wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 2 subunit 1 (Eukaryotic translation initiation factor 2 subunit alpha) (eIF-2-alpha) (eIF-2A) (eIF-2alpha) (eIF2-alpha) (Q6ZWX6)
Organism: Mus musculus (Mouse)
Function: Functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B. EIF2S1/eIF-2-alpha is a key component of the integrated stress response (ISR), required for adaptation to various stress: phosphorylation by metabolic-stress sensing protein kinases (EIF2AK1/HRI, EIF2AK2/PKR, EIF2AK3/PERK and EIF2AK4/GCN2) in response to stress converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, leading to a attenuation of cap-dependent translation, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activators ATF4 and QRICH1, and hence allowing ATF4- and QRICH1-mediated reprogramming.
Subcellular location: Cytoplasm, Stress granule {ECO:0000269|PubMed:19861488}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P56286}. Mitochondrion {ECO:0000250|UniProtKB:P05198}. Note=Colocalizes with NANOS3 in the stress granules (PubMed:19861488). Relocalizes to the surface of mitochondria in response to mitochondrial damage and phosphorylation by EIF2AK1/HRI (By similarity). {ECO:0000250|UniProtKB:P05198, ECO:0000269|PubMed:19861488}.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit 2
- Small ribosomal subunit protein uS3
- Translation initiation factor eIF2B subunit beta
- Translation initiation factor eIF2B subunit gamma
- Eukaryotic translation initiation factor 5
- Translation initiation factor eIF2B subunit delta
- Translation initiation factor eIF2B subunit alpha
- Eukaryotic translation initiation factor 3 subunit A
- Translation initiation factor eIF2B subunit epsilon
- Small ribosomal subunit protein uS5
Sequence:
MPGLSCRFYQHKFPEVEDVVMVNVRSIAEMGAYVSLLEYNNIEGMILLSELSRRRIRSINKLIRIGRNECVVVIRVDKEKGYIDLSKRRVSPEEAIKCEDKFTKSKTVYSILRHVAEVLEYTKDEQLESLFQRTAWVFDDKYKRPGYGAYDAFKHAVSDPSILDSLDLNEDEREVLINNINRRLTPQAVKIRADIEVACYGYEGIDAVKEALRAGLNCSTETMPIKINLIAPPRYVMTTTTLERTEGLSVLNQAMAVIKEKIEEKRGVFNVQMEPKVVTDTDETELARQLERLERENAEVDGDDDAEEMEAKAED
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (Q8IQ26)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNSVIQCLSHTQELTRFLRSHHGSRSLSTKDQQILHEFAKLIQEMWTANVHTVTPMELKRAFSTKHRMYSDYNQQDAQEFLRFFLDSLHSALNSGVKGETLNIDDNLSDNKKADLTWEWYTRHENSLVRDLFVGQLKSTLKCTTCGNTSVTFDPFWDLSVPLPSSSRCKLEACLDLFIREEVLDGDEMPTCAKCKTRRKCTKSFTIQRFPKYLVIHLKRFSETRWSKLSNIVEFPTSDSELNMGSYGANSNSNVHYSLYAISNHMGSTAGGHYVALCKHPVSRKWHEFNDNIVSDALSENHLVSSSAYILFYERT
Protein: Transmembrane protein 179B (Q7Z7N9)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Transcription initiation protein SPT3 homolog
- Transcription factor SPT20 homolog
- Transcription initiation factor TFIID subunit 12
- SAGA-associated factor 29
- Transcriptional adapter 3
- Transformation/transcription domain-associated protein
Sequence:
MALSWLQRVELALFAAAFLCGAVAAAAMTRTQGSFSGRCPLYGVATLNGSSLALSRPSAPSLCYFVAGASGLLALYCLLLLLFWIYSSCIEDSHRGAIGLRIALAISAIAVFLVLVSACILRFGTRSLCNSIISLNTTISCSEAQKIPWTPPGTALQFYSNLHNAETSSWVNLVLWCVVLVLQVVQWKSEATPYRPLERGDPEWSSETDALVGSRLSHS
Protein: Urea transporter 1 (Solute carrier family 14 member 1) (Urea transporter B) (UT-B) (Urea transporter, erythrocyte) (P97689)
Organism: Rattus norvegicus (Rat)
Function: Mediates the transport of urea driven by a concentration gradient across the cell membrane. Mediates the transport of urea across the cell membranes of erythrocytes and the renal inner medullary collecting duct which is critical to the urinary concentrating mechanism (By similarity). Facilitates water transport in erythrocytes (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8VHL0}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8VHL0}; Multi-pass membrane protein {ECO:0000255}. Note=Restricted to the basolateral membrane in various portions of the urothelium. {ECO:0000250|UniProtKB:Q8VHL0}.
Interaction partners:
Sequence:
MEDIPTMVKVDRGESQILSCRGRRCGLKVLGYVTGDMKEFANWLKDKPVVLQFMDWILRGISQVVFVSNPISGILILAGLLVQNPWWALCGCVGTVVSTLTALLLSQDRSAIAAGLQGYNATLVGILMAVFSDKGDYFWWLIFPVSAMSMTCPVFSSALSSLFSKWDLPVFTLPFNMALSLYLSATGHYNTFFPSKLFMPVSSVPNITWSELSALELLKSLPVGVGQIYGCDNPWTGAIFLCAILLSSPLMCLHAAIGSLLGVIAGLSLAAPFKDIYSGLWGFNSSLACIAIGGMFMALTWQTHLLALACALFTAYFGACMTHLMAAVHLPACTWSFCLATLLFLLLTTENPNIYRMPLSKVTYSEENRIFYLQNKKRVVDSPL
Protein: C4H2-type domain-containing protein (Q65ZB3)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MISRTKVDDYFAKRNELLEELSELENTEKFIKETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDRESKIVKRYEALLKLIESTNEKLKETGCDIALSQDDLPQTHLKIEPPAAPVTPVLSGGLPSPFPNFNFRNLFQPMLLEQLGSFSTNSPTPQFRPPPHMAAAMQHHQLKVTDHQSPPMKVVKNFL
Protein: A-type potassium channel modulatory protein KCNIP2 (Cardiac voltage-gated potassium channel modulatory subunit) (Kv channel-interacting protein 2) (KChIP2) (Potassium channel-interacting protein 2) (Q9NS61)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels. Modulates channel density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3 trafficking to the cell surface. May be required for the expression of I(To) currents in the heart (By similarity).
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:Q9JM59}; Lipid-anchor {ECO:0000250|UniProtKB:Q9JM59}. Note=Detected on lipid rafts (By similarity). {ECO:0000250|UniProtKB:Q9JM59}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000250|UniProtKB:Q9JM59}; Lipid-anchor {ECO:0000250|UniProtKB:Q9JM59}.; SUBCELLULAR LOCATION: [Isoform 6]: Cell membrane {ECO:0000250|UniProtKB:Q9JM59}; Lipid-anchor {ECO:0000250|UniProtKB:Q9JM59}.
Interaction partners:
- A-type voltage-gated potassium channel KCND2
- A-type voltage-gated potassium channel KCND3
- Voltage-gated potassium channel KCNC1
- A-type potassium channel modulatory protein KCNIP1
- Potassium voltage-gated channel subfamily A member 4
- Kv channel-interacting protein 4
- A-type voltage-gated potassium channel KCND1
- Potassium voltage-gated channel subfamily A member 5
- A-type potassium channel modulatory protein DPP6
- Serine/threonine-protein kinase Kist
Sequence:
MRGQGRKESLSDSRDLDGSYDQLTGHPPGPTKKALKQRFLKLLPCCGPQALPSVSETLAAPASLRPHRPRLLDPDSVDDEFELSTVCHRPEGLEQLQEQTKFTRKELQVLYRGFKNECPSGIVNEENFKQIYSQFFPQGDSSTYATFLFNAFDTNHDGSVSFEDFVAGLSVILRGTVDDRLNWAFNLYDLNKDGCITKEEMLDIMKSIYDMMGKYTYPALREEAPREHVESFFQKMDRNKDGVVTIEEFIESCQKDENIMRSMQLFDNVI
Protein: Pre T-cell antigen receptor alpha (pT-alpha) (pTa) (pT-alpha-TCR) (Q6ISU1)
Organism: Homo sapiens (Human)
Function: The pre-T-cell receptor complex (composed of PTCRA, TCRB and the CD3 complex) regulates early T-cell development.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:38422122}.
Interaction partners:
- DNA-binding protein Ikaros
- Neurogenic locus notch homolog protein 3
- T-cell surface glycoprotein CD3 gamma chain
Sequence:
MAGTWLLLLLALGCPALPTGVGGTPFPSLAPPIMLLVDGKQQMVVVCLVLDVAPPGLDSPIWFSAGNGSALDAFTYGPSPATDGTWTNLAHLSLPSEELASWEPLVCHTGPGAEGHSRSTQPMHLSGEASTARTCPQEPLRGTPGGALWLGVLRLLLFKLLLFDLLLTCSCLCDPAGPLPSPATTTRLRALGSHRLHPATETGGREATSSPRPQPRDRRWGDTPPGRKPGSPVWGEGSYLSSYPTCPAQAWCSRSALRAPSSSLGAFFAGDLPPPLQAGAA
Protein: Cycloartenol synthase (AtCYC) (EC 5.4.99.8) (2,3-epoxysqualene--cycloartenol cyclase) (P38605)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts oxidosqualene to cycloartenol and 1% parkeol. Involved in plastid biogenesis. Essential for the male gametophyte function.
Interaction partners:
- Cycloartenol-C-24-methyltransferase
- Squalene epoxidase 1
- Squalene epoxidase 2, mitochondrial
- Squalene epoxidase 3
- Squalene epoxidase 5
- Squalene epoxidase 6
- Squalene epoxidase 4
- Sterol 14-demethylase
- Cycloeucalenol cycloisomerase
- Ergosterol biosynthetic protein 28
Sequence:
MWKLKIAEGGSPWLRTTNNHVGRQFWEFDPNLGTPEDLAAVEEARKSFSDNRFVQKHSADLLMRLQFSRENLISPVLPQVKIEDTDDVTEEMVETTLKRGLDFYSTIQAHDGHWPGDYGGPMFLLPGLIITLSITGALNTVLSEQHKQEMRRYLYNHQNEDGGWGLHIEGPSTMFGSVLNYVTLRLLGEGPNDGDGDMEKGRDWILNHGGATNITSWGKMWLSVLGAFEWSGNNPLPPEIWLLPYFLPIHPGRMWCHCRMVYLPMSYLYGKRFVGPITSTVLSLRKELFTVPYHEVNWNEARNLCAKEDLYYPHPLVQDILWASLHKIVEPVLMRWPGANLREKAIRTAIEHIHYEDENTRYICIGPVNKVLNMLCCWVEDPNSEAFKLHLPRIHDFLWLAEDGMKMQGYNGSQLWDTGFAIQAILATNLVEEYGPVLEKAHSFVKNSQVLEDCPGDLNYWYRHISKGAWPFSTADHGWPISDCTAEGLKAALLLSKVPKAIVGEPIDAKRLYEAVNVIISLQNADGGLATYELTRSYPWLELINPAETFGDIVIDYPYVECTSAAIQALISFRKLYPGHRKKEVDECIEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTLKNSPHVAKACEFLLSKQQPSGGWGESYLSCQDKVYSNLDGNRSHVVNTAWAMLALIGAGQAEVDRKPLHRAARYLINAQMENGDFPQQEIMGVFNRNCMITYAAYRNIFPIWALGEYRCQVLLQQGE
Protein: Cytosolic carboxypeptidase 6 (EC 3.4.17.24) (ATP/GTP-binding protein-like 4) (Protein deglutamylase CCP6) (Q5VU57)
Organism: Homo sapiens (Human)
Function: Metallocarboxypeptidase that mediates protein deglutamylation of tubulin and non-tubulin target proteins. Catalyzes the removal of polyglutamate side chains present on the gamma-carboxyl group of glutamate residues within the C-terminal tail of tubulin protein. Specifically cleaves tubulin long-side-chains, while it is not able to remove the branching point glutamate. Also catalyzes the removal of polyglutamate residues from the carboxy-terminus of non-tubulin proteins such as MYLK. Mediates the deglutamylation of nucleotidyltransferase CGAS, leading to CGAS antiviral defense response activation (By similarity). Involved in KLF4 deglutamylation which promotes KLF4 proteasome-mediated degradation, thereby negatively regulating cell pluripotency maintenance and embryogenesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q09LZ8}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23085998}. Golgi apparatus {ECO:0000269|PubMed:23085998}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:23085998}. Note=Colocalizes with gamma-tubulin in the centrioles at interphase and dividing cells and with glutamylated tubulin in basal bodies of ciliated cells. {ECO:0000269|PubMed:23085998}.
Interaction partners:
- BEN domain-containing protein 5
- Tubulin monoglutamylase TTLL4
- Tubulin polyglutamylase TTLL6
Sequence:
MAEGSQSAPEAGNDMGNDDAIGGNVSKYIVLPTGYCGQPKKGHLIFDACFESGNLGRVDQVSEFEYDLFIRPDTCNPRFRVWFNFTVENVKESQRVIFNIVNFSKTKSLYRDGMAPMVKSTSRPKWQRLPPKNVYYYRCPDHRKNYVMSFAFCFDREEDIYQFAYCYPYTYTRFQHYLDSLQKRNMDYFFREQLGQSVQQRKLDLLTITSPDNLREGAEQKVVFITGRVHPGETPSSFVCQGIIDFLVSQHPIACVLREYLVFKIAPMLNPDGVYLGNYRCSLMGFDLNRHWLDPSPWVHPTLHGVKQLIVQMYNDPKTSLEFYIDIHAHSTMMNGFMYGNIFEDEERFQRQAIFPKLLCQNAEDFSYSSTSFNRDAVKAGTGRRFLGGLLDHTSYCYTLEVSFYSYIISGTTAAVPYTEEAYMKLGRNVARTFLDYYRLNPVVEKVAIPMPRLRNKEIEVQRRKEKSPPYKHPLLRGPASNYPNSKGDKKSSVNHKDPSTPF
Protein: DNA-directed RNA polymerases I and III subunit RPAC2 (RNA polymerases I and III subunit AC2) (AC19) (DNA-directed RNA polymerases I and III 16 kDa polypeptide) (RPA19) (P28000)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerase I subunit RPA190
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC10
- DNA-directed RNA polymerase III subunit RPC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MTEDIEQKKTATEVTPQEPKHIQEEEEQDVDMTGDEEQEEEPDREKIKLLTQATSEDGTSASFQIVEEDHTLGNALRYVIMKNPDVEFCGYSIPHPSENLLNIRIQTYGETTAVDALQKGLKDLMDLCDVVESKFTEKIKSM
Protein: Nucleolin 1 (Protein NUCLEOLIN LIKE 1) (AtNUC-L1) (Protein PARALLEL 1) (AtPARL1) (Q9FVQ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in pre-rRNA processing and ribosome assembly. Is associated with intranucleolar chromatin and pre-ribosomal particles and plays a role in controlling activation and repression of a specific subset of rRNA genes located in distinctive nucleolar organizer regions. Binds specifically rDNA chromatin and may be required to maintain rDNA chromatin structure, but is probably not required for the overall histone methylation status of 45S rRNA genes. Involved in leaf polarity establishment by functioning cooperatively with AS1 to repress abaxial genes ARF3, ARF4, KAN1, KAN2, YAB1 and YAB5, and the knox homeobox genes KNAT1, KNAT2, KNAT6, and STM to promote adaxial development in leaf primordia at shoot apical meristems at high temperatures.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:17108323, ECO:0000269|PubMed:17286797, ECO:0000269|PubMed:17369435, ECO:0000269|PubMed:27792779}. Note=Found in the dense fibrillar component region of the nucleolus. {ECO:0000269|PubMed:17108323}.
Interaction partners:
- DEAD-box ATP-dependent RNA helicase 10
- rRNA 2'-O-methyltransferase fibrillarin 2
- Probable nucleolar protein 5-2
- Nucleolar protein 56
- M phase phosphoprotein 10
- Protein THALLO
- H/ACA ribonucleoprotein complex subunit 4
- G-patch domain-containing protein 1
- Pumilio homolog 23
- 18S rRNA
Sequence:
MGKSKSATKVVAEIKATKPLKKGKREPEDDIDTKVSLKKQKKDVIAAVQKEKAVKKVPKKVESSDDSDSESEEEEKAKKVPAKKAASSSDESSDDSSSDDEPAPKKAVAATNGTVAKKSKDDSSSSDDDSSDEEVAVTKKPAAAAKNGSVKAKKESSSEDDSSSEDEPAKKPAAKIAKPAAKDSSSSDDDSDEDSEDEKPATKKAAPAAAKAASSSDSSDEDSDEESEDEKPAQKKADTKASKKSSSDESSESEEDESEDEEETPKKKSSDVEMVDAEKSSAKQPKTPSTPAAGGSKTLFAANLSFNIERADVENFFKEAGEVVDVRFSTNRDDGSFRGFGHVEFASSEEAQKALEFHGRPLLGREIRLDIAQERGERGERPAFTPQSGNFRSGGDGGDEKKIFVKGFDASLSEDDIKNTLREHFSSCGEIKNVSVPIDRDTGNSKGIAYLEFSEGKEKALELNGSDMGGGFYLVVDEPRPRGDSSGGGGFGRGNGRFGSGGGRGRDGGRGRFGSGGGRGRDGGRGRFGSGGGRGSDRGRGRPSFTPQGKKTTFGDE
Protein: Probable splicing factor, arginine/serine-rich 4 (CeSC35) (RNA-binding protein srp-2) (Q09511)
Organism: Caenorhabditis elegans
Function: May play a functionally redundant role in embryogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10906451}.
Interaction partners:
- Probable splicing factor, arginine/serine-rich 6
- Splicing factor U2AF 35 kDa subunit
- Probable splicing factor, arginine/serine-rich 3
- Splicing factor 3B subunit 1 domain-containing protein
- Probable splicing factor, arginine/serine-rich 7
- Splicing factor U2AF 65 kDa subunit
- Probable splicing factor, arginine/serine-rich 5
- Probable splicing factor, arginine/serine-rich 2
- RRM domain-containing protein
- RRM domain-containing protein
Sequence:
MSRGGGGDRRAAPDINGLTSLKIDNLSYQTTPNDLRRTFERYGDIGDVHIPRDKYSRQSKGFGFVRFYERRDAEHALDRTDGKLVDGRELRVTLAKYDRPSDERGGRGGGGGRRRSRSPRRRSRSPRYSRSRSPRRSRSRTRSPPSRDRRDSPDRRDNSRSRSRSPPPREDGSPKERRSRSRSASRSPSRSRSNSR
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8I1V7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGPPSTAPDYSSAKHALDSIGKRVHAQVQNEAKQRSNGDLKGLLTSATLSGGESAFTENPCELIKDKGDELLGDSGERHPCGNGSASEKRFSEVSGGECDDKKIEGNGRNNGGACAPYRRLFLCNKNMEKMGRTSTTKHDLLLDVCMAANYEAQSLIRYHDQYDATYPGSDFSMCTMLARSFADIGDIIRGKDLYLGKKKKKKTETERDQLESKLKKIFGDIYNELTNGRNGVKDHYQDDNGGNYFQLREDWWTANRATVWKAITCKADTGNAYFRPTCSNRQGPSQAHHYCRCNGDKPDDDKPNTDPPTYFDYVPQYLRWFEEWAEDFCRKKKIYVGIVKTYCREKYKSGNEPRYCSRNGYDCTKTKRAIGKYRMGNQCISCLYACNPYVDWINNQKEQFDKQKKKYTDEINEASRSSRRQKRGARSTGSSSNYDGYESKFYNILKDDYGTVDDFLKLLNKEKSCQAVKDNDGGTINFTEKNDDKNNNNKDKGTFYRSEYCQVCPDCGVKYNGSGWEEKKKNDQCNIKLYKPKKDAPHTPIKILKSGEGKEEIEKKLEAFCDKKDGGNSDSSLYDPWQCYQFDQLEKDEKEEGVDDRNYDNDVRTGGGLCILQKKNGEENGKKQKTYNDFFNFWVAHMLKDSIHWKKKLEKCLQNGTKTRCRNNEKCNKECECFQRWVEKKKTEWGKIKDHFKTQNIGDETNCDPIVTLEGVLKLQFLNEDSTQDKQNSLDSEELKHLKHLSEMLQETSGDGLTCGASDNEKETLMDKLIEHEEGIAKECLRKQNECEKKAKPEGRSDSHDDPQPPDDADNEDDLDDEDDEDEEEEVQVEDNTQEEGEQPVVPQQEEGSSSPTPAPAGPDVCDIVSQLFSDPSQFSDACTLKYVTGKNYGWKCIPSGNTSDTTGSESEATGARQRRDTDSSGDTTGGKDGATGGLCIPPRRRRLYVGGLSQWASQRTQGETSSQSGENLLEAFIQSAAIETFFLWHKYKAENTKTQGVGAGGADFLPATSSVATALAPGAVPSRPSLQLLSGVGVPGEPGMAPGVKSIPVPPLGVGVGGIPGVGALGGGALGPGGPVGLDGVPGQAQPLTLLRPGVLGNGLQSPQSRLRTLDGHFAGGESEDKTPQQWLQQGHIPPDFLRLMFYTLADYRDICIGGDRDIVGDTIVSNTEGSSSSKIKISEKIKEILNHDNKQEPAPKPSVEKTTPTEWWSQNGQHIWNGMICALTYTDSGGSITEDKDVRDKLIDKDTGKPQKNGDNDYTYEKVELKDDESGPKGNDTIQPATLKDFVEIPTYFRWLHEWGSDFCGKRARMLKDVKDNCRNIDKAGHHYCSGDGYDCTRDVIERNDKFVDLNCLGCYKQCRKYKKWIDIKFVEYHNQEKKYKDEYGKLTKDKSSDDKKLEGYKCAENFLKELKHCKPSEDNNDQDNKINFDKPEKTFNPSKYCKACPVYGVKYIGGNYIPNEEKDYKSKKGRVKKENDTIPKNIEVLVLGRKGEEKDKDKHLHDACKNTGLFEVARYEQWNCQKKKGIDQCKITKFANDIDFDKDIVFNEFFQRWLRYFVQDYNKLKDKINPCTKKETEKEKEKSYKCTQGCNDKCECVKEWLSKKKQEWTQIKTLYKQYSKISDQEIAFRVKSYFVDQGLFDNDYKKAQEVVEKPCDKEKLWGCTGDNLKEGEDPGKCHMGDFITNLISKLQKKIDDCNKNQAQNSVETQPSDENTAQCQDTHPDDEEDLLLEENENQVAQPNICPNQVEDKKIEEEVEKCETAQTTAEETAAAGGERQTPPAPAPAAPPSPPRPLPKPKPPKPDLPPALKNAMLSSTIMWSVGIGFAAFTYFFLKKKTKASVGNLFQILQIPKGDYDIPTLKSSNRYIPYASDRYKGKTYIYMEGDSSGDEKYAFMSDTTDVTSSESEYEELDVNDIYVPGSPKYKTLIEVVLEPSGNNTPTSDIPSDNTPTPQPITDDEWNQLKHDFISNMLQNTQNTEPNILHDNVDNNTHPTMSRHNMDQKPFIMSIHDRNLFSGEEYNYDMFNSGNNPINISDSTNSMDSLTSNNHSPYNDKNDLYSGIDLINDALSGNHIDIYDEMLKRKENELFGTQHHPKNITSNRVVTQTSSDDPIHNQLNLFHTWLDRHRDMCEKLKNDNERLAKLKEEWENETHSGDINSGIPSGNHVLNTDVSIQIHMDNPKPINEFTNMDTSPDKSTMDTIIDDLEKYNEPYYYDFYEYDIYYDVNDDDKTSMDNNNNLVNKNNPVDSNSSTYNHHNPADINKTFVDINNHNQHPIEKPTKIQIEMNSNNREVDEQQYPIADIWNI
Protein: Gadd45b1 protein (Gadd45bl protein) (Growth arrest and DNA-damage-inducible, beta b) (Growth arrest and DNA-damage-inducible, beta like) (Q5NU21)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 4
- Cellular tumor antigen p53
- Proliferating cell nuclear antigen
- Cyclin-dependent kinase 1
- Cyclin B3
- Cyclin B1
- Cyclin B2
- Phosphoinositide-3-kinase, regulatory subunit 3A
Sequence:
MTLEEVVGCNSTERKMETVSEALEELLMAAQRQNCLTVGVYESAQLMNVDPDSVVLCVLATDEEDENDVALQIHFTLIQAFCCDIDINIVRVSGMRRLAQVLEEPLSTDNNANEPRDLHCILVTNPQAEHLKLKEVGSYCKESRCRNQWVPSIALQER
Protein: Cytidylate kinase (CK) (EC 2.7.4.25) (Cytidine monophosphate kinase) (CMP kinase) (Protein MssA) (p25) (P0A6I0)
Organism: Escherichia coli (strain K12)
Function: ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors.
Subcellular location: Cytoplasm.
Interaction partners:
- GTPase Der
- Small ribosomal subunit protein bS1
- Uridine kinase
- Nucleoside diphosphate kinase
- 5'/3'-nucleotidase SurE
- 3-phosphoshikimate 1-carboxyvinyltransferase
- 5'-deoxynucleotidase YfbR
- Ribonucleoside-diphosphate reductase 1 subunit beta
- Ribonucleoside-diphosphate reductase 1 subunit alpha
- Nucleoside triphosphate pyrophosphohydrolase
Sequence:
MTAIAPVITIDGPSGAGKGTLCKAMAEALQWHLLDSGAIYRVLALAALHHHVDVASEDALVPLASHLDVRFVSTNGNLEVILEGEDVSGEIRTQEVANAASQVAAFPRVREALLRRQRAFRELPGLIADGRDMGTVVFPDAPVKIFLDASSEERAHRRMLQLQEKGFSVNFERLLAEIKERDDRDRNRAVAPLVPAADALVLDSTTLSIEQVIEKALQYARQKLALA
Protein: Pro-glucagon [Cleaved into: Glicentin; Glicentin-related polypeptide (GRPP); Oxyntomodulin (OXM) (OXY); Glucagon; Glucagon-like peptide 1 (GLP-1); Glucagon-like peptide 1(7-37) (GLP-1(7-37)); Glucagon-like peptide 1(7-36) (GLP-1(7-36)); Glucagon-like peptide 2 (GLP-2)] (P55095)
Organism: Mus musculus (Mouse)
Function: Plays a key role in glucose metabolism and homeostasis. Regulates blood glucose by increasing gluconeogenesis and decreasing glycolysis. A counterregulatory hormone of insulin, raises plasma glucose levels in response to insulin-induced hypoglycemia. Plays an important role in initiating and maintaining hyperglycemic conditions in diabetes.
Subcellular location: Secreted {ECO:0000269|PubMed:22037645}.; SUBCELLULAR LOCATION: [Glucagon-like peptide 1]: Secreted {ECO:0000269|PubMed:22037645}.
Interaction partners:
- Glucagon receptor
- Glucagon-like peptide 1 receptor
- Gastric inhibitory polypeptide receptor
- Glucagon-like peptide 2 receptor
- Guanine nucleotide-binding protein G
- Appetite-regulating hormone
- Dipeptidyl peptidase 4
- Glucose-dependent insulinotropic receptor
- Vasoactive intestinal polypeptide receptor 2
- Leptin
Sequence:
MKTIYFVAGLLIMLVQGSWQHALQDTEENPRSFPASQTEAHEDPDEMNEDKRHSQGTFTSDYSKYLDSRRAQDFVQWLMNTKRNRNNIAKRHDEFERHAEGTFTSDVSSYLEGQAAKEFIAWLVKGRGRRDFPEEVAIAEELGRRHADGSFSDEMSTILDNLATRDFINWLIQTKITDKK
Protein: Transmembrane protein 182 (B2RVY9)
Organism: Mus musculus (Mouse)
Function: Negatively regulates myogenesis and skeletal muscle regeneration via its association with ITGB1. Modulates ITGB1 activation by decreasing ITGB1-LAMB1 interaction and inhibiting ITGB1-mediated intracellular signaling during myogenesis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:A0A1D5NY17}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transmembrane 6 superfamily member 1
Sequence:
MRLNVAVFFGALFGALGVLLFLVAFGSDYWLLATEVGRCSGEQNIENITFHHEGFFWRCWFSGVVEENNSNIWKFWYTNQPPSKNCTHAYLSPYPFMRGEHNSTSYDSAIIYRGFWAVLLLLGVVAALTASFLIICAAPFSSHFLYKAGGGSYIASGVLFSLVVILYVIWVQAVADMESYRALRMRDCWEFTPSILYGWSFFLAPAGVFFSLLAGLLFLVVGRHIQIHH
Protein: Protein dip1 (O74771)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in protein-linked oligosaccharide phosphorylation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 3
- Actin-related protein 2
- Actin
- Actin-related protein 2/3 complex subunit 1
- Actin-related protein 2/3 complex subunit 3
- Protein BZZ1
- Actin-binding protein wsp1
Sequence:
MEFTDVFYNLENEKQFLAEIDELLTIPYEKNELEIGVSKFLSFINKYGEPYLITEFQLQRCMEKFLNSPLYQLDENAVLSIFYDCFFFLKEQQTLKFIIIVFQSEIQENEYCLRLLASTGFIPVLIKAMKQFKDRSENVAFTSFRYALFLVYYICRSRRLSPTDLVAIDEYFLVNLFKTSEEAWNDEDMDSFGMCVLTLLSINEQFMLVRLASKGSFEIANGIMDLLSSSKVDNGIYSEGLVFTLNREKDPRSRMLILKQLFLLFTTPATYEIFYTNDLNVLIDIFIREINNIPDELSDLRYAYLQVLIPLLENTQVRHPPHYKTKCIVDAVNNVLISHSKSSNMEDARTTDVAIRVLEVPWLQQEMKSLGTAQ
Protein: Cytosolic Fe-S cluster assembly factor NUBP1 homolog (Q38C73)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03038}.
Interaction partners:
Sequence:
MNLANSHCIGPDSPDAGLAPSCKGCPNASLCASAPKGPDPDIELIRQRLSGVKRKVLIVSGKGGVGKSTLTKELAFAIGKRGLNVAVVDLDICGPSIPRLTGARGENAHYSATGIEPVMIDETVTMMSMHYFLENKNEAVLFRGPRKNGAVKMFLKDVIWNDVDVMLIDTPPGTSDEHITTASLLQQCGGVSGAVLVTTPQMVAEADVRREVNFCQKAKLNIMGIVENMSGFVCPNCGSGSFIFPRTNTRGAGKRLSEEFGIPLWGEIPLDPKLMSSCEEGTPLAESVDQNNPTLDVLNSISRKLIESLAME