developing seeds. Regulates the timing of programmed cell death (PCD) of the endothelial cells by chaperoning and inhibiting cysteine proteases during their trafficking to vacuoles.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:18676877}. Vacuole {ECO:0000269|PubMed:18676877}. Note=Found in protein storage vacuoles and lytic vacuoles in endothelial cells of developing seeds.
Interaction partners:
- Endoplasmic reticulum oxidoreductin-1
- Heat shock 70 kDa protein BIP1
- Cysteine proteinase RD21A
- Calreticulin-1
- Heat shock 70 kDa protein BIP2
- Endoplasmic reticulum oxidoreductin-2
- Calnexin homolog 1
- Calreticulin-2
- Heat shock 70 kDa protein BIP3
- Transcription factor MEE8
Sequence:
MAMRGFTLFSILVLSLCASSIRSEETETKEFVLTLDHTNFTDTINKHDFIVVEFYAPWCGHCKQLAPEYEKAASALSSNVPPVVLAKIDASEETNREFATQYEVQGFPTIKIFRNGGKAVQEYNGPREAEGIVTYLKKQSGPASAEIKSADDASEVVSDKKVVVVGIFPKLSGSEFDSFMAIAEKLRSELDFAHTSDAKLLPRGESSVTGPVVRLFKPFDEQFVDSKDFDGEALEKFVKESSIPLITVFDKDPNNHPYVIKFFESTNTKAMLFINFTGEGAESLKSKYREVATSNKGQGLSFLLGDAENSQGAFQYFGLEESQVPLIIIQTADDKKYLKTNVEVDQIESWVKDFKDGKIAPHKKSQPIPAENNEPVKVVVSDSLDDIVLNSGKNVLLEFYAPWCGHCQKLAPILDEVAVSYQSDSSVVIAKLDATANDFPKDTFDVKGFPTIYFKSASGNVVVYEGDRTKEDFISFVDKNKDTVGEPKKEEETTEEVKDEL
Protein: Protein transport protein sft1 (Q09730)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Vesicle SNARE required for retrograde transport within the Golgi complex.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- Protein transport protein gos1
- Integral membrane protein sed5
- Synaptobrevin homolog ykt6
- Protein transport protein bos1
- Protein transport protein sec22
- Syntaxin pep12
- Protein sly1
- Intracellular protein transport protein uso1
- Protein transport protein bet1
- Probable vesicular-fusion protein sec17 homolog
Sequence:
MNDQNERRLETLSGQVSSLKNVTYDIYSRANDYTRIDRATESFSGLSNSVKKSTENFFRVVRSAGRRRIMTMVLAIVGSILIIYYASKWFF
Protein: Anaphase-promoting complex subunit cut9 (20S cyclosome/APC complex protein cut9) (Cell untimely torn protein 9) (P41889)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the anaphase-promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes, it catalyzes the formation of protein-ubiquitin conjugates that are subsequently degraded by the 26S proteasome. May play a pivotal role in the control of anaphase.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Anaphase-promoting complex subunit 8
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 5
- Anaphase-promoting complex subunit 3
- Anaphase-promoting complex subunit 4
- Mitotic spindle checkpoint component mad3
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit hcn1
- Anaphase-promoting complex subunit 11
Sequence:
MVVKRTQTDSRMQSTPGNHNHPDAHANAAYMTPPSMGALNANNSNSQLSTLTISPMTYLANNTSTDGSFLKERNAQNTDSLSREDYLRLWRHDALMQQQYKCAAFVGEKVLDITGNPNDAFWLAQVYCCTGDYARAKCLLTKEDLYNRSSACRYLAAFCLVKLYDWQGALNLLGETNPFRKDEKNANKLLMQDGGIKLEASMCYLRGQVYTNLSNFDRAKECYKEALMVDAKCYEAFDQLVSNHLLTADEEWDLVLKLNYSTYSKEDAAFLRSLYMLKLNKTSHEDELRRAEDYLSSINGLEKSSDLLLCKADTLFVRSRFIDVLAITTKILEIDPYNLDVYPLHLASLHESGEKNKLYLISNDLVDRHPEKAVTWLAVGIYYLCVNKISEARRYFSKSSTMDPQFGPAWIGFAHSFAIEGEHDQAISAYTTAARLFQGTHLPYLFLGMQHMQLGNILLANEYLQSSYALFQYDPLLLNELGVVAFNKSDMQTAINHFQNALLLVKKTQSNEKPWAATWANLGHAYRKLKMYDAAIDALNQGLLLSTNDANVHTAIALVYLHKKIPGLAITHLHESLAISPNEIMASDLLKRALEENSLTSGFLNSKYVFEDEVSEYMQQSNLNTSDKSMSMEDQSGKVTESVNDRTQVLYADSRSEMMMDDIEGNVSEQR
Protein: Triggering receptor expressed on myeloid cells 1 (TREM-1) (Triggering receptor expressed on monocytes 1) (CD antigen CD354) (Q9NP99)
Organism: Homo sapiens (Human)
Function: Cell surface receptor that plays important roles in innate and adaptive immunity by amplifying inflammatory responses. Upon activation by various ligands such as PGLYRP1, HMGB1 or HSP70, multimerizes and forms a complex with transmembrane adapter TYROBP/DAP12. In turn, initiates a SYK-mediated cascade of tyrosine phosphorylation, activating multiple downstream mediators such as BTK, MAPK1, MAPK3 or phospholipase C-gamma. This cascade promotes the neutrophil- and macrophage-mediated release of pro-inflammatory cytokines and/or chemokines, as well as their migration and thereby amplifies inflammatory responses that are triggered by bacterial and fungal infections. By also promoting the amplification of inflammatory signals that are initially triggered by Toll-like receptor (TLR) and NOD-like receptor engagement, plays a major role in the pathophysiology of acute and chronic inflammatory diseases of different etiologies including septic shock and atherosclerosis.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:17098818, ECO:0000269|PubMed:21393102}; Single-pass type I membrane protein {ECO:0000305}. Note=Recruited to lipid rafts when activated. {ECO:0000269|PubMed:17098818}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:26561551}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Triggering receptor expressed on myeloid cells 2
- Trem-like transcript 1 protein
- High mobility group protein B1
- Trem-like transcript 2 protein
- Peptidoglycan recognition protein 1
- fMet-Leu-Phe receptor
- Aquaporin-9
- C-type lectin domain family 5 member A
- CMRF35-like molecule 7
Sequence:
MRKTRLWGLLWMLFVSELRAATKLTEEKYELKEGQTLDVKCDYTLEKFASSQKAWQIIRDGEMPKTLACTERPSKNSHPVQVGRIILEDYHDHGLLRVRMVNLQVEDSGLYQCVIYQPPKEPHMLFDRIRLVVTKGFSGTPGSNENSTQNVYKIPPTTTKALCPLYTSPRTVTQAPPKSTADVSTPDSEINLTNVTDIIRVPVFNIVILLAGGFLSKSLVFSVLFAVTLRSFVP
Protein: Small nuclear ribonucleoprotein U5 subunit 40 (Uncharacterized protein DKFZp434D199) (WD repeat domain 57 (U5 snRNP specific), isoform CRA_b) (Q9NSS8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MILISAGCPGGLWPIVVLVGLFIWICFAVRVWDVRPFAPKERCVKIFQGNVHNFEKNLLRCSWSPDGSKIAAGSADRFVYVWDTTSRRILYKLPGHAGSINEVAFHPDEPIIISASSDKRLYMGEIQ
Protein: Protein AIR2 (Arginine methyltransferase-interacting RING finger protein 2) (Q12476)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the TRAMP (TRF4) complex which has a poly(A) RNA polymerase activity and is involved in a post-transcriptional quality control mechanism limiting inappropriate expression of genetic information. Polyadenylation is required for the degradative activity of the exosome on several of its nuclear RNA substrates like cryptic transcripts generated by RNA polymerase II and III, or hypomethylated pre-tRNAi-Met. Both complexes polyadenylate RNA processing and degradation intermediates of snRNAs, snoRNAs and mRNAs that accumulate in strains lacking a functional exosome. AIR2 also inhibits the methylation of NPL3 mediated by HMT1 through its interaction with HMT1.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- ATP-dependent RNA helicase DOB1
- Poly
- Poly
- Poly
- Protein AIR1
- Nuclear polyadenylated RNA-binding protein 3
- Exosome complex exonuclease RRP6
- Exosome complex exonuclease DIS3
- Probable E3 ubiquitin-protein ligase HUL4
- Protein NRD1
Sequence:
MEKNTAPFVVDTAPTTPPDKLVAPSIEEVNSNPNELRALRGQGRYFGVSDDDKDAIKEAAPKCNNCSQRGHLKKDCPHIICSYCGATDDHYSRHCPKAIQCSKCDEVGHYRSQCPHKWKKVQCTLCKSKKHSKERCPSIWRAYILVDDNEKAKPKVLPFHTIYCYNCGGKGHFGDDCKEKRSSRVPNEDGSAFTGSNLSVELKQEYYRHMNRNSDENEDYQFSESIYDEDPLPRPSHKRHSQNDHSHSGRNKRRASNFHPPPYQKSNVIQPTIRGETLSLNNNISKNSRYQNTKVNVSSISENMYGSRYNPSTYVDNNSISNSSNYRNYNSYQPYRSGTLGKRR
Protein: Pelle-like serine/threonine-protein kinase pik-1 (EC 2.7.11.1) (G5ECP4)
Organism: Caenorhabditis elegans
Function: Through association with the adapter actl-1, may act downstream of the receptor complex composed of ilcr-1 and ilcr-2, which is a signaling complex that modulates neuronal activity and animal behavior in response to sensory neuron input.
Interaction partners:
- Protein pellino
- Death domain-containing protein
- TIR domain-containing protein
- TNF Receptor Associated Factor
- ACT1-like protein
- CUE domain-containing protein
- Rho-GAP domain-containing protein
- Interleukin cytokine receptor-related protein 1
- Interleukin cytokine receptor-related protein 2
- Interleukin cytokine-related protein 17.1
Sequence:
MDDSLGVSEVVMIPFMKREVLQQICAILDTDNTWETIAPYMPGIELRDVEGCKRYSSYNQSPSELLLRIWSSKGYSTTHLYQLFAKTKLIRLMRMMRSQVHEKYHYLENKVTNSTSRVSKQMVQPPGSQSASRLKKTEIKESSPSPAAAAASQLSRSNTDDTLRVAIEGTLPVTYCELLEATNGFAVSNVIGKGGYGTVYKGELKGTGGIVAVKRLHSGNDTSQNGSRERLRQSLTELRTLARFRHDNILPIYAYSLEGSEPCLVYQFMSNGSLEDRLLCRKGSVPLTWIQRKEISIGAGRGLGFLHSFGKTPIIHGDIKTANILLDKHMEPKIGDFGLCRDGHVEAEAMEKHPLIASHIKGTLAYLAPEFITSKILTTKLDVYSFGIVLLEIASGQRAYSDSRETRGLVEYCQVNKELAAHRKIPVREIFIDRRAPPLVGDEEKSFLDALIEVGLAGANNDRKVRPTMSQIVEYLCKNSIPPVV
Protein: Rab effector MyRIP (Exophilin-8) (Myosin-VIIa- and Rab-interacting protein) (Synaptotagmin-like protein lacking C2 domains C) (SlaC2-c) (Slp homolog lacking C2 domains c) (Q8K3I4)
Organism: Mus musculus (Mouse)
Function: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments. Functions as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12221080}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}. Melanosome {ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:12221080}. Note=In presynaptic and postsynaptic areas in photoreceptor cells and in the basal microvilli of retinal pigment epithelium cells. Associated with melanosomes. Colocalizes with actin filaments. In insulin-secreting cells, associated with dense core secretory granules. {ECO:0000269|PubMed:11964381, ECO:0000269|PubMed:12221080}.
Interaction partners:
- Ras-related protein Rab-27A
- Unconventional myosin-Va
- Unconventional myosin-VIIa
- Exocyst complex component 3-like protein
- Exocyst complex component 3
- Exocyst complex component 4
- Ras-related protein Rab-27B
- SH3 domain-binding protein 1
- Exocyst complex component 8
- Exocyst complex component 2
Sequence:
MGRKLDLSGLTDDETEHVLQVVQRDFNLRKKEEDRLSEMKQRLAEENSKCSILSKHQKFVERCCMRCCSPFTFLVNARRRCGECKFSVCKSCCSYQKHEKLWVCCVCQQARLLRTQSLEWFYNNVKSRFKRFGSAKVLKNLYRKHRLESGACFDILGGGLFEPNLENEGSISGSDSTFYRQSEGHSMMDTLAVALRVAEEAIEEAISKAESHGDSLDKQNEASYLRDHKQELTEELAGTILQRIIRKQKDKAELRAEEEEPEWPRSQSGSVKARGEGTTAPPGRHKARATFRRSQSAFSFTMEDALKSGSAEAAPRSPKDRAQRLLEEAALPSWRSMDGLDGTNLAPLLQSPDGNWMTLKDGSRQPPTRLLTKPKSGTFQALEVASSVTSAYDEIGSDSEEDFDYSEALSKLCPPSQSRLKQPQPQPTQAQSSGQGPLATSPSNPEAMCSDSETSSTSSSREAGCRAKLSWLQRKAPKNPAVEKMPLQGELDVNFNPQAAGGETSDSSDPEETLRTAERRARRWRRARVGPEESNRGLPSPGAHPRALHTAQVSDNVSETDISNETQNSRSSTDSVEEKLRNRLYELAMKMSEKETSSGEDQESESKAEPKNQKGSLSSEENNQGVQEELKKKCSAVSLCNISTEVLKVINATEELIAESAGPWEIPPVSTDRENGMFPLGTDQVRLDKQLTSLEENVYLAAGTVYGLEGQLSELEDAARCIHSSTGETELADLEDQVAAAAAQVHHAELQISDIESRISALTIAGLNIAPCVRLTRRRDQKQRSQVQTIDTSRQQRRKLPAPPVKAEKIEASSVTPIKTFNRNFLLQGSSTNRPTASTGDTKDLMEPDLESAVMY
Protein: Protein ROH1D (Q9CA69)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:26485022}. Note=Present in the cytosol of cells of the root apical meristem and transition zone. {ECO:0000269|PubMed:26485022}.
Interaction partners:
- AT5g12010/F14F18_180
- Nuclease
- At4g27652
- Protein BPS1, chloroplastic
- Exocyst complex component EXO70A1
- Exocyst complex component EXO70C2
- U-box domain-containing protein 10
Sequence:
MPATEYQRSFGRSFLNLRRDTAVNSVESTTVTPELTQMEAELVSFQRKVAERFIDLNASSCEDLLSLEWVGKLLDSFLSCQEEFRSIVINHRSMITKPPMDRLVSDYFERSVKALDVCNAIRDGVEQIRQWQKLIEIVICAFNNNGGGSSGKRPLGEGQFRRARKTLIELAIGMLDEKDSSSSSVSSQHRNRSFGRNKEQLHHRTIGHFRSLSWSVSRSWSASKQLQAIGNNLATPRASDITATNGLIVPVYTMTTVLLFVMWALVAAIPCQDRGLQVHFNVPRNYQWGGSLMSLHDRIIEESKKRERKNTCGLLKEIHQFEKTSRLMNELVDSVQFPLSEEKEMEVRERVEELGKLQEALKNGLDPFERKVREVFHRIVRSRTEGLDTVGKHHGSE
Protein: C-type lectin domain family 12 member A (C-type lectin-like molecule 1) (CLL-1) (Dendritic cell-associated lectin 2) (DCAL-2) (Killer cell C-type lectin-like receptor L1) (hKLRL1) (Myeloid inhibitory C-type lectin-like receptor) (MICL) (CD antigen CD371) (Q5QGZ9)
Organism: Homo sapiens (Human)
Function: Cell surface receptor that modulates signaling cascades and mediates tyrosine phosphorylation of target MAP kinases.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:15238421, ECO:0000269|PubMed:15548716, ECO:0000269|PubMed:16239426, ECO:0000269|PubMed:16838277, ECO:0000269|PubMed:34234773, ECO:0000269|PubMed:38367667}; Single-pass type II membrane protein {ECO:0000255}. Note=Ligand binding leads to internalization (PubMed:16239426). Clusters at phagocytic vesicles upon monosodium urate crystal-binding (PubMed:38367667). {ECO:0000269|PubMed:16239426, ECO:0000269|PubMed:38367667}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 11
- Collectin-11
- Myeloid cell surface antigen CD33
- Syntaxin-18
- C-type lectin domain family 12 member B
- Interleukin-3 receptor subunit alpha
- Nuclear receptor subfamily 0 group B member 2
- Syntaxin-6
- Hepatitis A virus cellular receptor 2
- Vesicle transport through interaction with t-SNAREs homolog 1A
Sequence:
MSEEVTYADLQFQNSSEMEKIPEIGKFGEKAPPAPSHVWRPAALFLTLLCLLLLIGLGVLASMFHVTLKIEMKKMNKLQNISEELQRNISLQLMSNMNISNKIRNLSTTLQTIATKLCRELYSKEQEHKCKPCPRRWIWHKDSCYFLSDDVQTWQESKMACAAQNASLLKINNKNALEFIKSQSRSYDYWLGLSPEEDSTRGMRVDNIINSSAWVIRNAPDLNNMYCGYINRLYVQYYHCTYKKRMICEKMANPVQLGSTYFREA
Protein: SWR1-complex protein 7 (Q06707)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- SWR1-complex protein 4
- SWR1-complex protein 5
- Protein AF-9 homolog
- Vacuolar protein sorting-associated protein 72
- Vacuolar protein sorting-associated protein 71
- Bromodomain-containing factor 1
- Helicase SWR1
- RuvB-like protein 1
- RuvB-like protein 2
- SWR1-complex protein 3
Sequence:
MDCPSNVVLLLLQLVLQRQQTLAHRDKSVDLQTLLKDPVIDNDVLVEFKTHKLVQLYGPQYCRDISLRGLKTMVTDIFANGIPKNAQSSGNDQPVTVVDLANYYYMQRINELQNTELPQLKEALLTRLEHMI
Protein: Muscarinic acetylcholine receptor M1 (P08482)
Organism: Rattus norvegicus (Rat)
Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
Subcellular location: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein.
Interaction partners:
- Metabotropic glutamate receptor 5
- Guanine nucleotide-binding protein G
- Muscarinic acetylcholine receptor M5
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit gamma
- Muscarinic acetylcholine receptor M3
- Lysophosphatidic acid receptor 6
- Lysophosphatidic acid receptor 4
- Muscarinic acetylcholine receptor M2
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MNTSVPPAVSPNITVLAPGKGPWQVAFIGITTGLLSLATVTGNLLVLISFKVNTELKTVNNYFLLSLACADLIIGTFSMNLYTTYLLMGHWALGTLACDLWLALDYVASNASVMNLLLISFDRYFSVTRPLSYRAKRTPRRAALMIGLAWLVSFVLWAPAILFWQYLVGERTVLAGQCYIQFLSQPIITFGTAMAAFYLPVTVMCTLYWRIYRETENRARELAALQGSETPGKGGGSSSSSERSQPGAEGSPESPPGRCCRCCRAPRLLQAYSWKEEEEEDEGSMESLTSSEGEEPGSEVVIKMPMVDSEAQAPTKQPPKSSPNTVKRPTKKGRDRGGKGQKPRGKEQLAKRKTFSLVKEKKAARTLSAILLAFILTWTPYNIMVLVSTFCKDCVPETLWELGYWLCYVNSTVNPMCYALCNKAFRDTFRLLLLCRWDKRRWRKIPKRPGSVHRTPSRQC