wanglab/gogpt-training-data huggingface dataset:
Protein: dolichyl-diphosphooligosaccharide--protein glycotransferase (EC 2.4.99.18) (Q5ALU8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycotransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1
- Dolichyl-diphosphooligosaccharide--protein glycotransferase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit delta
- Protein transport protein SEC61 subunit alpha
- Protein transport protein Sec61 subunit beta
- Dol-P-Glc:Glc
- Mannosyl-oligosaccharide glucosidase
Sequence:
MASTISSKPQLKVLGIDVESIRVLLKVIIFISIAGAAISSRLFSVIRFESIIHEFDPWFNFRATKYLVTHSFYEFLNWFDDRTWYPLGRVTGGTLYPGLMVTSGAIWHILRDWFALPVDIRNICVLLAPVFSGLTAICTYFLTKEMKDSSAGLLAAIFMGIAPGYISRSVAGSYDNEAIAITLLMATFYFWIKSMKMGSVFYATLTALFYFYMVSAWGGYVFITNLIPLHVFVLIFMGRYNAKLYTAYTTWYALGTLASMQIPFVGFLPIRSNDHMAALGVFGLLQLVAFGDYVKSKVPTKQFKSFLIVSIVLVVGLGIGGLFGLTAMGWIAPWTGRFYSLWDTNYAKIHIPIIASVSEHQPTAWPAFFFDTSMLIWLFPAGIYLCFQELKDEHVFIIIYSVLCSYFAGVMVRLMLTLTPVICVAAAIALSKLFDVYLDIVDLFTEKVGKYDDDVSDESKSSTKKSSSRFPIAGYLSKVLVLSTFTFYLFYFVLHCTWVTSNAYSSPSVVLASRNPDGSQHIIDDYREAYYWLRMNTPEDAKVMAWWDYGYQIGGMADRTTLVDNNTWNNTHIATVGKAMSSPEDVSYEILRQHDVDYVLVIFGGLLGYSGDDINKFLWMVRIAEGIWPDEIKERDYFTDRGEYKVDKDASSAMKNSLMYKLSYHRFTELFGGRDGVDRVRNQQIPANEVPKLNVVEEAFTSENWIVRIYKVKDLDNVGRDLHQATAFEESSSGTSKRNRSIKRPKLEVRE
Protein: Oxidation resistance protein 1 (Q8IPN6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MSTDEYRKTSLFATGSFDLDFPIPDLIGKTEILTEEHREKLCSHLPARAEGYSWSLIFSTSQHGFALNSLYRKMARLESPVLIVIEDTEHNVFGALTSCSLHVSDHFYGTGESLLYKFNPSFKVFHWTGENMYFIKGNMESLSIGAGDGRFGLWLDGDLNQGRSQQCSTYGNEPLAPQEDFVIKTLECWAFV
Protein: Protein eva-1 homolog A (Protein FAM176A) (Transmembrane protein 166) (Q9H8M9)
Organism: Homo sapiens (Human)
Function: Acts as a regulator of programmed cell death, mediating both autophagy and apoptosis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17492404}; Single-pass membrane protein {ECO:0000269|PubMed:17492404}. Lysosome membrane {ECO:0000269|PubMed:17492404}; Single-pass membrane protein {ECO:0000269|PubMed:17492404}.
Interaction partners:
- Autophagy-related protein 16-1
Sequence:
MRLPLSHSPEHVEMALLSNILAAYSFVSENPERAALYFVSGVCIGLVLTLAALVIRISCHTDCRRRPGKKFLQDRESSSDSSDSEDGSEDTVSDLSVRRHRRFERTLNKNVFTSAEELERAQRLEERERIIREIWMNGQPEVPGTRSLNRYY
Protein: Histone H3-like centromeric protein CENH3 (Centromeric histone CENH3) (Centromeric histone H3) (Histone H3-like centromeric protein HTR12) (Q8RVQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity).
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000269|PubMed:12034896, ECO:0000269|PubMed:17028205, ECO:0000269|PubMed:21695238}. Note=Localizes exclusively in the kinetochore domain of centromeres (PubMed:12034896, PubMed:17028205). Localized at centromeres in both mitotic and meiotic cells (PubMed:21695238). {ECO:0000269|PubMed:12034896, ECO:0000269|PubMed:17028205, ECO:0000269|PubMed:21695238}.
Interaction partners:
- Histone H4
- Protein TONSOKU
- Histone H2B.6
- Chromo domain-containing protein LHP1
- Lysine-specific demethylase ELF6
- DNA
- Histone acetyltransferase GCN5
- Histone-lysine N-methyltransferase CLF
- Chromatin structure-remodeling complex protein SYD
- Histone-lysine N-methyltransferase ASHH2
Sequence:
MARTKHRVTRSQPRNQTDAAGASSSQAAGPTTTPTRRGGEGGDNTQQTNPTTSPATGTRRGAKRSRQAMPRGSQKKSYRYRPGTVALKEIRHFQKQTNLLIPAASFIREVRSITHMLAPPQINRWTAEALVALQEAAEDYLVGLFSDSMLCAIHARRVTLMRKDFELARRLGGKGRPW
Protein: Ankyrin 2 (A0A5F9ZI56)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MTTMLQKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKMMVNRTTESGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERGAPLLARTKNGLSPLHMAAQGDHVECVKHLLQHKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNIVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADQDAHTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKVVTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTMTGDGGEYLRPEDLKELGDDSLPSSQFLDGMNYLRYSLEGGRSDSLRSFSSDRSHTLSHASYLRDSAVMDDSVVIPSHQVSTLAKEAERNSYRLSWGTENLDNVALSSSPIHSGFLVSFMVDARGGAMRGCRHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQFLGKLHLPTAPPPLNEGESLVSRILQLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSENGDSWKEHFCDYTEDELNEILNGMDEVLDSPEDLEKKRICRIITRDFPQYFAVVSRIKQDSNLIGPEGGVLSSTVVPQVQAVFPEGALTKRIRVGLQAQPMHSELVKKILGNKATFSPIVTLEPRRRKFHKPITMTIPVPKASSDVMLNGFGGDAPTLRLLCSITGGTTPAQWEDITGTTPLTFVNECVSFTTNVSARFWLIDCRQIQESVTFASQVYREIICVPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFAEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSFFAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLPIYTKESESDQEQEEEIDMTSEKNPQDEQERIEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLVECLTKINRMDIVHLMETNTEPLQERISHSYAEIEQTITLDHSEGFSVLQEELCTAQHKQKEEQAVSKESETCDHPPIVSEEDISVGYSTFQDGVPKTEGDSSATALFPQTHKEQVQQDFSGKMQDLPEESSLEYQQEYFVTTPGTETSETQKAMIVPSSPSKTPEEVSTPAEEEKLYLQTPTSSERGGSPIIQEPEEPSEHREESSPRKTSLVIVESADNQPETCERLDEDAAFEKELTEELGELEASSDEEAMVTTRVVRRRVIIQGDDMPEIPPETVTEEEYIDEHGHTVVKKVTRKIIRRYVSSEGTEKEEIMVQGMPQEPVNIEEGDGYSKVIKRVVLKSDTEQSEDNNE
Protein: Cysteine and glycine-rich protein 3 (Cardiac LIM protein) (Cysteine-rich protein 3) (CRP3) (LIM domain protein, cardiac) (Muscle LIM protein) (P50461)
Organism: Homo sapiens (Human)
Function: Positive regulator of myogenesis. Acts as cofactor for myogenic bHLH transcription factors such as MYOD1, and probably MYOG and MYF6. Enhances the DNA-binding activity of the MYOD1:TCF3 isoform E47 complex and may promote formation of a functional MYOD1:TCF3 isoform E47:MEF2A complex involved in myogenesis (By similarity). Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation (By similarity). The role in regulation of cytoskeleton dynamics by association with CFL2 is reported conflictingly: Shown to enhance CFL2-mediated F-actin depolymerization dependent on the CSRP3:CFL2 molecular ratio, and also shown to reduce the ability of CLF1 and CFL2 to enhance actin depolymerization. Proposed to contribute to the maintenance of muscle cell integrity through an actin-based mechanism. Can directly bind to actin filaments, cross-link actin filaments into bundles without polarity selectivity and protect them from dilution- and cofilin-mediated depolymerization; the function seems to involve its self-association. In vitro can inhibit PKC/PRKCA activity. Proposed to be involved in cardiac stress signaling by down-regulating excessive PKC/PRKCA signaling (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P50463}. Cytoplasm {ECO:0000269|PubMed:18505755}. Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:24860983}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:24934443}. Note=Nucleocytoplasmic shuttling protein. Mainly cytoplasmic. In the Z line, found associated with GLRX3 (By similarity). {ECO:0000250|UniProtKB:P50462, ECO:0000250|UniProtKB:P50463}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:24860983}.
Interaction partners:
- Telethonin
- Titin
- Alpha-actinin-2
- Myosin-7
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myozenin-2
- Myosin-binding protein C, cardiac-type
- Myosin light chain 3
- Myosin light chain 1/3, skeletal muscle isoform
- Xin actin-binding repeat-containing protein 2
Sequence:
MPNWGGGAKCGACEKTVYHAEEIQCNGRSFHKTCFHCMACRKALDSTTVAAHESEIYCKVCYGRRYGPKGIGYGQGAGCLSTDTGEHLGLQFQQSPKPARSVTTSNPSKFTAKFGESEKCPRCGKSVYAAEKVMGGGKPWHKTCFRCAICGKSLESTNVTDKDGELYCKVCYAKNFGPTGIGFGGLTQQVEKKE
Protein: Transcription factor Spi-C (Pu.1-related factor) (Prf) (Q6P3D7)
Organism: Mus musculus (Mouse)
Function: Controls the development of red pulp macrophages required for red blood cells recycling and iron homeostasis. Transcription factor that binds to the PU-box, a purine-rich DNA sequence (5'-GAGGA[AT]-3') that can act as a lymphoid-specific enhancer. Regulates VCAM1 gene expression.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MTCCIDQDSLGQTFQDAIDILIQQSAGESQYSSENRNYMAIINPYPHVRGNANYYGMSPTENPLYDWRGVTNGSADLYLEGGFHQSVQNIAESQLVQPPFFQQKGGRGRRKLRLFEYLFESLCNSEMVSCIQWVDKARGIFQFISKNKETLAELWGQRKGNRKPMTYQKMARALRNYARTGEIIKIRRKLTYQFSEAVLQRLAPANYLGKDLFYPQYGQPDQGYLSLNHWNANHYAHGSYQS
Protein: NIPA-like protein 3 (Q6P499)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1
Sequence:
MDGSHSAALKLQQLPPTSSSSAVSEASFSYKENLIGALLAIFGHLVVSIALNLQKYCHIRLAGSKDPRAYFKTKTWWLGLFLMLLGELGVFASYAFAPLSLIVPLSAVSVIASAIIGIIFIKEKWKPKDFLRRYVLSFVGCGLAVVGTYLLVTFAPNSHEKMTGENVTRHLVSWPFLLYMLVEIILFCLLLYFYKEKNANNIVVILLLVALLGSMTVVTVKAVAGMLVLSIQGNLQLDYPIFYVMFVCMVATAVYQAAFLSQASQMYDSSLIASVGYILSTTIAITAGAIFYLDFIGEDVLHICMFALGCLIAFLGVFLITRNRKKPIPFEPYISMDAMPGMQNMHDKGMTVQPELKASFSYGALENNDNISEIYAPATLPVMQEEHGSRSASGVPYRVLEHTKKE
Protein: LD24714p (Pre-mRNA processing factor 40) (Q9VQK5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Putative RNA-binding protein Alsin2
- U1 small nuclear ribonucleoprotein 70 kDa
- U1 small nuclear ribonucleoprotein C
- BcDNA.LD23634
- Pre-mRNA-processing factor 39
- Cell division cycle 5, isoform A
- Branchpoint-bridging protein
- Probable small nuclear ribonucleoprotein Sm D1
- Probable small nuclear ribonucleoprotein G
- RE11167p
Sequence:
MNVPPSVGNGGAPPGRGIGYTPPGAIVPQFPPPGFGAPPPPELAAAFGVMATSTEWTEHKAPDGRPYYYNQNTKQSSWEKPEALMTPAELLHNQCPWKEYRSDTGKVYYHNVATKETCWEPPPEYVDMKAKAKAEEAAAAAKAVAAMTSSSLAGMVPPAALASILPAALPVAPRLPTPEIHSPLTPSSNENSSSAMDQAMAATLAAIEVPQQNAKKDDKSESAVVFKDKREAIESFKELLRDRNVPSNANWDQCVKIISKDPRYAAFKNLNERKQTFNAYKTQKIKDEREESRLKAKKAKEDLEQFLMSSDKMNSQMKYFRCEEVFAGTRTWTAVPEPDRRDIYEDCIFNLAKREKEEARLLKKRNMKVLGELLESMTSINHATTWSEAQVMLLDNVAFKNDVTLLGMDKEDALIVFEEHIRTLEKEEDEEREREKKRMKRQQRKNRDSFLALLDSLHEEGKLTSMSLWVELYPIISADLRFSAMLGQSGSTPLDLFKFYVENLKARFHDEKKIIREILKEKAFVVQAKTSFEDFATVVCEDKRSASLDAGNVKLTYNSLLEKAEAIEKERMKEEVRRLRKLENEIKNEWLEANVSVAEPYESAKKLVEHLEAFALYEKEIGVEKIWEDFVKESEDACSHHHSRSRKSKKNKKHKKRVRSVSRSDIENEHIEVEKSKRRRSKTRSHSLTSIGSIESEKLLKKKKKRKNKLRGSSCESDVPGIQSPGTQALLQNDSNSHSPAKKKKKEKRAKKDKRHNRHNRSGTPLSPAQSVESSGSRNEELTLSDGELESKRAALLAQLSEQLDE
Protein: Potassium inward rectifier (Kir)-like channel 3 (AtKCO3) (Q9XFR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable calcium-activated potassium channel.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:16984403, ECO:0000269|PubMed:17764516}; Multi-pass membrane protein {ECO:0000269|PubMed:16984403, ECO:0000269|PubMed:17764516}.
Interaction partners:
- Potassium channel KAT3
- Potassium channel SKOR
- Potassium channel GORK channel)
- Potassium transporter 2
- Two pore calcium channel protein 1
- Potassium transporter 9
- Potassium transporter 7
- Potassium transporter 3
- K
Sequence:
MPMTPSEFKNRLLFGSLPRSSSDPTDLQFTEPNVPPSLFSLPEHNDDTATDMAPDQETEQSVSKSIARQALALLVVYLSLGVLIYWLTLDSDNAYQTHPVAVALYFFVVTFCGFLIVHFVVKIGWLDSFCFSVMMVTTVGFGDRAFNTWLGTFLAAVWLLVSTLAVARAFLFLADARADKRNRERAKKVLGESISISQFFAADIDNDGRLSLAEFAIYKLKQMEKITQEDFIQICNQFDKLDRTQSGRITLVDLTTATSV
Protein: AP-3 complex subunit sigma-2 (AP-3 complex subunit sigma-3B) (Adaptor-related protein complex 3 subunit sigma-2) (Sigma-3B-adaptin) (Sigma3B-adaptin) (Sigma-adaptin 3b) (Q8BSZ2)
Organism: Mus musculus (Mouse)
Function: Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Subcellular location: Golgi apparatus. Cytoplasmic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.
Interaction partners:
- AP-3 complex subunit delta-1
- AP-3 complex subunit mu-2
- AP-3 complex subunit mu-1
- AP-3 complex subunit beta-1
- AP-3 complex subunit beta-2
- AP-3 complex subunit sigma-1
- Arpin
- AP-4 complex subunit epsilon-1
- AP-2 complex subunit alpha-1
- AP-1 complex subunit gamma-1
Sequence:
MIQAILVFNNHGKPRLVRFYQRFPEEIQQQIVRETFHLVLKRDDNICNFLEGGSLIGGSDYKLIYRHYATLYFVFCVDSSESELGILDLIQVFVETLDKCFENVCELDLIFHMDKVHYILQEVVMGGMVLETNMNEIVAQIEAQNRLEKSEGGLSAAPARAVSAVKNINLPEIPRNINIGDLNIKVPNLSQFV
Protein: HIT domain-containing protein (Q57WA7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Tyrosyl-DNA Phosphodiesterase
Sequence:
MKRAVAAQKAVGGAVAKRSVANANAPRTRLPFLRNVAQNARRSPDTYRTATPFTSYPPHVSGQQQKKPTSHVLYKDPQCIIVNDAYPKSRLHCLVIPLDLSLDSLSALRPNHVPLLQHLMEVAEQYVQFTREDAASNEAGIQALSFMTGFHSLPSLPQLHMHLISRDLDGPCMKTKKHYNSFATPFFLPADQVVNDLRKNGCVTLNRNVEELNRFEHEEPRCLWCGLNPGGFQQLRVHLRTCKGNRAYVASSTAPVQQ
Protein: Vesicle-associated membrane protein-associated protein B/C (VAMP-B/VAMP-C) (VAMP-associated protein B/C) (VAP-B/VAP-C) (O95292)
Organism: Homo sapiens (Human)
Function: Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity. Involved in cellular calcium homeostasis regulation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:32344433, ECO:0000269|PubMed:33124732}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9P0L0}. Note=Present in mitochondria-associated membranes that are endoplasmic reticulum membrane regions closely apposed to the outer mitochondrial membrane. {ECO:0000269|PubMed:22131369}.
Interaction partners:
- Regulator of microtubule dynamics protein 3
- Acyl-CoA-binding domain-containing protein 5
- Cyclic AMP-dependent transcription factor ATF-6 alpha
- Acyl-CoA-binding domain-containing protein 4
- Oxysterol-binding protein 1
- Vesicle-associated membrane protein-associated protein A
- Oxysterol-binding protein-related protein 9
- Membrane-associated phosphatidylinositol transfer protein 1
- StAR-related lipid transfer protein 3
- Ceramide transfer protein
Sequence:
MAKVEQVLSLEPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGIIDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPTDTSDMEAVWKEAKPEDLMDSKLRCVFELPAENDKPHDVEINKIISTTASKTETPIVSKSLSSSLDDTEVKKVMEECKRLQGEVQRLREENKQFKEEDGLRMRKTVQSNSPISALAPTGKEEGLSTRLLALVVLFFIVGVIIGKIAL
Protein: Leucine-rich repeat protein soc-2 (Suppressor of Clr protein 2) (Suppressor of activated let-60 Ras protein 8) (Q22875)
Organism: Caenorhabditis elegans
Function: Acts as a Ras effector and participates in MAPK pathway activation. Probably acts as a regulatory subunit of protein phosphatase that specifically dephosphorylates Raf kinase and stimulates Raf activity at specialized signaling complexes upon Ras activation. Required for vulval development. Involved in fluid homeostasis. Plays a role in nicotinic acetylcholine receptor (nAChR)-mediated sensitivity to nicotine.
Interaction partners:
- Ras protein let-60
- Raf homolog serine/threonine-protein kinase
- Serine/threonine-protein phosphatase 2A regulatory subunit sur-6
- Kinase suppressor of Ras A
- GTP binding protein
- Receptor tyrosine-protein kinase let-23
- Latrophilin-like protein 1
- Sex muscle abnormal protein 5
Sequence:
METSKEFEFRPAKETSRSKSPGGIVGRLSNFARNKARHSLSEKGSNSVGGSGGAGFDKPRKDLLKEFHKCKEAQDQRLDLSSIEITSIPSPIKELTQLTELFLYKNKLTCLPTEIGQLVNLKKLGLSENALTSLPDSLASLESLETLDLRHNKLTEVPSVIYKIGSLETLWLRYNRIVAVDEQIGNLSKLKMLDVRENKIRELPSAIGKLTSLVVCLVSYNHLTRVPEEIGDCHSLTQLDLQHNDLSELPYSIGKLVNLVRIGIRYNKIRCIPSELESCQQLEEFIVESNHLQLLPPNLLTMLPKIHTVNLSRNELTAFPAGGPQQFVSTVTINMEHNQISKIPIGIFSKATRLTKLNLKENELVSLPLDMGSWTSITELNLSTNQLKVLPEDIEKLVNLEILVLSNNQLKKLPNQIGNLNKLRELDLEENELETVPTEIGFLQHLTKLWVQSNKILTLPRSIGNLCSLQDLRLGENNLTAIPEEIGHLDSLKSLYLNDNSSLHNLPFELALCQSLEIMSIENSPLSQIPPEITAGGPSLVIQYLKMQGPYRGVVMNSQ
Protein: Protein kinase, putative (EC 2.7.1.-) (Q57YS8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Anti-silencing protein ASF 1 like protein, putative
Sequence:
MKNNDANHMRKRSREDPTNAEAAEFSEDQGVGGQQTEVKGTKSSSTSRVSPEIPDESACIYEYVSGPTAVSTSGGNSGNSPGSTHPSERKLKQATLPSYGLVNDTAVFRKELADRDAQIDELREKLAAVETRMSERETTLVNTQAQLQEAVDRNNRYQVVLREEMLRAARQERCDARRALHLKQFELGQIAVWHSNGREVWVEGNKMRQLTMQLEELSVRRDEVEELKKTAEKRARQILRSNDEDSMAPEAQAALMELQEAALLYTAEFAALGSAIQSLKQQQQDLNHEKKVFLKEIRRVNDEDASAFVAVPALGHNGRYVMMHLLGKGGFSEVWKAFDLQEARYVACKIHRVQREWSQQVRQHYRDRAVRELKIMRMLEHPHLTRLFDAFDHGTATFVSVMEFSAGTDLDTHLKRCGTLREVEARLIIMQVVSALRYFAAQHQPVIHYDLKPANILLHSSNQSSLLIKITDFGLSKLIPKRDGASDNPTIELTSQGAGTYWYLPPECFDTTATPRISNKVDVWSCGVIFYQMLFGRRPFAEGESQQQIWQNKLIVSSAHTLTFPDTPRVSQEAKDLIQKCLEYHPADRYDVMQLSQDPYLQRNTRRLSRTERTLPAATQNSSTTVVTTAAAASGVTLTGSVEEKLSNIP
Protein: Progesterone receptor (PR) (Nuclear receptor subfamily 3 group C member 3) (Q63449)
Organism: Rattus norvegicus (Rat)
Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Depending on the isoform, progesterone receptor functions as transcriptional activator or repressor (By similarity).
Subcellular location: Nucleus. Cytoplasm. Note=Nucleoplasmic shuttling is both hormone- and cell cycle-dependent. On hormone stimulation, retained in the cytoplasm in the G(1) and G(2)/M phases (By similarity). {ECO:0000250}.
Interaction partners:
- Nuclear receptor coactivator
- Estrogen receptor
- Nuclear receptor corepressor 2
- Nuclear receptor coactivator 3
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Peptidyl-prolyl cis-trans isomerase FKBP4
- Nuclear receptor corepressor 1
- Mitogen-activated protein kinase 14
Sequence:
MTELQAKDPRTLHTSGAAPSPTHVGSPLLARLDPDPFQGSQHSDASSVVSPIPISLDRLLFSRSCQAQELPDEKTQNQQSLSDVEGAFSGVEASRRRSRNPRAPEKDSRLLDSVLDTLLAPSGPEQSQTSPPACEAITSWCLFGPELPEDPRSVPATKGLLSPLMSRPESKAGDSSGTGAGQKVLPKAVSPPRQLLLPTSGSAHWPGAGVKPSQQPATVEVEEDGGLETEGSAGPLLKSKPRALEGMCSGGGVTANAPGAAPGGVTLVPKEDSRFSAPRVSLEQDAPVAPGRSPLATTVVDFIHVPILPLNHALLAARTRQLLEGDSYDGGAAAQVPFAPPRGSPSAPSPPVPCGDFPDCTYPPEGDPKEDGFPVYGEFQPPGLKIKEEEEGTEAASRSPRPYLLAGASAATFPDFPLPPRPPRAPPSRPGEAAVAAPSAAVSPVSSSGSALECILYKAEGAPPTQGSFAPLPCKPPAASSCLLPRDSLPAAPTSSAAPAIYPPLGLNGLPQLGYQAAVLKDSLPQVYPPYLNYLRPDSEASQSPQYGFDSLPQKICLICGDEASGCHYGVLTCGSCKVFFKRAMEGQHNYLCAGRNDCIVDKIRRKNCPACRLRKCCQAGMVLGGRKFKKFNKVRVMRALDGVALPQSVAFPNESQTLGQRITFSPNQEIQLVPPLINLLMSIEPDVVYAGHDNTKPDTSSSLLTSLNQLGERQLLSVVKWSKSLPGFRNLHIDDQITLIQYSWMSLMVFGLGWRSYKHVSGQMLYFAPDLILNEQRMKELSFYSLCLTMWQIPQEFVKLQVTHEEFLCMKVLLLLNTIPLEGLRSQSQFEEMRSSYIRELIKAIGLRQKGVVPSSQRFYQLTKLLDSLHDLVKQLHLYCLNTFIQSRALAVEFPEMMSEVIAAQLPKILAGMVKPLLFHKK
Protein: Peptidyl-prolyl cis-trans isomerase ESS1 (PPIase ESS1) (EC 5.2.1.8) (Parvulin ESS1) (Processing/termination factor 1) (P22696)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential PPIase specific for phosphoserine and phosphothreonine N-terminal to the proline residue. Required for efficient pre-mRNA 3'-end processing and transcription termination, probably by inducing conformational changes by proline-directed isomerization in the C-terminal domain (CTD) of RPB1, thereby altering cofactor binding with the RNA polymerase II transcription complex. Also targets the SIN3-RPD3 histone deacetylase complex (HDAC).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB1
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Peptidyl-prolyl cis-trans isomerase
- Transcription factor BYE1
- RNA polymerase II subunit A C-terminal domain phosphatase
- Bud emergence protein 1
- Pyrroline-5-carboxylate reductase
- Peptidyl-prolyl cis-trans isomerase CYP8
- Transcription elongation factor SPT5
- Threonine synthase
Sequence:
MPSDVASRTGLPTPWTVRYSKSKKREYFFNPETKHSQWEEPEGTNKDQLHKHLRDHPVRVRCLHILIKHKDSRRPASHRSENITISKQDATDELKTLITRLDDDSKTNSFEALAKERSDCSSYKRGGDLGWFGRGEMQPSFEDAAFQLKVGEVSDIVESGSGVHVIKRVG
Protein: DnaJ heat shock protein family (Hsp40) member B6 (A0A0J9YX62)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVDYYEVLGVQRHASPEDIKKAYRKLALKWHPDKNPENKEEAERKFKQVAEAYEVLSDAKKRDIYDKYGKEGLNGGGGGGSHFDSPFEFGFTFRNPDDVFREFFGGRDPFSFDFFEDPFEDFFGNRRGPRGSRSRGTGSFFSAFSGFPSFGSGFSSFDTGFTSFGSLGHGGLTSFSSTSFGGSGMGNFKSISTSTKMVNGRKITTKRIVENGQERVEVEEDGQLKSLTINGVADDDALAEERMRRGQNALPAQPAGLRPPKPPRPASLLRHAPHCLSEEEGEQDRPRAPGPWDPLASAAGVQREAAVEQAQSETSLGARGQRGHKPRLGCCVLT
Protein: Replication protein O (P03688)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Necessary for the bidirectional replication of DNA. It interacts with the ori (origin of replication) region of the genome during the initiation of replication.
Interaction partners:
Sequence:
MTNTAKILNFGRGNFAGQERNVADLDDGYARLSNMLLEAYSGADLTKRQFKVLLAILRKTYGWNKPMDRITDSQLSEITKLPVKRCNEAKLELVRMNIIKQQGGMFGPNKNISEWCIPQNEGKSPKTRDKTSLKLGDCYPSKQGDTKDTITKEKRKDYSSENSGESSDQPENDLSVVKPDAAIQSGSKWGTAEDLTAAEWMFDMVKTIAPSARKPNFAGWANDIRLMRERDGRNHRDMCVLFRWACQDNFWSGNVLSPAKLRDKWTQLEINRNKQQAGVTASKPKLDLTNTDWIYGVDLKTSPHRWLTLTVSRCVGSPTTCRNSTTKSRRYSR
Protein: TLC domain-containing protein 3A (Protein CT120) (Protein FAM57A) (Q8TBR7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Glutathione hydrolase 7
- Amino acid transporter heavy chain SLC3A2
Sequence:
MLLTLAGGALFFPGLFALCTWALRRSQPGWSRTDCVMISTRLVSSVHAVLATGSGIVIIRSCDDVITGRHWLAREYVWFLIPYMIYDSYAMYLCEWCRTRDQNRAPSLTLRNFLSRNRLMITHHAVILFVLVPVAQRLRGDLGDFFVGCIFTAELSTPFVSLGRVLIQLKQQHTLLYKVNGILTLATFLSCRILLFPFMYWSYGRQQGLSLLQVPFSIPFYCNVANAFLVAPQIYWFCLLCRKAVRLFDTPQAKKDG
Protein: Uncharacterized protein (A0A060VN46)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Cytochrome c
- Cytochrome c
- Cytochrome c domain-containing protein
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Telomerase protein component 1
- Cathepsin H
- Peptidase C1A papain C-terminal domain-containing protein
- Peptidase C1A papain C-terminal domain-containing protein
Sequence:
MIMEWKIVVPLFAVAFTVANAGLIGGPMDANMNDQGTRDALQFAVVEHNKKTNDMFVRQVAKVVNAQKQVVSGMKYIFTVQMGRTPCRKGGVEKVCSVHKDPQMAVPYKCTFEVWSRPWMSDIQMVKNQCES