wanglab/gogpt-training-data huggingface dataset:
Protein: HLH106 (Q24146)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDTTLMNLIDAPLDESMDLFKAEDVFEPFDADLHSDMLDIILNDMDLAPTQMYNMLLDEPRTHTQQTQSVDQQPQSVEQQPHVKSEHSSPVHIKEELHQQQQQSPLLVYKPDPLIATSYNCPQQQPTGLLKAAQPTATIHHMDAQRMPPNTAVYPPSLGSSFVYQSMSPPTSPVESANQNVNVMQPVAATPAPASAPLPQQSYPQPFITYNSKAGMTSDEAMYLLLQPTVASPTPSPPVAPPPTSTGSRASKVRVAPLAPSPAAMEVQGKVPINRVQPKVKEVKRSAHNAIERRYRTSINDKINELKNLVVGEQAKLNKSAVLRKSIDKIRDLQRQNHDLKAELQRLQRELMARDGSKVKDLLQLGTRPGRASKKRRESSQTFTTDAGLTPPRSDESDPSLSPMHSDISLPPSPYGGSTASCSSGSSSSNEEPLVVPSSMRGMATHSRLGLCMFMFAILAVNPFKTFLQRGHYDSNDDLGDMSGQRRILSYDVEGEGFAVWQQSSWIWLLNFTLMLGCLVKLLVYGDPQLDAQTDAYCQHRQRADFYFSQGQSSQAYAGYLNCLHMFGLSLPASRLECYLQTTWQFLRFLFHRLWLGRVLSRRSGGLFSNAASRKQALASARELALLFNRLNQLQLTGNGSRGDMNGIMMALFASNMAEVAHNLLTPRETICIHVMTALRMKRSAPKWLQQFFARYYMSRARQECGRTRATEQTQELRWAFTAYGYRYCATHVFTYDLSDSGEQDGFFTRLRNPCDPAAHVIKQYREHLLFKSIQCLVGAGHKSGGLPTSSVSGEAEQLQQQQHSGTIVSNVLKYTSLLKDTLWADEDERDTNVVWWADVLETAVHWLLGEDTLAEQLYGRIKQMPTQLQQCGENDHLPKALHAVLRAKMILLKNNGNALDKSLKQLVNILCDESSVELQECLTVNRITDAKGIKLLFQLLTCDWLLETRTALWELEHMNMEDDGFYQVPGEVLEKFQTDLNSLRNIVENIPNAQSRIYLYEAVCRLMAGASPCPTQQLLDRSLRSRNAHSSIFCGSKDRRQQNFVGGERERASAMYVACKYLPPALLSSPGERAGMLAEAAKTLEKVGDKRKLKECYQLMKSLGNGIGSVKA
Protein: 26S proteasome regulatory subunit 10B homolog A (26S proteasome AAA-ATPase subunit RPT4a) (26S proteasome subunit 10B homolog A) (Regulatory particle triple-A ATPase subunit 4a) (Q9SEI3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 13 homolog A
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome non-ATPase regulatory subunit 7 homolog A
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome regulatory subunit 6A homolog A
- Proteasome subunit alpha type-7-A
- Proteasome subunit alpha type-3
Sequence:
MTDVDESVRRRTAAVSEYRKKLLQHKELESRVRTARENLRGAKKEFNKTEDDLKSLQSVGQIIGEVLRPLDNERLIVKASSGPRYVVGCRSKVDKEKLTSGTRVVLDMTTLTIMRALPREVDPVVYNMLHEDPGNISYSAVGGLGDQIRELRESIELPLMNPELFLRVGIKPPKGVLLYGPPGTGKTLLARAIASNIDANFLKVVSSAIIDKYIGESARLIREMFNYAREHQPCIIFMDEIDAIGGRRFSEGTSADREIQRTLMELLNQLDGFDNLGKVKMIMATNRPDVLDPALLRPGRLDRKIEIPLPNEQSRMDILKIHAAGIAKHGEIDYEAIVKLAEGFNGADLRNICTEAGMFAIRAERDYVIHEDFMKAVRKLSEAKKLESSSHYNADFGKE
Protein: Clathrin interactor 1 isoform 1 (A0A0S2Z4Y4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLNMWKVRELVDKATNVVMNYSEIESKVREATNDDPWGPSGQLMGEIAKATFMYEQFPELMNMLWSRMLKDNKKNWRRVYKSLLLLAYLIRNGSERVVTSAREHIYDLRSLENYHFVDEHGKDQGINIRQKVKELVEFAQDDDRLREERKKAKKNKDKYVGVSSDSVGGFRYSERYDPEPKSKWDEEWDKNKSAFPFSDKLGELSDKIGSTIDDTISKFRRKDREDSPERCSDSDEEKKARRGRSPKGEFKDEEETVTTKHIHITQATETTTTRHKRTANPSKTIDLGAAAHYTGDKASPDQNASTHTPQSSVKTSVPSSKSSGDLVDLFDGTSQSTGGSADLFGGFADFGSAAASGSFPSQVTATSGNGDFGDWSAFNQAPSGPVASSGEFFGSASQPAVELVSGSQSALGPPPAASNSSDLFDLMGSSQATMTSSQSMNFSMMSTNTVGLGLPMSRSQNTDMVQKSVSKTLPSTWSDPSVNISLDNLLPGMQPSKPQQPSLNTMIQQQNMQQPMNVMTQSFGAVNLSSPSNMLPVRPQTNALIGGPMPMSMPNVMTGTMGMAPLGNTPMMNQSMMGMNMNIGMSAAGMGLTGTMGMGMPNIAMTSGTVQPKQDAFANFANFSK
Protein: Glutaredoxin-1 (EC 1.11.1.9) (EC 2.5.1.18) (Glutathione-dependent oxidoreductase 1) (P25373)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. GRX1 is less active as an oxidoreductase than GRX2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Glutathione reductase
- Thioredoxin-2
- Thioredoxin-1
- Peroxiredoxin PRX1, mitochondrial
- Monothiol glutaredoxin-3
- Catalase T
- Glutathione peroxidase-like peroxiredoxin HYR1
- Glutathione peroxidase-like peroxiredoxin 1
- Monothiol glutaredoxin-7
- Glutaredoxin-2
Sequence:
MVSQETIKHVKDLIAENEIFVASKTYCPYCHAALNTLFEKLKVPRSKVLVLQLNDMKEGADIQAALYEINGQRTVPNIYINGKHIGGNDDLQELRETGELEELLEPILAN
Protein: Protein O-mannosyl-transferase TMTC4 (EC 2.4.1.109) (Transmembrane O-mannosyltransferase targeting cadherins 4) (Transmembrane and tetratricopeptide repeat-containing 4) (Q5T4D3)
Organism: Homo sapiens (Human)
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000305}.
Interaction partners:
Sequence:
MAVLDTDLDHILPSSVLPPFWAKLVVGSVAIVCFARSYDGDFVFDDSEAIVNNKDLQAETPLGDLWHHDFWGSRLSSNTSHKSYRPLTVLTFRINYYLSGGFHPVGFHVVNILLHSGISVLMVDVFSVLFGGLQYTSKGRRLHLAPRASLLAALLFAVHPVHTECVAGVVGRADLLCALFFLLSFLGYCKAFRESNKEGAHSSTFWVLLSIFLGAVAMLCKEQGITVLGLNAVFDILVIGKFNVLEIVQKVLHKDKSLENLGMLRNGGLLFRMTLLTSGGAGMLYVRWRIMGTGPPAFTEVDNPASFADSMLVRAVNYNYYYSLNAWLLLCPWWLCFDWSMGCIPLIKSISDWRVIALAALWFCLIGLICQALCSEDGHKRRILTLGLGFLVIPFLPASNLFFRVGFVVAERVLYLPSVGYCVLLTFGFGALSKHTKKKKLIAAVVLGILFINTLRCVLRSGEWRSEEQLFRSALSVCPLNAKVHYNIGKNLADKGNQTAAIRYYREAVRLNPKYVHAMNNLGNILKERNELQEAEELLSLAVQIQPDFAAAWMNLGIVQNSLKRFEAAEQSYRTAIKHRRKYPDCYYNLGRLYADLNRHVDALNAWRNATVLKPEHSLAWNNMIILLDNTGNLAQAEAVGREALELIPNDHSLMFSLANVLGKSQKYKESEALFLKAIKANPNAASYHGNLAVLYHRWGHLDLAKKHYEISLQLDPTASGTKENYGLLRRKLELMQKKAV
Protein: Large ribosomal subunit protein bL34m (Probable 54S ribosomal protein L34, mitochondrial) (L34mt) (Q9P7L9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein mL43
- Small ribosomal subunit protein uS15m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL30m
- Large ribosomal subunit protein bL17m
Sequence:
MMFMQQFRNLLHPAMKGARNISILAGGGTMRGFPTRNPFNTATLYSSLPTMNIFGQMQQVRWKTYGNEYQPSNRKRKRKHGFLSRIRSVNGRRVLRDRRQKGRMYLSH
Protein: Sarcomere length short, isoform A (Q9VGN5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMKEVESGKKLRHVACNDRSQPILTCKSITKLDDKFIYETEKGNSHNKLLKQIQGGIKLKPTKTNDRSKPVLDGLRKFRRQMTIEEQLQKSQSKINMLSEAPSSHALGPGSATALGAGGSRPSIVSAMSIDEESPDELDDIDKIRDDLQSTKQMLALELRNREAQDRENKKLLAKIRTLETELEREKSREKNLEYGSNVIVATMDPTPTAEQTYVNSLKREVEDARKVSKEVEQNYQSTAEQLVEAKTEIEEQRRQIQLLERKLAAALQATPSTNRPHISNCFAYDDDDYDDCFHYDHYHAARHQGGGSLDGSRRPSDANFGRDSSPELEPEVSESDPDEPEEKKVERRERRSGKELKILRSKLTKLKVKEEAAKKEKDALKQAMKKNQSILKEENKKFKKLEKEVQKMAASMKLDEDDVDGEEKDEDEEEAEEEHASEEEEESDDESEESESEESEAETGSESEPEDSPNSAKKANVEPRVKKHESRFAAMKKCNVLLQANVDNLQDQIVQVRSRATNLQDELDAVIADLGF
Protein: Serine/threonine-protein kinase 52 (EC 2.7.11.1) (Protein CONVERGENCE OF BLUE LIGHT AND CO2 2) (Q9FGB1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:29101334, ECO:0000269|PubMed:31904040}.
Interaction partners:
Sequence:
MKEGKDGFVRADQIDLKSLDEQLERHLSRALTLEKNKKKDEEDTTAVAIGGSASSSPVTLNGGGFVGKRKQRLEWEIDPSKLIIKTVLARGTFGTVHRGIYDGQDVAVKLLDWGEEGHRSEAEIVSLRADFAQEVAVWHKLDHPNVTKFIGATMGASGLQLQTESGPLAMPNNICCVVVEYLPGGALKSYLIKNRRRKLTFKIVVQLALDLARGLSYLHSQKIVHRDVKTENMLLDKTRTVKIADFGVARVEASNPNDMTGETGTLGYMAPEVLNGNPYNRKCDVYSFGICLWEIYCCDMPYPDLTFSEVTSAVVRQNLRPDIPRCCPSALAAVMKRCWDANPDKRPEMDEVVPMLESIDTTKGGGMIPNDQQQGCLCFRRKRGP
Protein: Tetratricopeptide repeat domain 9C (Tetratricopeptide repeat protein 9C) (Zgc:56497) (Q7ZUI3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Acid sphingomyelinase-like phosphodiesterase.
- Tetratricopeptide repeat domain 4.
- von Willebrand factor D and EGF domain-containing protein precursor
- Tetratricopeptide repeat protein 39C
- DnaJ homolog subfamily C member 7
- Intraflagellar transport protein 56
- Outer dynein arm-docking complex subunit 4
- Zinc finger MYND domain-containing protein 10
- Axonemal dynein light intermediate polypeptide 1
- Coiled-coil domain-containing protein 39
Sequence:
MDEKVADPPAGDDGSSCLGAAGGSSASRLDSQLQEAVRLKTEGNAFYRGRNVRSAIGRYHRALLVLRSLDSEVNSVMQGFGAPVPKLNQEQDELLRSTQIDCYNNLAACLLQRELVDYTRVLEYSLKVLHWRPADTKALYRAGVASLELGDAPAARQYLTQASRGKPNDADVKKQLQRVEERLSQDYQKEKALYKGMFSKQKQAEEQIAEEKTRELV
Protein: Ribonuclease P protein subunit p30 (RNaseP protein p30) (RNase P subunit 2) (P78346)
Organism: Homo sapiens (Human)
Function: Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences.
Subcellular location: Nucleus, nucleolus {ECO:0000305}.
Interaction partners:
- Ribonuclease P protein subunit p29
- Ribonuclease P protein subunit p21
- Ribonuclease P protein subunit p20
- Ribonuclease P protein subunit p38
- Ribonuclease P protein subunit p40
- Ribonuclease P protein subunit p14
- Ribonucleases P/MRP protein subunit POP1
- Ribonuclease P/MRP protein subunit POP5
- Ribonuclease P protein subunit p25
- Ribonuclease P protein subunit p25-like protein
Sequence:
MAVFADLDLRAGSDLKALRGLVETAAHLGYSVVAINHIVDFKEKKQEIEKPVAVSELFTTLPIVQGKSRPIKILTRLTIIVSDPSHCNVLRATSSRARLYDVVAVFPKTEKLFHIACTHLDVDLVCITVTEKLPFYFKRPPINVAIDRGLAFELVYSPAIKDSTMRRYTISSALNLMQICKGKNVIISSAAERPLEIRGPYDVANLGLLFGLSESDAKAAVSTNCRAALLHGETRKTAFGIISTVKKPRPSEGDEDCLPASKKAKCEG
Protein: Gag polyprotein (Pr55Gag) [Cleaved into: Matrix protein p17 (MA); Capsid protein p24 (CA); Spacer peptide 1 (SP1) (p2); Nucleocapsid protein p7 (NC); Spacer peptide 2 (SP2) (p1); p6-gag] (P05888)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate MN) (HIV-1)
Function: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with the RNA packaging sequence (Psi).
Subcellular location: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion assembly. {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Matrix protein p17]: Virion membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host nucleus {ECO:0000250}. Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Capsid protein p24]: Virion {ECO:0000250|UniProtKB:P12493}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p7]: Virion {ECO:0000250|UniProtKB:P12493}.
Interaction partners:
Sequence:
MGARASVLSGGELDRWEKIRLRPGGKKKYKLKHVVWASRELERFAINPGLLETSEGCRQILGQLQPSLQTGSEERKSLYNTVATLYCVHQKIKIKDTKEALEKIEEEQNKSKKKAQQAAADTGNRGNSSQVSQNYPIVQNIQGQMVHQAISPRTLNAWVKVVEEKAFSPEVIPMFSALSEGATPQDLNTMLNTVGGHQAAMQMLKETINEEAAEWDRLHPAHAGPIAPGQMREPRGSDIAGTTSTLQEQIGWMTNNPPIPVGEIYKRWIILGLNKIVRMYSPSSILDIRQGPKEPFRDYVDRFYKTLRAEQASQEVKNWMTETLLVQNANPDCKTILKALGPAATLEEMMTACQGVGGPGHKARVLAEAMSQVTNSATIMMQRGNFRNQRKIIKCFNCGKEGHIAKNCRAPRKRGCWKCGKEGHQMKDCTERQANFLGKIWPSCKGRPGNFPQSRTEPTAPPEESFRFGEETTTPYQKQEKKQETIDKDLYPLASLKSLFGNDPLSQ
Protein: ARF guanine-nucleotide exchange factor 1 (P47102)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Activates the ARF proteins by exchanging bound GDP for free GTP. Plays a role in maintaining mitochondrial morphology, and in the turnover of mitochondria through mitophagy.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P39993}. Membrane {ECO:0000250|UniProtKB:P39993}; Peripheral membrane protein {ECO:0000250|UniProtKB:P39993}. Endoplasmic reticulum {ECO:0000269|PubMed:25190516}. Mitochondrion {ECO:0000269|PubMed:25190516}. Note=Soluble and partially membrane-bound. {ECO:0000250|UniProtKB:P39993}.
Interaction partners:
- ADP-ribosylation factor 1
- Coatomer subunit gamma
- ADP-ribosylation factor 2
- ARF guanine-nucleotide exchange factor 2
- ADP-ribosylation factor-like protein 1
- ADP-ribosylation factor 3
- Protein GMH1
- ADP-ribosylation factor guanine nucleotide-exchange factor SEC7
- ADP-ribosylation factor GTPase-activating protein GLO3
- ADP-ribosylation factor GTPase-activating protein GCS1
Sequence:
MHDVPMETVLAVNPATMIVKECINLCSAMNKQSRDKSQTSVAALLGGGSDIFLSQSDSFVDSFHNLPTSSYHDPLISGLVQLRLKINDLKGLDSLNALELLKPFLEIVSASSVSGYTTSLALDSLQKVFTLKIINKTFNDIQIAVRETVVALTHCRFEASKQISDDSVLLKVVTLLRDIITSSFGDYLSDTIIYDVLQTTLSLACNTQRSEVLRKTAEVTIAGITVKLFTKLKLLDPPTKTEKYINDESYTDNNLKDDIIGTTTSDNDLSSTDDDSAVADDNKNEKPVQQVIREQENDEETAEKAENVEPNYGITVIKDYLGLLLSLVMPENRMKHTTSAMKLSLQLINAAIEISGDKFPLYPRLFSLISDPIFKSVLFIIQSSTQYSLLQATLQLFTSLVVILGDYLPMQIELTLRRIFEILEDTTISGDVSKQKPPAIRELIIEQLSILWIHSPAFFLQLFVNFDCNLDRSDLSIDFIKELTKFSLPAAAVNTSNNIPPICLEGVLSLIENIYNDLQRFDRAEFVKNQKEIDILKQRDRKTEFILCVETFNEKAKKGIQMLIEKGFIDSDSNRDIASFLFLNNGRLNKKTIGLLLCDPKKTSLLKEFIDLFDFKGLRVDEAIRILLTKFRLPGESQQIERIVEAFSSKYSADQSNDKVELEDKKAGKNGSESMTEDDIIHVQPDADSVFVLSYSIIMLNTDSHNPQVKDHMTFDDYSNNLRGCYNGKDFPRWYLHKIYTSIKVKEIVMPEEHHGNERWFEDAWNNLISSTSVMTEMQRDFTNPISKLAQIDILQYEKAIFSNVRDIILKTLFKIFTVASSDQISLRILDAISKCTFINYYFSFDQSYNDTVLHLGEMTTLAQSSAKAVELDVDSIPLVEIFVEDTGSKISVSNQSIRLGQNFKAQLCTVLYFQIIKEISDPSIVSTRLWNQIVQLILKLFENLLMEPNLPFFTNFHSLLKLPELPLPDPDISIRKAKMSRSLLSTFASYLKGDEEPSEEDIDFSIKAFECVKASHPLSSVFENNQLVSPKMIETLLSSLVIEKTSENSPYFEQELLFLLEISIILISEASYGQEFGALIADHMINISNLDGLSKEAIARLASYKMFLVSRFDNPRDILSDLIEHDFLVKNEIFNTKYYESEWGKQVINDLFTHLNDVKYNERALKNVKFWNFLRILISAKDRQFAVYTFLEKYIQNGDIFVDDGNFMNILSLLDEMSCAGAVGTKWEQNYENSVEDGCEAPESNPYRSIIDLSSRSINITADLLSTVGRSNSALNKNEIIAAIQGLAHQCLNPCDELGMQALQALENILLSRASQLRTEKVAVDNLLETGLLPIFELDEIQDVKMKRITSILSVLSKIFLGQLVEGVTSNETFLRVLNVFNKYVDDPTVERQLQELIISKREIEKE
Protein: Tyrosine-protein phosphatase 2 (EC 3.1.3.48) (Protein-tyrosine-phosphate phosphohydrolase 2) (PTPA) (P34138)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Extracellular signal-regulated kinase 1
- Probable serine/threonine-protein kinase roco5
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco6
- Probable serine/threonine-protein kinase roco11
Sequence:
MDESFDAFEIKPNSSIIEHFNNHPTCIDKEFNFILQKTELRALETDKFRSALEAKNKLKNRYSNVLPFEETRVKINIDDDDDDEDDNEDDIIVSNNNNNNNNNEKRIKRNSIGSSGQSDVMSNSSDEEDHGGSGDEGTTLSDYINASFINNGTYICTQGPLLNTIVDFWKMIWEQNSNIIVMLTREEENFKTKCDKYWPDKDEERYGNFIVKFDNNITIPDILIRREFTLENLKDNKTRKIYHFQYTTWPDHGTPVSTTGFLKFVSFVDHEKRSGPIVVHCSAGIGRSGTFVAIHSIVAKFAKHYDEKKQAPSINLPKLVVEMRNERPGMVQTRDQYRFCYLAISEAMNTVLKKEQKKRKGLSYSYSSIPLTGPEHD
Protein: Membrane-associated progesterone receptor component 2 (Progesterone membrane-binding protein) (Steroid receptor protein DG6) (O15173)
Organism: Homo sapiens (Human)
Function: Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (By similarity). May serve as a universal non-classical progesterone receptor in the uterus (Probable). Intracellular heme chaperone required for delivery of labile, or signaling heme, to the nucleus (By similarity). Plays a role in adipocyte function and systemic glucose homeostasis. In brown fat, which has a high demand for heme, delivery of labile heme in the nucleus regulates the activity of heme-responsive transcriptional repressors such as NR1D1 and BACH1 (By similarity).
Subcellular location: Membrane {ECO:0000305|PubMed:23793472}; Single-pass membrane protein {ECO:0000305}. Nucleus envelope {ECO:0000269|PubMed:27754849, ECO:0000269|PubMed:28111073}. Endoplasmic reticulum {ECO:0000269|PubMed:27754849}. Secreted {ECO:0000269|PubMed:37453717}.
Interaction partners:
- Progesterone receptor
- Membrane progestin receptor beta
- Membrane progestin receptor alpha
- Membrane progestin receptor gamma
- Aladin
- Cytochrome b5 type B
Sequence:
MAAGDGDVKLGTLGSGSESSNDGGSESPGDAGAAAEGGGWAAAALALLTGGGEMLLNVALVALVLLGAYRLWVRWGRRGLGAGAGAGEESPATSLPRMKKRDFSLEQLRQYDGSRNPRILLAVNGKVFDVTKGSKFYGPAGPYGIFAGRDASRGLATFCLDKDALRDEYDDLSDLNAVQMESVREWEMQFKEKYDYVGRLLKPGEEPSEYTDEEDTKDHNKQD
Protein: BBSome complex assembly protein BBS10 (Bardet-Biedl syndrome 10 protein) (Q8TAM1)
Organism: Homo sapiens (Human)
Function: Probable molecular chaperone that assists the folding of proteins upon ATP hydrolysis. Plays a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Involved in adipogenic differentiation.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:19190184}. Note=Located within the basal body of the primary cilium of differentiating preadipocytes. {ECO:0000269|PubMed:19190184}.
Interaction partners:
- Chaperonin-containing T-complex member BBS12
- BBSome complex member BBS7
- T-complex protein 1 subunit beta
- BBSome complex member BBS2
- T-complex protein 1 subunit epsilon
- BBSome complex member BBS1
- BBSome complex member BBS5
- Protein PTHB1
- BBSome complex member BBS4
- T-complex protein 1 subunit gamma
Sequence:
MLSSMAAAGSVKAALQVAEVLEAIVSCCVGPEGRQVLCTKPTGEVLLSRNGGRLLEALHLEHPIARMIVDCVSSHLKKTGDGAKTFIIFLCHLLRGLHAITDREKDPLMCENIQTHGRHWKNCSRWKFISQALLTFQTQILDGIMDQYLSRHFLSIFSSAKERTLCRSSLELLLEAYFCGRVGRNNHKFISQLMCDYFFKCMTCKSGIGVFELVDDHFVELNVGVTGLPVSDSRIIAGLVLQKDFSVYRPADGDMRMVIVTETIQPLFSTSGSEFILNSEAQFQTSQFWIMEKTKAIMKHLHSQNVKLLISSVKQPDLVSYYAGVNGISVVECLSSEEVSLIRRIIGLSPFVPPQAFSQCEIPNTALVKFCKPLILRSKRYVHLGLISTCAFIPHSIVLCGPVHGLIEQHEDALHGALKMLRQLFKDLDLNYMTQTNDQNGTSSLFIYKNSGESYQAPDPGNGSIQRPYQDTVAENKDALEKTQTYLKVHSNLVIPDVELETYIPYSTPTLTPTDTFQTVETLTCLSLERNRLTDYYEPLLKNNSTAYSTRGNRIEISYENLQVTNITRKGSMLPVSCKLPNMGTSQSYLSSSMPAGCVLPVGGNFEILLHYYLLNYAKKCHQSEETMVSMIIANALLGIPKVLYKSKTGKYSFPHTYIRAVHALQTNQPLVSSQTGLESVMGKYQLLTSVLQCLTKILTIDMVITVKRHPQKVHNQDSEDEL
Protein: Splicing factor ESS-2 (ES2 similar protein 2) (P34420)
Organism: Caenorhabditis elegans
Function: Regulates pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000269|PubMed:25194163}.
Interaction partners:
Sequence:
MSSFDKNDERAQLMVPKSINEGKVVKLSQKTLVTKKIERQVVPEEKYIAGLDKIIEKDYFPHLKKMQAQKEYLEAVANKDINKIKELQMKFCSTGSVRTDRSFRTPITTRSTTEAPDVSSFDADTPGPSSASTSSAHDWMQSPMPFANEEGDNEALNRKRKKKKEETLTSYLNKYTSEDNASFEELAKVMREREDARRPWVYKAEEEHNKNLVTRQAIAAEADVQLALKHAVDADDNRPLNVDNWAYKAWNTVLFNPDGAALTPAEIADAARKQQTEINKRGTRFPDSGKLKPSDEAMTRAAVSHALANAGKVDFLGNEVTPANSFKLLETPNPNPDDMDSPLMTWGEIDGTPFRLDAPDVTEHSLPGAAPVFKIPEVPYREKIAQSMNDSIAAKYRDKRKVAMRAAEGAHFSRTPGFGSKRVSDKLAQLSPAAQKLATKKLGLKMLPAHKSPFASPKIMSNWSRPSSSKRSTTPGSAWSRGSTTPGSSWSQGAQTPGTPGIESMIRRKGDNVGPSTSAGAADRANAGDFF
Protein: Tribbles homolog 3 (TRB-3) (Neuronal cell death-inducible putative kinase) (SINK) (p65-interacting inhibitor of NF-kappa-B) (Q96RU7)
Organism: Homo sapiens (Human)
Function: Inactive protein kinase which acts as a regulator of the integrated stress response (ISR), a process for adaptation to various stress. Inhibits the transcriptional activity of DDIT3/CHOP and is involved in DDIT3/CHOP-dependent cell death during ER stress. May play a role in programmed neuronal cell death but does not appear to affect non-neuronal cells. Acts as a negative feedback regulator of the ATF4-dependent transcription during the ISR: while TRIB3 expression is promoted by ATF4, TRIB3 protein interacts with ATF4 and inhibits ATF4 transcription activity (By similarity). Disrupts insulin signaling by binding directly to Akt kinases and blocking their activation (By similarity). May bind directly to and mask the 'Thr-308' phosphorylation site in AKT1 (By similarity). Interacts with the NF-kappa-B transactivator p65 RELA and inhibits its phosphorylation and thus its transcriptional activation activity. Interacts with MAPK kinases and regulates activation of MAP kinases. Can inhibit APOBEC3A editing of nuclear DNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:22977230}.
Interaction partners:
- RAC-alpha serine/threonine-protein kinase
- Cyclic AMP-dependent transcription factor ATF-4
- Glutathione-specific gamma-glutamylcyclotransferase 1
- RAC-beta serine/threonine-protein kinase
- RIB43A-like with coiled-coils protein 2
- DNA damage-inducible transcript 3 protein
- Peroxisome proliferator-activated receptor alpha
- RAC-gamma serine/threonine-protein kinase
- E3 ubiquitin-protein ligase COP1
- Asparagine synthetase
Sequence:
MRATPLAAPAGSLSRKKRLELDDNLDTERPVQKRARSGPQPRLPPCLLPLSPPTAPDRATAVATASRLGPYVLLEPEEGGRAYQALHCPTGTEYTCKVYPVQEALAVLEPYARLPPHKHVARPTEVLAGTQLLYAFFTRTHGDMHSLVRSRHRIPEPEAAVLFRQMATALAHCHQHGLVLRDLKLCRFVFADRERKKLVLENLEDSCVLTGPDDSLWDKHACPAYVGPEILSSRASYSGKAADVWSLGVALFTMLAGHYPFQDSEPVLLFGKIRRGAYALPAGLSAPARCLVRCLLRREPAERLTATGILLHPWLRQDPMPLAPTRSHLWEAAQVVPDGLGLDEAREEEGDREVVLYG
Protein: Grainyhead-like 2b protein (Grainyhead-like protein 2 homolog isoform X1) (Grainyhead-like transcription factor 2b) (F7VJQ5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU01313}.
Interaction partners:
Sequence:
MSQETDSKRLVVVVPNEPSFHQRRPYTSEDEAWRSYLENPLTAATKAMMSINGDEDSAAALGLLYEYYKVPKDKRVPISKVVEMSDEPEKRSTPVGNSSQMEPETVDNHVQVLKSVPVNLSLNTDHQDNKREQYSVPAGESGTAAVVKAEAHTAVFMTSGGHYRTEGEEQMRVICEQTHSFDTSTINHSAYGKDDHRSSPESTYEDDSNEKYRSSSIGPDDFIFDQSHMLDTFQYTLEASKSLRQKQGEGPMTYLNKGQFYAITLSETSANKRLRHPISKVRSVVMVVFSEDKNRDEQLKYWKYWHSRQHTAKQRVLDIADYKESFNTIGNIEEIAYNAVSFTWDLNEEAKIFITVNCLSTDFSSQKGVKGLPLMIQIDTYSYNNRSNKPLHRAYCQIKVFCDKGAERKIRDEERKQNRKKTKGKDGGSGTVTVPKKCDSTLFKTMTDLDAQPVLFIPDVHFGNLQRAGQVFAFNTEEIECEGSVLVKRMFRSSEEDFCPPPHKQLREDTQKRVLLYVRKESDEVFDALMLRSPTVRGLMDAISEKYGVPIDRMAKIYKKSKKGILVNMDDNIIEHYSNEDTFILNIESYADAYKITLTEI
Protein: Cation/H+ exchanger transmembrane domain-containing protein (Q387G6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVDHISLCVLFASPLSFPLSNLFLFIFAFYSRELSSWKRRRVMAKHPGEGEGEQQRLSMGAKRSTHAQSPSQPPDATAAPIEILDASKPLPGDSSDCRPGSSETIIVFPPPSIFKRVGSTQRPLRGDTKPHASGTAVSFDEKTTSREPISHQTKVNPPPSINVHRVPTGGQPVPAGPRQVNEVPPKMDDDAADTASTPEPDDEHLRSLTVDVMSPIISEEGEAKGTVTCPVDAICEQVDNLSSDGDKADIAFVLYSQYLKDYERKPSFTADTWDEIKYVGDSGRRFGVLYDEERGAVQLILFGKCYRIFILSFLLRFICLILFWAVMYMLASRSKFSPGGLYFDTLCTILFAGVVGSIISRVTRVPSVACAVLAAALYNNIPPTGSLTAGTSLDMRGVISLFGLTVGMIRGGLALNLRALKANFFRYLCFSVVPMVAEAFAHGFLAKILFRYPTTTWALLHGFIVTANAPGIIIPALIELQRKGYGTRGGPGVMILISVSVEATFCVWTIQLLLAIQFNTMGLLLAGLLGPIQIIVGLVVGVGLGYAFYFVVFDILYKEGQRVPLRESTILYATQRHLSHVRLTSCFIVMLVSMVCTSVGRMVSCIGGAAVIIVTMLALFSHWCDVASKMEHLTAKGDVLVFFRVLWDYVAMPALFAMAGASVNFSEVFSGDFFAPGIACVLAGLVVRCLSSMITPLLLRMPFTWRELVFCGIGSLGKGPMQAAFGAVPLMFLQTMGANSGNSTGTADDFSADDDIKHAQTLKNSAVLSMLVACPLCSILLGVLAQKLLRRDAPSVPAAAK
Protein: NADH dehydrogenase [ubiquinone] 1 subunit C2 (E9PM14)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004298}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004298}; Matrix side {ECO:0000256|ARBA:ARBA00004298}.
Interaction partners:
Sequence:
MIARRNPEPLRFLPDEARSLPPPKLTDPRLLYIGFLGYCSGLIDNLIRRRPIATAGLHRQLLYITAFFFAGYYLVKREDYLYAVRDREMFGYMKLHPEDFPEEGISS