wanglab/gogpt-training-data huggingface dataset:
Protein: Protein HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 244, chloroplastic (O65502)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Auxiliary factor required, together with HCF173, for the biogenesis of photosystem II (PSII), especially for the synthesis of the reaction center proteins (e.g. D1), via the regulation of the corresponding mRNA (e.g. psbA) translation initiation (ribosomal loading) and stabilization. Forms a trimeric complex with OHP1 and OHP2 that is required to promote PSII core subunit assembly. The trimeric complex forms a transient PSII reaction center-like complex with PsbA, PsbD, PsbE, PsbF and PsbI subunits in thylakoids for early assembly of PSII as well as PSII repair. The trimeric complex is required for the recruitment of ribosomes to the psbA mRNA during PSII biogenesis and repair.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:23027666}. Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:23027666}; Peripheral membrane protein {ECO:0000269|PubMed:23027666}; Stromal side {ECO:0000269|PubMed:23027666}. Note=Predominantly present at thylakoid membranes. {ECO:0000269|PubMed:23027666}.
Interaction partners:
- Light-harvesting complex-like protein OHP1, chloroplastic
- Light-harvesting complex-like protein OHP2, chloroplastic
- Protein HIGH CHLOROPHYLL FLUORESCENCE PHENOTYPE 173
- Photosystem II stability/assembly factor HCF136
- Protein PAM68, chloroplastic
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
Sequence:
MASLRLPAQLVTRGNLIHHNSSSSSSGRLSWRRSLTPENTIPLFPSSSSSSLNRERSIVVPVTCSAAAVNLAPGTPVRPTSILVVGATGTLGRQIVRRALDEGYDVRCLVRPRPAPADFLRDWGATVVNADLSKPETIPATLVGIHTVIDCATGRPEEPIKTVDWEGKVALIQCAKAMGIQKYVFYSIHNCDKHPEVPLMEIKYCTEKFLQESGLNHITIRLCGFMQGLIGQYAVPILEEKSVWGTDAPTRVAYMDTQDIARLTLIALRNEKINGKLLTFAGPRAWTTQEVITLCERLAGQDANVTTVPVSVLRVTRQLTRFFQWTNDVADRLAFSEVLSSDTVFSAPMTETNSLLGVDQKDMVTLEKYLQDYFSNILKKLKDLKAQSKQSDIYF
Protein: Apurinic-apyrimidinic endonuclease (AP endonuclease) (EC 3.1.21.-) (Q10002)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- exodeoxyribonuclease III
- Endonuclease III homolog
- Uracil-DNA glycosylase
- Flap endonuclease 1
- dUTP diphosphatase
- DNA ligase 1
- Probable tyrosyl-DNA phosphodiesterase
- ERCC1-like central domain-containing protein
- XPA C-terminal domain-containing protein
- Apoptotic enhancer 1 protein
Sequence:
MANKKVTFREDVKSPAIRKLKQKLTPLKIKKGRGKIQKHIQKTLQKMKEEEESENQSPGTTVEETLTEENISTDKEETSKLENKPKKTRKTSGETIAQKKSRETVGVEVLKTSEGSSKMLGFHVSAAGGLEQAIYNARAEGCRSFAMFVRNQRTWNHKPMSEEVVENWWKAVRETNFPLDQIVPHGSYLMNAGSPEAEKLEKSRLAMLDECQRAEKLGITMYNFHPGSTVGKCEKEECMTTIAETIDFVVEKTENIILVLETMAGQGNSIGGTFEELKFIIDKVKVKSRVGVCIDTCHIFAGGYDIRTQKAYEEVMKNFGEVVGWNYLKAIHINDSKGDVGSKLDRHEHIGQGKIGKAAFELLMNDNRLDGIPMILETPEGKYPEEMMIMYNMDKR
Protein: Mitochondrial guide RNA binding complex subunit 2 (B6SBL9)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MLRARLKIFSALNGATSAFSRAVAPLQIATRQQSFSAAAPAASGDFSHITRNTVWGLWNEGNLFSLSVPELAFFLQEHCRVANVDPRAKKSALVRQVEEILSAEQQASATVPQEDNPHAIVVTDYDRAEDALEEADEYGDWGAEPGFEDRRELDFMELSPGRMGERYDPLSPRAFQLLHSETATDVGIASIDPSKLPGQSKVKNALAAIHVAPNDANKMRFRMAFEWCLMNIWNMNMPGELNIGAGKALYYRSVAKQNRNVMPLWTVQKHLYAQHPYAWFAIASESNVAAMESLAAALNMSIQQERTTSYKVTIRRMAEFFDCELNGQLKCTMMNKPWDRFFVSHYIRSKMPDLRYVVRARHPIKKRIADAYLEADILRSTRDSVQSVLSPELGDVVYCCERVVRKWAKKTATGVTLQLVETKRTPLIITKAGDEGERLEYEWIVPLPQQAERIDIAALTDELWEYGNKLAAALEEGMEELMVHTMTAVSAY
Protein: Regulatory protein E2 (P04015)
Organism: Human papillomavirus 11
Function: Plays a role in the initiation of viral DNA replication. A dimer of E2 interacts with a dimer of E1 in order to improve specificity of E1 DNA binding activity. Once the complex recognizes and binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also regulates viral transcription through binding to the E2RE response element (5'-ACCNNNNNNGGT-3') present in multiple copies in the regulatory regions of the viral genome. Activates or represses transcription depending on E2RE's position with regards to proximal promoter elements including the TATA-box. Repression occurs by sterically hindering the assembly of the transcription initiation complex.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001}.
Interaction partners:
Sequence:
MEAIAKRLDACQDQLLELYEENSIDIHKHIMHWKCIRLESVLLHKAKQMGLSHIGLQVVPPLTVSETKGHNAIEMQMHLESLAKTQYGVEPWTLQDTSYEMWLTPPKRCFKKQGNTVEVKFDGCEDNVMEYVVWTHIYLQDNDSWVKVTSSVDAKGIYYTCGQFKTYYVNFNKEAQKYGSTNHWEVCYGSTVICSPASVSSTVREVSIAEPTTYTPAQTTAPTVSACTTEDGVSAPPRKRARGPSTNNTLCVANIRSVDSTINNIVTDNYNKHQRRNNCHSAATPIVQLQGDSNCLKCFRYRLNDKYKHLFELASSTWHWASPEAPHKNAIVTLTYSSEEQRQQFLNSVKIPPTIRHKVGFMSLHLL
Protein: RNA-binding protein 20 (RNA-binding motif protein 20) (Q3UQS8)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that acts as a regulator of mRNA splicing of a subset of genes encoding key structural proteins involved in cardiac development, such as TTN (Titin), CACNA1C, CAMK2D or PDLIM5/ENH. Acts as a repressor of mRNA splicing: specifically binds the 5'UCUU-3' motif that is predominantly found within intronic sequences of pre-mRNAs, leading to the exclusion of specific exons in target transcripts. RBM20-mediated exon skipping is hormone-dependent and is essential for TTN isoform transition in both cardiac and skeletal muscles. RBM20-mediated exon skipping of TTN provides substrates for the formation of circular RNA (circRNAs) from the TTN transcripts (By similarity). Together with RBM24, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:22466703, ECO:0000269|PubMed:23886709, ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:33110103, ECO:0000269|PubMed:35041844, ECO:0000269|PubMed:35394688}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:35041844, ECO:0000269|PubMed:35394688}. Note=The active form that regulates alternative splicing localizes to the nucleus (PubMed:35394688). Also localizes to cytoplasmic ribonucleoprotein granules; localization to cytoplasmic ribonucleoprotein granules plays an important regulatory role (PubMed:35394688). Subcellular localization is regulated by phosphorylation of different parts of the protein: while phosphorylation of the RS (arginine/serine-rich) region promotes nuclear localization, phosphorylation of the C-terminal disordered region promotes localization to cytoplasmic ribonucleoprotein granules (PubMed:29895960, PubMed:35394688). {ECO:0000269|PubMed:29895960, ECO:0000269|PubMed:35394688}.
Interaction partners:
- Titin
- RNA-binding protein 24
Sequence:
MVLAVAMSQDADPSGPEQPDRDACVMPGVQGPSVPQGQQGMQPLPPPPPPQPQASLPQIIQNAAKLLDKSPFSVNNQNPLLTSPASVQLAQIQAQLTLHRLKMAQTAVTNNTAAATVLNQVLSKVAMSQPLFNQLRHPSVLGTAHGPTGVSQHAASVPSAHFPSTAIAFSPPSQTGGPGPSVSLPSQPPNAMVVHTFSGVVPQTPAQPAVILSLGKAGPTPATTGFYDYGKANSGQAYGSETEGQPGFLPASASATASGSMTYEGHYSHTGQDGQPAFSKDFYGPNAQGPHIAGGFPADQTGSMKGDVGGLLQGTNSQWERPPGFSGQNKPDITAGPSLWAPPASQPYELYDPEEPTSDRAPPAFGSRLNNSKQGFGCSCRRTKEGQAVLSVRPLQGHQLNDFRGLAPLHLPHICSICDKKVFDLKDWELHVKGKLHAQKCLLFSESAGLRSIRASGEGTLSASANSTAVYNPTGNEDYTSNLGTSYAAIPTRAFAQSNPVFPSASSGTSFAAQRKGAGRVVHICNLPEGSCTENDVINLGLPFGKVTNYILMKSTNQAFLEMAYTEAAQAMVQYYQEKPAIINGEKLLIRMSTRYKELQLKKPGKNVAAIIQDIHSQRERDMLREADRYGPERPRSRSPMSRSLSPRSHSPPGPSRADWGNGRDSYAWRDEDRETVPRRENGEDKRDRLDVWAHDRKHYPRQLDKAELDERLEGGRGYREKYLKSGSPGPLHSVSGYKGREDGYHRKEPKAKLDKYPKQQPDVPGRSRRKEEARLREPRHPHPEDSGKAEDLEPKITRAPDGTKSKQSEKSKTKRADRDQEGADDKKESQLAENEAGAEEQEGMVGIQQEGTESCDPENTRTKKGQDCDSGSEPEGDNWYPTNMEELVTVDEVGEEDFIMEPDLPELEEIVPIDQKDKTLPKICTCVTATLGLDLAKDFTKQGETLGNGDAELSLKLPGQVPSTSASCPNDTDLEMPGLNLDAERKPAESETGLSLEVSNCYEKEARGEEDSDVSLAPAVQQMSSPQPADERARQSSPFLDDCKARGSPEDGSHEASPLEGKASPPTESDLQSQACRENPRYMEVKSLNVRSPEFTEAELKEPLSLPSWEPEVFSELSIPLGVEFVVPRTGFYCKLCGLFYTSEEAAKVSHCRSTVHYRNLQKYLSQLAEEGLKETEGTDSPSPERGGIGPHLERKKL
Protein: Uncharacterized protein C17D1.05 (Q10203)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MSFVDGVNSWFSAASYWDGLGPTNVVQPEDDLAFVSQFEEVESAYDNLVKNGMIAPRRKNSFASSVNNPFSTSALSEALNGSVSMSHVPSSGLLKSTLSSTPTAGSNLLGTSPAEPASGLVGSSGFGSSMLGSSLPGNATSNFGSQASTSLLHPRRSTTSLLSSSAHHSRSSYYDLATPTRSSFSYNTVGAASLPSGGLSNLSSSLRSSSKSAGFSLFESASNSFTPSSFIESANMESLSIPSRRRPSSIAPIGTRPSRKEIAFSNSSTPTDQTLRPPNPPAANGNATPVTAVNNVSAVADSPQSTGSSVSSSLPTLSLDFKQEYSGNNHDMSGLSSSLSKSHNSTSALSSQIWSSPCASTLGGVNVW
Protein: Sm-like protein LSM1A (AtLSM1a) (Q945P8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. LSM1A and LSM1B are essential for the formation of the cytoplasmic LSM1-LSM7 complex which regulates developmental gene expression by the decapping of specific development-related transcripts. Required for P-body formation during heat stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23221597, ECO:0000269|PubMed:23620288}. Cytoplasm, P-body {ECO:0000269|PubMed:23221597}. Note=Translocates from cytosol to P-bodies upon heat stress. {ECO:0000269|PubMed:23221597}.
Interaction partners:
- Sm-like protein LSM2
- Sm-like protein LSM3A
- Sm-like protein LSM3B
- Sm-like protein LSM5
- Sm-like protein LSM4
- Sm-like protein LSM7
- Sm-like protein LSM6A
- Sm-like protein LSM36B
- mRNA-decapping enzyme subunit 2
- mRNA-decapping enzyme-like protein
Sequence:
MSWAAPDDIFFSTSLAAYLDKKLLVLLRDGRKLMGLLRSFDQFANAVLEEAYERVIVGDLYCDIPLGLYIIRGENVVLIGELDVEKEELPAHMVQVPEAEIKRAQKAEKEEMLLKGTMRKRMEFLDLD
Protein: Cell cycle serine/threonine-protein kinase CDC5/MSD2 (EC 2.7.11.21) (P32562)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein kinase required for the cell cycle where it is involved in mitotic exit. A component of the fear (CDC14 early anaphase release) network which promotes CDC14 release from the nucleolus during early anaphase. Phosphorylates SCC1/MCD1 and NET1.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:32553169}. Note=Recruited to the spindle pole bodies by CSA1 during metaphase. {ECO:0000269|PubMed:32553169}.
Interaction partners:
- Sporulation-specific protein 12
- Tyrosine-protein phosphatase CDC14
- Kinetochore protein SLK19
- G2/mitotic-specific cyclin-1
- Mitotic check point protein BUB2
- Separin
- Sister chromatid cohesion protein 1
- Protein TEM1
- Mitotic check point protein BFA1
- Protein SIC1
Sequence:
MSLGPLKAINDKQLNTRSKLVHTPIKGNTADLVGKENHFKQTKRLDPNNDHHHQPAQKKKREKLSALCKTPPSLIKTRGKDYHRGHFLGEGGFARCFQIKDDSGEIFAAKTVAKASIKSEKTRKKLLSEIQIHKSMSHPNIVQFIDCFEDDSNVYILLEICPNGSLMELLKRRKVLTEPEVRFFTTQICGAIKYMHSRRVIHRDLKLGNIFFDSNYNLKIGDFGLAAVLANESERKYTICGTPNYIAPEVLMGKHSGHSFEVDIWSLGVMLYALLIGKPPFQARDVNTIYERIKCRDFSFPRDKPISDEGKILIRDILSLDPIERPSLTEIMDYVWFRGTFPPSIPSTVMSEAPNFEDIPEEQSLVNFKDCMEKSLLLESMSSDKIQRQKRDYISSIKSSIDKLEEYHQNRPFLPHSLSPGGTKQKYKEVVDIEAQRRLNDLAREARIRRAQQAVLRKELIATSTNVIKSEISLRILASECHLTLNGIVEAEAQYKMGGLPKSRLPKIKHPMIVTKWVDYSNKHGFSYQLSTEDIGVLFNNGTTVLRLADAEEFWYISYDDREGWVASHYLLSEKPRELSRHLEVVDFFAKYMKANLSRVSTFGREEYHKDDVFLRRYTRYKPFVMFELSDGTFQFNFKDHHKMAISDGGKLVTYISPSHESTTYPLVEVLKYGEIPGYPESNFREKLTLIKEGLKQKSTIVTVD
Protein: HAT transposon superfamily (F4HQA2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Retrotransposon ORF-1 protein
- Retrotransposon ORF-1 protein
- Retrotransposon ORF-1 protein
- Zinc finger BED domain-containing protein DAYSLEEPER
- TOM1-like protein 2
- TOM1-like protein 1
Sequence:
MVREKDICWEYAEKLDGNKVKCKFCSRVLNGGISRLKHHLSRLPSKGVNPCAKVRDDVTDRVRSILSAKDDPPITNKYKPPPPLSPPFDAPASKLVFPSSPPNAQDIAERSISLFFFENKIDFAVARSPSYHHMLDAVAKCGPGFVAPSPKTEWLDRVKSDISLQLKDTEKEWVTTGCTIIAEAWTDNKSRALINFSVSSPSRIFFHKSVDASSYFKNSKCLADLFDSVIQDIGQEHIVQIIMDNSFCYTGISNHLLQNYATIFVSPCASQCLNIILEEFSKVDWVNQCISQAQVISKFVYNNSPVLDLLRKLTGGQDIIRSGVTRSVSNFLSLQSMMKQKARLKHMFNCPEYTTNTNKPQSISCVNILEDNDFWRAVEESVAISEPILKVLREVSTGKPAVGSIYELMSKAKESIRTYYIMDENKHKVFSDIVDTNWCEHLHSPLHAAAAFLNPSIQYNPEIKFLTSLKEDFFKVLEKLLPTSDLRRDITNQIFTFTRAKGMFGCNLAMEARDSVSPGLWWEQFGDSAPVLQRVAIRILSQVCSGYNLERQWSTFQQMHWERRNKIDREILNKLAYVNQNLKLGRMITLETDPIALEDIDMMSEWVEEAENPSPAQWLDRFGTALDGGDLNTRQFGGAIFSANDHNIFGL
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase (1-AGP acyltransferase) (1-AGPAT) (EC 2.3.1.23) (EC 2.3.1.51) (EC 2.3.1.n7) (Lysophosphatidic acid acyltransferase) (LPAAT) (Sphingolipid compensation protein 1) (P33333)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acyltransferase that catalyzes the sn-2-specific, acyl-CoA-dependent acylation of lysophosphatidic acid (LPA) to phosphatidic acid (PA) in lipid particles. Together with ALE1, plays a central role in PA biosynthesis. PA is the intermediate, from which all glycerophospholipids are synthesized. Can also acylate lysophosphoinositol (LPI) and lysophosphoserine (LPS). The fatty acyl substrates include 18:1-acyl-CoA, 14:0-acyl-CoA, 12:0-acyl-CoA and 10:0-acyl-CoA.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:18154737, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093}.
Interaction partners:
- Lysophospholipid acyltransferase
- Glycerol-3-phosphate O-acyltransferase 1
- Phosphatidate cytidylyltransferase
- Glycerol-3-phosphate O-acyltransferase 2
- Lipid phosphate phosphatase 1
- Diacylglycerol pyrophosphate phosphatase 1
- CTP-dependent diacylglycerol kinase 1
- Phosphatidic acid phosphohydrolase 1
- NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- Phospholipase D1
Sequence:
MSVIGRFLYYLRSVLVVLALAGCGFYGVIASILCTLIGKQHLAQWITARCFYHVMKLMLGLDVKVVGEENLAKKPYIMIANHQSTLDIFMLGRIFPPGCTVTAKKSLKYVPFLGWFMALSGTYFLDRSKRQEAIDTLNKGLENVKKNKRALWVFPEGTRSYTSELTMLPFKKGAFHLAQQGKIPIVPVVVSNTSTLVSPKYGVFNRGCMIVRILKPISTENLTKDKIGEFAEKVRDQMVDTLKEIGYSPAINDTTLPPQAIEYAALQHDKKVNKKIKNEPVPSVSISNDVNTHNEGSSVKKMH
Protein: Vomeronasal type-1 receptor (A6H6D3)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}.
Interaction partners:
Sequence:
MRLPLPLEHKKMLLYQLWCSDPCLALLMLSLKCIFILHTRKKEMIWKLIKKILFLFMTMLGILGNMFVSVNFMLSWWGSPEKKSVHLILIHLAFTNIIILLTKGLQKTIVAFGLRNFLNNLGCKIIVYMERVAHGLSLCTSSLLTVVQAIIISPRASGWRRLRPKSVWHILPFFLFFWILNALISMNLINSITSTRLNISQLKSDDNYCYFMLPSQKIKWIVLPLMVLRDAVFQGAMGGASGYMVFLLHKHHQHVLYLKNSKLLYRTPPELRAAQSVLLLMLCFVFFYWTDCAFSLVLSLSSRDKTLTVNPRELLTLGYATFSPLVLIHRDGLLFECCHAQLKKLRNCLSFICSTRKKKLSVLQHCG
Protein: Mucin 1, cell surface associated (A0A087X0L2)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MTPGTQSPFFLLLLLTVLTATTAPKPATVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAIPAPTTTKSCRETFLKWPGSVVVQLTLAFREGTINVHDVETQFNQYKTEAASRYNLTISDVSVSDVPFPFSAQSGAGVPGWGIALLVLVCVLVALAIVYLIALAVCQCRRKNYGQLDIFPARDTYHPMSEYPTYHTHGRYVPPSSTDRSPYEKVSAGNGGSSLSYTNPAVAATSANL
Protein: Zinc finger protein 135 (Zinc finger protein 61) (Zinc finger protein 78-like 1) (P52742)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of cell morphology and cytoskeletal organization. May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MTPGVRVSTDPEQVTFEDVVVGFSQEEWGQLKPAQRTLYRDVMLDTFRLLVSVGHWLPKPNVISLLEQEAELWAVESRLPQGVYPDLETRPKVKLSVLKQGISEEISNSVILVERFLWDGLWYCRGEDTEGHWEWSCESLESLAVPVAFTPVKTPVLEQWQRNGFGENISLNPDLPHQPMTPERQSPHTWGTRGKREKPDLNVLQKTCVKEKPYKCQECGKAFSHSSALIEHHRTHTGERPYECHECLKGFRNSSALTKHQRIHTGEKPYKCTQCGRTFNQIAPLIQHQRTHTGEKPYECSECGKSFSFRSSFSQHERTHTGEKPYECSECGKAFRQSIHLTQHLRIHTGEKPYQCGECGKAFSHSSSLTKHQRIHTGEKPYECHECGKAFTQITPLIQHQRTHTGEKPYECGECGKAFSQSTLLTEHRRIHTGEKPYGCNECGKTFSHSSSLSQHERTHTGEKPYECSQCGKAFRQSTHLTQHQRIHTGEKPYECNDCGKAFSHSSSLTKHQRIHTGEKPYECNQCGRAFSQLAPLIQHQRIHTGEKPYECNQCGRAFSQSSLLIEHQRIHTKEKPYGCNECGKSFSHSSSLSQHERTHTGEKPYECHDCGKSFRQSTHLTQHRRIHTGEKPYACRDCGKAFTHSSSLTKHQRTHTG
Protein: Protein S100 (S100 calcium-binding protein) (A0A0S2Z4C5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE
Protein: Medium-wave-sensitive opsin 1 (Green cone photoreceptor pigment) (Green-sensitive opsin) (Medium wavelength-sensitive cone opsin) (O35476)
Organism: Rattus norvegicus (Rat)
Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. May increase spectral sensitivity in dim light.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- G protein subunit alpha transducin 2
- G protein subunit alpha transducin 1
- Short-wave-sensitive opsin 1
- Arrestin-C
- Cone-rod homeobox protein
- Recoverin
- Guanine nucleotide-binding protein subunit gamma
- Phosphodiesterase
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MAQQLTGEQTLDHYEDSTQASIFTYTNSNSTRGPFEGPNYHIAPRWVYHLTSTWMILVVIASVFTNGLVLAATMRFKKLRHPLNWILVNLAVADLAETIIASTISVVNQIYGYFVLGHPLCVIEGYIVSLCGITGLWSLAIISWERWLVVCKPFGNVRFDAKLATVGIVFSWVWAAVWTAPPIFGWSRYWPYGLKTSCGPDVFSGTSYPGVQSYMMVLMVTCCIFPLSIIVLCYLQVWLAIRAVAKQQKESESTQKAEKEVTRMVVVMVFAYCLCWGPYTFFACFATAHPGYAFHPLVASLPSYFAKSATIYNPIIYVFMNRQFRNCILQLFGKKVDDSSELSSTSKTEVSSVSSVSPA
Protein: Prefoldin subunit 3 (von Hippel-Lindau-binding protein 1) (VBP-1) (VHL-binding protein 1) (P61759)
Organism: Mus musculus (Mouse)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins (By similarity).
Subcellular location: Cytoplasm. Nucleus. Note=In complex with VHL can translocate to the nucleus.
Interaction partners:
- Prefoldin subunit 2
- Prefoldin subunit 4
- Prefoldin subunit 1
- Prefoldin subunit 5
- Prefoldin subunit 6
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit eta
Sequence:
MAAAKDGCGLETAAGNGRRLHLGIPEAVFVEDVDSFMKQPGNETADTVLKKLDEQYQKYKFMELNLAQKKRRLKGQIPEIKQTLEILKYMQKKKESTNSMETRFLLADNLYCKASVPPTDKVCLWLGANVMLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQFTTTEVNMARVYNWDVKRRNKDDSTKNKA
Protein: Huntingtin interacting protein 1 related (F1LML7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Cyclin-G-associated kinase
- Clathrin heavy chain 1
- Epsin-3
- Epsin-2
- Epsin-1
- Clathrin light chain A
- Huntingtin
- Src-like-adapter 2
- Phosphatidylinositol-binding clathrin assembly protein
- Src substrate cortactin
Sequence:
MNSIKNVPARVLSRRPGHSLEAEREQFDKTQAISISKAINSQEAPVKEKHARRIILGTHHEKGAFTFWSYAIGLPLPSSSILSWKFCHVLHKVLRDGHPNVLHDCQRYRSNIREIGDLWGHLRDQYGHLVNIYTKLLLTKISFHLKHPQFPAGLEVTDEVLEKAAGTDVNNIFQLTVEMFDYMDCELKLSESVFRQLNTAIAVSQMSSGQCRLAPLIQVIQDCSHLYHYTVKLMFKLHSCLPADTLQGHRDRFHEQFHSLRNFFRRASDMLYFKRLIQIPRLPEGPPNFLRASALAEHIKPVVVIPEEAPEEEEPENLIEISSGPPAGEPVQVVADLFDQTFGPPNGSMKDDRDLQIENLKREVETLRAELEKIKMEAQRYISQLKGQVNSLEAELEEQRKQKQKALVDNEQLRHELAQLKALQLEGARNQGLREEAERKASATEARYSKLKEKHNELINTHAELLRKNADTAKQLTVTQQSQEEVARVKEQLAFQMEQVKRESEMKMEEQSDQLEKLKRELVAKAGELAHAQEALSRTEQSGSELSSRLDTLNAEKEALSGAIRQREAELLAAQSLVREKEEALSQEQQRSAQEKGELQGRLAEKESQEQGLQQKLLDEQFAVLRGAAAEAEAILQDAVSKLDDPLHLRCTSSPDYLVSRAQAALDSVSGLEKGHTQYLASSEDASALVAALTRFSHLAADTIVNGGATSHLAPTDPADRLIDTCRECGARALELMGQLQDQTKLPRAQPSLMRAPLQGILQLGQDLKPKSLDVRQEELGAMVDKEMAATSAAIEDAVRRIEDMMNQARHESSGVKLEVNERILNSCTDLMKAIRLLVMTSTSLQKEIVESGRGAATQQEFYAKNSRWTEGLISASKAVGWGATQLVESADKVVLHMGKYEELIVCSHEIAASTAQLVAASKVKANKNSPHLSRLQECSRTVNERAANVVASTKSGQEQIEDRDTMDFSGLSLIKLKKQEMETQVRVLELEKTLEAERVRLGELRKQHYVLAGGMGTPGEEEPSRPSPAPRSGATKKPPLAQKPSIAPRPDNQLDKKDGVYPAQLVNY
Protein: phosphatidate phosphatase (EC 3.1.3.4) (F7FDH2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MNYVGQLAGQVFVTVKELYKGLNPATLSGCIDIIVVRQPNGSLQCSPFHVRFGKMGVLRSREKVVDIEINGESVDLHMKLGDNGEAFFVQETDNDQEVIPMYLATSPILSEGASRMESQLKRNSVDRIRGLDPTTAAQGLPPSDTPSTGSLGKKRRKRRRKAHLDNLKRDDNVNTSEDEDMFPIEMSSDEDTALMDGSRALPNDVPPFQDDIPKENLPSISTYPQSASYPNSDREWSPSPSSLVDCQRTPPHLAEGVLSSSCPLQSCHFHASESPSGSRPSTPKSDSELVSKSADRLTPKNNLEMLWLWGELPQAAKSSSPHKMKDSSPLGGRKMADKIHFQTIHSESSDTFSDQSPTMARGLLIHQSKAQTEMQFVNEEDLEALGAAAPPLSVAEELKAPASSTAQTSSKSDSPSRKKDKRSRHLGADGVYLDDLTDMDPEVAALYFPKNGDPGGLPKQASDNGARSANQSPQSVGSSGIDSGVESTSDSLRDLPSIAISLCGGLSDHREITKDAFLEQAVSYQQFADNPAIIDDPNLVVKIGNKYYNWTTAAPLLLAMQAFQKPLPKSSCLSYLHMILDAIRFCLSKIFSPPTATVESIMRDKMPKKGGRWWFSWRGRNATIKEESKPEQGLPGKGHNTGEQPAQLGLTTRIKHESSSSDEEHSATKPSSSSHLSLLSNVSYKKTLRLTSEQLKSLKLKNGPNDVVFSVTTQYQGTCRCEGTIYLWNWDDKVIISDIDGTITRSDTLGHILPTLGKDWTHQGIAKLYHKVSQNGYKFLYCSARAIGMADMTRGYLHWVNERGTVLPQGPLLLSPSSLFSALHREVIEKKPEKFKVQCLTDIKNLFFPNTEPFYAAFGNRPADVYSYKQVGVSLNRIFTVNPKGELVQEHAKTNISSYVRLCEVVDHVFPLLKRSHSCDFPCSDTFSNFTFWREPLPPFENQDVHSASA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8JGT0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASSSGSKAEFIVGGKYKLVRKIGSGSFGDIYLAINITNGEEVAVKLESQKARHPQLLYESKLYKILQGGVGIPHIRWYGQEKDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSGGQGQQAQTPTGF
Protein: RIMS-binding protein 2 (RIM-BP2) (O15034)
Organism: Homo sapiens (Human)
Function: Plays a role in the synaptic transmission as bifunctional linker that interacts simultaneously with RIMS1, RIMS2, CACNA1D and CACNA1B.
Subcellular location: Cell membrane {ECO:0000250}. Synapse {ECO:0000250}. Note=Synaptic plasma membrane. {ECO:0000250}.
Interaction partners:
- Regulating synaptic membrane exocytosis protein 2
- Regulating synaptic membrane exocytosis protein 1
- Ras-related protein Rab-3C
- Protein unc-13 homolog B
- Ras-related protein Rab-3A
- Voltage-dependent P/Q-type calcium channel subunit alpha-1A
Sequence:
MREAAERRQQLQLEHDQALAVLSAKQQEIDLLQKSKVRELEEKCRTQSEQFNLLSRDLEKFRQHAGKIDLLGGSAVAPLDISTAPSKPFPQFMNGLATSLGKGQESAIGGSSAIGEYIRPLPQPGDRPEPLSAKPTFLSRSGSARCRSESDMENERNSNTSKQRYSGKVHLCVARYSYNPFDGPNENPEAELPLTAGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVDFVQDNESRLASTLGNEQDQNFINHSGIGLEGEHILDLHSPTHIDAGITDNSAGTLDVNIDDIGEDIVPYPRKITLIKQLAKSVIVGWEPPAVPPGWGTVSSYNVLVDKETRMNLTLGSRTKALIEKLNMAACTYRISVQCVTSRGSSDELQCTLLVGKDVVVAPSHLRVDNITQISAQLSWLPTNSNYSHVIFLNEEEFDIVKAARYKYQFFNLRPNMAYKVKVLAKPHQMPWQLPLEQREKKEAFVEFSTLPAGPPAPPQDVTVQAGVTPATIRVSWRPPVLTPTGLSNGANVTGYGVYAKGQRVAEVIFPTADSTAVELVRLRSLEAKGVTVRTLSAQGESVDSAVAAVPPELLVPPTPHPRPAPQSKPLASSGVPETKDEHLGPHARMDEAWEQSRAPGPVHGHMLEPPVGPGRRSPSPSRILPQPQGTPVSTTVAKAMAREAAQRVAESSRLEKRSVFLERSSAGQYAASDEEDAYDSPDFKRRGASVDDFLKGSELGKQPHCCHGDEYHTESSRGSDLSDIMEEDEEELYSEMQLEDGGRRRPSGTSHNALKILGNPASAGRVDHMGRRFPRGSAGPQRSRPVTVPSIDDYGRDRLSPDFYEESETDPGAEELPARIFVALFDYDPLTMSPNPDAAEEELPFKEGQIIKVYGDKDADGFYRGETCARLGLIPCNMVSEIQADDEEMMDQLLRQGFLPLNTPVEKIERSRRSGRRHSVSTRRMVALYDYDPRESSPNVDVEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEEVPDDVEVYLSDAPSHYSQDTPMRSKAKRKKSVHFTP