wanglab/gogpt-training-data huggingface dataset:
Protein: Cell division cycle protein cdt1 (P40382)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA replication licensing factor, required for pre-replication complex assembly. Faithful duplication of the genetic material requires 'once per cell cycle' DNA replication initiation and elongation. Central to this control is the tightly regulated formation of prereplicative complexes (preRCs) at future origins of DNA replication. Required for the recruitment of the MCM helicase complex to the replication origins.
Subcellular location: Nucleus {ECO:0000269|PubMed:10766248}. Note=Present in the nucleus after mitosis when DNA licensing takes place.
Interaction partners:
- DNA replication licensing factor mcm3
- Origin recognition complex subunit 3
- Cell division control protein 18
- DNA replication licensing factor mcm4
- DNA replication licensing factor mcm7
- DNA replication licensing factor mcm5
- Origin recognition complex subunit 1
- Origin recognition complex subunit 5
- DNA replication licensing factor mcm2
- DNA replication licensing factor mcm6
Sequence:
MKCRALYSHDNNILIFGFCVQIMSAGSQTKLNFSVRKTRSSSKRSNAAIIEPPKNPEDSQIIPAVKRLKENLDTESLEQNEVLPPVKNESVLFLEKVFNAVDICVKFHLSINTKPTFVLLENKVSGLTKISLKITHLAQILTVWPESFAITPCFTIHQGKRVATYELSYPRNANLPEAFSRSIEFKRRLEKWLLEHCSETEIPAQQLQALPSLSKNTVNESSLVRKLNLEKSTSRELRIPTQTLEPKFTTNTAKYANELVSCSMLDSSSTLSKSVNSKINLKSHQSSSSVQNSSRKLTSSQLTLRQSSLFDRVRKKQKAMEAKKAEEFKNNLVVHTLAKEKVSFVRIIDLIFVQLSTWPTKRSFSMSEIVTSMQMSISSSLSPDQCAKAIELLSKALPAWCTINLLGNIQVVTFSRIVNGKPYLRSQLIEELQTKASITILSNS
Protein: Major urinary protein 5 (Major urinary protein 8) (A2AKN8)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MKMLLLLCVGLTLVCVHAEEASSTGRNFNVEKINGEWHTIILASDKREKIEDNGNFRLFLEQIRVLENSLVLKVHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE
Protein: SCY1-like protein 2 (Coated vesicle-associated kinase of 104 kDa) (Q6P3W7)
Organism: Homo sapiens (Human)
Function: Component of the AP2-containing clathrin coat that may regulate clathrin-dependent trafficking at plasma membrane, TGN and endosomal system (Probable). A possible serine/threonine-protein kinase toward the beta2-subunit of the plasma membrane adapter complex AP2 and other proteins in presence of poly-L-lysine has not been confirmed. By regulating the expression of excitatory receptors at synapses, plays an essential role in neuronal function and signaling and in brain development (By similarity).
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000269|PubMed:15809293, ECO:0000269|PubMed:16914521}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:16914521}. Endosome membrane {ECO:0000269|PubMed:16914521}. Note=Colocalizes to the trans-Golgi network (TGN) and to endosomal membranes with clathrin, transferrin and plasma membrane adapter AP1 and AP3 complexes. {ECO:0000269|PubMed:16914521}.
Interaction partners:
- Clathrin interactor 1
Sequence:
MESMLNKLKSTVTKVTADVTSAVMGNPVTREFDVGRHIASGGNGLAWKIFNGTKKSTKQEVAVFVFDKKLIDKYQKFEKDQIIDSLKRGVQQLTRLRHPRLLTVQHPLEESRDCLAFCTEPVFASLANVLGNWENLPSPISPDIKDYKLYDVETKYGLLQVSEGLSFLHSSVKMVHGNITPENIILNKSGAWKIMGFDFCVSSTNPSEQEPKFPCKEWDPNLPSLCLPNPEYLAPEYILSVSCETASDMYSLGTVMYAVFNKGKPIFEVNKQDIYKSFSRQLDQLSRLGSSSLTNIPEEVREHVKLLLNVTPTVRPDADQMTKIPFFDDVGAVTLQYFDTLFQRDNLQKSQFFKGLPKVLPKLPKRVIVQRILPCLTSEFVNPDMVPFVLPNVLLIAEECTKEEYVKLILPELGPVFKQQEPIQILLIFLQKMDLLLTKTPPDEIKNSVLPMVYRALEAPSIQIQELCLNIIPTFANLIDYPSMKNALIPRIKNACLQTSSLAVRVNSLVCLGKILEYLDKWFVLDDILPFLQQIPSKEPAVLMGILGIYKCTFTHKKLGITKEQLAGKVLPHLIPLSIENNLNLNQFNSFISVIKEMLNRLESEHKTKLEQLHIMQEQQKSLDIGNQMNVSEEMKVTNIGNQQIDKVFNNIGADLLTGSESENKEDGLQNKHKRASLTLEEKQKLAKEQEQAQKLKSQQPLKPQVHTPVATVKQTKDLTDTLMDNMSSLTSLSVSTPKSSASSTFTSVPSMGIGMMFSTPTDNTKRNLTNGLNANMGFQTSGFNMPVNTNQNFYSSPSTVGVTKMTLGTPPTLPNFNALSVPPAGAKQTQQRPTDMSALNNLFGPQKPKVSMNQLSQQKPNQWLNQFVPPQGSPTMGSSVMGTQMNVIGQSAFGMQGNPFFNPQNFAQPPTTMTNSSSASNDLKDLFG
Protein: Succinyl-CoA:3-ketoacid coenzyme A transferase 2A, mitochondrial (EC 2.8.3.5) (3-oxoacid CoA-transferase 2A) (Testis-specific succinyl-CoA:3-oxoacid CoA-transferase 1) (SCOT-t1) (Q9JJN4)
Organism: Mus musculus (Mouse)
Function: Key enzyme for ketone body catabolism. Transfers the CoA moiety from succinate to acetoacetate. Formation of the enzyme-CoA intermediate proceeds via an unstable anhydride species formed between the carboxylate groups of the enzyme and substrate (By similarity). Probably play and important roles in the energy metabolism of spermatozoa.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- D-beta-hydroxybutyrate dehydrogenase, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic
- Dehydrogenase/reductase SDR family member 6
- Acetoacetyl-CoA synthetase
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Acetyl-CoA acetyltransferase, cytosolic
Sequence:
MAALRLLAWALPRGVSALRPPPALPHRLIRRYVSDRSGSVHFYTDPVKAVEGVKDGSTVMLGGFGLCGIPENLIGALKTKGVKDLKIVSSNVGVDDFGLGILLASKQVRRVVCSYLGENALCEKLYLAGELELEMTPQGTLAERIRAGGTGVPAFYTPTGYGTLVQEGGSPIRYAPDGHLITLSEPREVREFQGRFYLLEHAIRADFALIKGWKADRSGNVIFRGSARNFNVPMCKAADISVVEVEEIVDVGTFAPEDIHVPNIYVDRVIKGPKFEKRIERLTTRDSKPAPGSKDNDPSRTRIIKRAALEFQDGMYANLGIGIPVLASNYISPKMTVYLHSENGILGLGPFPLKNEVDADVINAGKQTVTVVPGGCFFASDDSFAMIRGGHLQLTMLGAMQVSQYGDLANWMVPGKKVKGMGGAMDLVSSKKTRVVVTMEHCTKTKQPKILKKCTMPLTGKRCVDLIITEKAVFEVNHSKGLTLVELWEGSSVDDIKATTACSFAVSPNLKPMQQIKLDA
Protein: DnaJ protein ERDJ3B (Chaperone protein dnaJ B6) (OsDjB6) (Endoplasmic reticulum dnaJ domain-containing protein 3B) (OsERdj3B) (B9FHF3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May play a role in protein folding in the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:24153418}.
Interaction partners:
- DnaJ protein P58IPK homolog A
- DnaJ protein P58IPK homolog B
- Os01g0757900 protein
- Heat shock 70 kDa protein BIP3
- Heat shock 70 kDa protein BIP1
- Heat shock 70 kDa protein BIP4
- Heat shock protein 81-2
- Os02g0710900 protein
- Heat shock 70 kDa protein BIP5
- Heat shock 70 kDa protein BIP2
Sequence:
MAAPRWIGPLLLLLLHFVAAVAGKSYYDVLQVPKGASEDQIKRSYRKLALKYHPDKNPNNEEANKRFAEINNAYEILTDQEKRKIYDRYGEEGLKQFQAQGGRGGGGGMNIQDIFSSFFGGGGGGMEEEEEQIIKGDDVIVELDASLEDLYMGGSLKVWREKNVIKPAPGKRRCNCRNEVYHRQIGPGMYQQMTEQVCDQCANVKYVREGDFLTVDIEKGMQDGQEVSFFEEGEPKIDGEPGDLKFRIRTAPHERFRREGNDLHTTVTISLLQALVGFEKTIKHLDNHMVEIGTKGITKPKEVRKFKGEGMPLYQSNKKGDLYVTFEVLFPKTLTDDQKSKLKSILT
Protein: Probable nicotianamine synthase 4 (EC 2.5.1.43) (S-adenosyl-L-methionine:S-adenosyl-L-methionine:S-adenosyl-methionine 3-amino-3-carboxypropyltransferase 4) (Q9C7X5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Synthesizes nicotianamine, a polyamine which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Interaction partners:
- Transcription factor bHLH47
- Ferric reduction oxidase 3, mitochondrial
- Transcription factor bHLH101
- Protein ZINC INDUCED FACILITATOR 1
- Ferric reduction oxidase 2
- Fe
- Transcription factor ORG3
- Transcription factor ORG2
- Transcription factor MYB72
- Transcription factor bHLH100
Sequence:
MGYCQDDQLVNKICDLYEKISKLETLKPCEDVDTLFKQLVSTCIPPNPNIDVTKMSENIQEMRSNLIKICGEAEGYLEHHFSSILTSFEDNPLHHLNLFPYYNNYLKLSKLEFDLLEQNLNGFVPRTVAFIGSGPLPLTSVVLASSHLKDSIFHNFDIDPSANMVAARLVSSDPDLSQRMFFHTVDIMDVTESLKGFDVVFLAALVGMDKKEKVKVVEHLEKHMSPGALLMLRSAHGPRAFLYPIVEPCDLEGFEVLSVYHPTDEVINSIVISRKLGEDANGVVHDHIDQASDLACNCSKIHVIMNKKKSIIEEFAGANEEQLT
Protein: Uncharacterized beta-glucan synthesis-associated protein C23H3.11c (O13941)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for synthesis of the major beta-glucans of the yeast cell wall.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein P22H7.03
Sequence:
MEKGHSDLPRQPERVAQNPFLTFDQDSFPSSYGSSLNVSEQTSGSSSTSPLPQISCLLRKDDVPLANKELSRSLIHVQELSRYPPFYNQDHQHLGVPRSRVGSDVWKMREKSFLSPSQFSSIDLSWVYRSKEEDDDFHDPKSSVVSLMGEEDYLGWSRFCDLFFLFVLSLGIGLLFIVFPALTFTGNITPSKEKFDAIMANQITDHLFAHMRVPRTNLIDKDTPSTAYHRTGYNGRKYNLVFSDEFNKEGRSFYSGNDQFWEAVNIHYAATNDLDWYDPDAITTVNGTLAIQLDAFWNRDLNFRSGMLQSWNKLCLKGGIIEVSASLAGSGEHAGLWPGIWTLGNLARPGYMATTDGVWPYAYSQCDVGITPNQSSYDGISYLPGQKLPNCVCLNEDHPSPGVGRGAPEIDILEGSTEKLHPDDELDIGVVSQSGQFAPFDFFWLPNYDYLAVYNDSITHMNSYVGGPFQQALSGITTLNNTWYGGNAFQIYGFDYKPGEGTNGYVSWFVGPNYTWSMLGSAVGQNGNVGPRQISEEPMSIIFNLGISNNWAYYYFRDLSFPAVMYIDYIRIYQDPDDTNSHIGCDPPGYPTTKYIEEHPLAYKNPNATTWEMAGYTWPKNSLMHKCNT
Protein: Biorientation defective 1, isoform A (Biorientation defective 1, isoform C) (LD18173p) (Q9VAY4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDDFIKTLIAEVKSQGVFDEFRFNCCLADVDTKPAYQNVRTQVETAVNDFLAKQQWTPETNKVQLRERLRKHLMDSDVLDKGVDQIVDQVVNPKVATIFEPKIESIVYKYLGITPPARPTMLSAPPLPPFGAHLNGSSLLNVETTVGLLPTDLEQISPDSDRATVKSESRDDELPPGVDDEDTSPSYELVSERKTLAIKEELNNVSLNNSDSVNGVSQASQLSQVSSDSRLTMASSTESMVDSHQHTAAHNSGEPENICEEAQMPKFSENSWDASAGTGRSEGRQLHFDIKQDAITFEGTERKNSVSETTSTGLQILSIEDEIMSEVKANIDDANNASIESIAPEPVQVPAPPKVNPPPPPRPASPKVEPPPPAPPGVESPPGPQPPASPRFDPPPPHTIEPPPPPAPPTLVPPPPPAPPTIKPPPPPAPPTVEPPPPPPPAPPTVEPPPPPPPAPTKVEPPPPPAPAEVEPPPPPAPTELEPPPPPAPPKVELPPPPAPPKAEAAITPRRAKGSNGFITELAVTPKESETRDKPHNVNTDVKEDEQPATTEDKQDKPLELGLDAPKDAVSTASESTESPTSTSSQSKSHSKSRDKEKEKDRRHHRHSDDKHRRRSTDRDRDRSRDKSHSKHSSSSSSKHSSSNSSSSKHKSSSSKNDKSSSSSSSRSNRESSSSKRSGTTSSSRHESSSHKKHKSSSSSSRSERDKGKEKDKEREKDSQSRSHHSSSSSSSSSRRKDHDRGRDRDRNKSNTSGSAENKAIHDDHSESKEKYKQRRGSDSNDEGKPPSSGGPAKNSQPEDSAATMKSDAPVENANGTNGNSNGSTNGACDNVSGVVIVSDILQQSTSSFVELTAGSQSHDRAESSKHEPEDIDGKEADNQPEKTELEARQDECASQNEVPTVEPQTLADSVPDLPAKESMDTLEDEKVETNVEENKSEEESKPENPPEECVDEPAQVGDVEDPPQDADKPATPVPISNEQSDEFSADFVTHFEENTDEFRTRLQLINQLIEDRKNLLNRLSEDGTQEEAVDIRALRRSLSKRRRSSMQEQHRVERETTPPQPRSPSSSSTAGSPAKRLRQDEPKSSPTPSDASINSKENEALEKQEHAV
Protein: Tyrosinase (EC 1.14.18.1) (Monophenol monooxygenase) (L8B082)
Organism: Homo sapiens (Human)
Subcellular location: Melanosome membrane {ECO:0000256|ARBA:ARBA00004573}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004573}.
Interaction partners:
Sequence:
MLLAVLYCLLWSFQTSAGHFPRACVSSKNLMEKECCPPWSGDRSPCGQLSGRGSCQNILLSNAPLGPQFPFTGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFWGPNCTERRLLVRRNIFDLSAPEKDKFFAYLTLAKHTISSDYVIPIGTYGQMKNGSTPMFNDINIYDLFVWMHYYVSMDALLGGSEIWRDIDFAHEAPAFLPWHRLFLLRWEQEIQKLTGDENFTIPYWDWRDAEKCDICTDEYMGGQHPTNPNLLSPASFFSSWQIVCSRLEEYNSHQSLCNGTPEGPLRRNPGNHDKSRTPRLPSSADVEFCLSLTQYESGSMDKAANFSFRNTLEGFASPLTGIADASQSSMHNALHIYMNGTMSQVQGSANDPIFLLHHAFVDSIFEQWLRRHRPLQEVYPEANAPIGHNRESYMVPFIPLYRNGDFFISSKDLGYDYSYLQDSDPDSFQDYIKSYLEQASRIWSWLLGAAMVGAVLTALLAGLVSLLCRHKRKQLPEEKQPLLMEKEDYHSLYQSHL
Protein: Ferredoxin (P68163)
Organism: Datura inoxia (Downy thornapple) (Datura meteloides)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:7764481}.
Interaction partners:
Sequence:
ATYKVKLVTPDGPVEFDCPDDVYILDRAEEEGHDLPYSCRAGSCSSCAGKVTAGTVDQSDGNYLDDDQMAEGFVLTCVAYPQSDVTIETHKEEELTG
Protein: Protein phosphatase methylesterase 1 (PME-1) (EC 3.1.1.89) (Yms2) (P38796)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Demethylates proteins that have been reversibly carboxymethylated. Demethylates the phosphatase PP2A catalytic subunits PPH21 and PPH22. Forms inactive complexes (PP2Ai) with phosphatase PP2A-like catalytic subunits. Involved in the regulation of cell cycle progression at START.
Interaction partners:
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
- Protein phosphatase PP2A regulatory subunit A
- Serine/threonine-protein phosphatase PP2A-2 catalytic subunit
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
- Ribosome assembly protein RSM22
- Small ribosomal subunit protein mS38
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein uS8m
- Small ribosomal subunit protein mS41
- Small ribosomal subunit protein uS3m
Sequence:
MSDDLRRKIALSQFERAKNVLDATFQEAYEDDENDGDALGSLPSFNGQSNRNRKYTGKTGSTTDRISSKEKSSLPTWSDFFDNKELVSLPDRDLDVNTYYTLPTSLLSNTTSIPIFIFHHGAGSSGLSFANLAKELNTKLEGRCGCFAFDARGHAETKFKKADAPICFDRDSFIKDFVSLLNYWFKSKISQEPLQKVSVILIGHSLGGSICTFAYPKLSTELQKKILGITMLDIVEEAAIMALNKVEHFLQNTPNVFESINDAVDWHVQHALSRLRSSAEIAIPALFAPLKSGKVVRITNLKTFSPFWDTWFTDLSHSFVGLPVSKLLILAGNENLDKELIVGQMQGKYQLVVFQDSGHFIQEDSPIKTAITLIDFWKRNDSRNVVIKTNWGQHKTVQNT
Protein: Sodium/hydrogen exchanger (Q3TM63)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MGPRGTAHSVRAPLSWLLLLLLSLQVAVPAGALAETLLDAPRARGASSNPPSPASVVAPGTTPFEESRLPVFTLDYPHVQIPFEITLWILLASLAKIGFHLYHKLPTIVPESCLLIMVGLLLGGIIFGVDEKSPPAMKTDVFFLYLLPPIVLDAGYFMPTRPFFENFGTIFWYAVVGTLWNSIGIGVSLFGICQIEAFGLSDITLLQNLLFGSLISAVDPVAVLAVFENIHVNEQLYILVFGESLLNDAVTVVLYNLFKSFCQMKTIQTVDVFAGIANFFVVGIGGVLIGILLGFIAAFTTRFTHNIRVIEPLFVFLYSYLSYITAEMFHLSGIMA
Protein: tRNA (guanine(37)-N(1))-methyltransferase (EC 2.1.1.228) (M1G-methyltransferase) (tRNA [GM37] methyltransferase) (tRNA methyltransferase 5 homolog) (Q32P41)
Organism: Homo sapiens (Human)
Function: Involved in mitochondrial tRNA methylation. Specifically methylates the N1 position of guanosine-37 in various tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03152, ECO:0000269|PubMed:26189817}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03152}. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03152}. Note=Predominantly in the mitochondria and in the nucleus. {ECO:0000255|HAMAP-Rule:MF_03152}.
Interaction partners:
- Multifunctional methyltransferase subunit TRM112-like protein
- tRNA wybutosine-synthesizing protein 3 homolog
- S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase TYW1
- tRNA wybutosine-synthesizing protein 2 homolog
- tRNA dimethylallyltransferase
- tRNA methyltransferase 10 homolog A
- tRNA wybutosine-synthesizing protein 4
- tRNA
- tRNA methyltransferase 10 homolog B
- tRNA
Sequence:
MVLWILWRPFGFSGRFLKLESHSITESKSLIPVAWTSLTQMLLEAPGIFLLGQRKRFSTMPETETHERETELFSPPSDVRGMTKLDRTAFKKTVNIPVLKVRKEIVSKLMRSLKRAALQRPGIRRVIEDPEDKESRLIMLDPYKIFTHDSFEKAELSVLEQLNVSPQISKYNLELTYEHFKSEEILRAVLPEGQDVTSGFSRIGHIAHLNLRDHQLPFKHLIGQVMIDKNPGITSAVNKINNIDNMYRNFQMEVLSGEQNMMTKVRENNYTYEFDFSKVYWNPRLSTEHSRITELLKPGDVLFDVFAGVGPFAIPVAKKNCTVFANDLNPESHKWLLYNCKLNKVDQKVKVFNLDGKDFLQGPVKEELMQLLGLSKERKPSVHVVMNLPAKAIEFLSAFKWLLDGQPCSSEFLPIVHCYSFSKDANPAEDVRQRAGAVLGISLEACSSVHLVRNVAPNKEMLCITFQIPASVLYKNQTRNPENHEDPPLKRQRTAEAFSDEKTQIVSNT
Protein: Protein phosphatase 1 regulatory subunit 3C (Protein phosphatase 1 regulatory subunit 5) (PP1 subunit R5) (Protein targeting to glycogen) (PTG) (Q7TMB3)
Organism: Mus musculus (Mouse)
Function: Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown. Dramatically increases basal and insulin-stimulated glycogen synthesis upon overexpression in a variety of cell types.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Glycogen [starch] synthase, muscle
- Glycogen [starch] synthase, liver
- Protein phosphatase 1 regulatory subunit 3A
- Protein phosphatase 1 regulatory subunit 3B
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Glycogenin-1
- Protein phosphatase 1 regulatory subunit
- Serine/threonine-protein phosphatase PP1-beta catalytic subunit
- Protein phosphatase 1 regulatory subunit 3E
Sequence:
MSCTRMIHVLDPRPLTSSVMPVDMAMRICLAHSPPLKSFLGPYNGFQRRNFVNKLKPLKPCLSVKQEAKSQSEWKSPHNQAKKRVVFADSKGLSLTAIHVFSDLPEEPAWDLQFDLLDLNDISSSLKLHEEKNLVFDFPQPSTDYLSFRDRFQKNFVCLENCSLQDRTVTGTVKVKNVSFEKKVQVRITFDTWKTYTDVDCVYMKNVYSSSDSDTFSFAIDLPRVIPTEEKIEFCISYHANGRIFWDNNEGQNYRIVHVQWKPDGVQTQVAPKDCAFQQGPPKTEIEPTVFGSPRLASGLFPEWQSWGRVENLTSYR
Protein: Progonadoliberin [Cleaved into: Gonadoliberin (Gonadotropin-releasing hormone) (GnRH) (Luliberin) (Luteinizing hormone-releasing hormone) (LH-RH); GnRH-associated peptide (GnRH-associated peptide)] (F1QW13)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU000635}.
Interaction partners:
- Progonadoliberin
- Kisspeptin
- Gonadotropin-releasing hormone receptor 1
- Type II GnRH receptor
- Lhb protein
- Gonadotropin-releasing hormone receptor 2.
- Follicle-stimulating hormone beta subunit
- KiSS-1 metastasis suppressor
- KISS1 receptor b
- FMRFamide related peptide 1
Sequence:
MEWKGRLLVQLLLLVCVLEVSLCQHWSYGWLPGGKRSVGEMEATFRMLDPGDTVLSIPADSPMEQLSPIHIVNEVDAEGLPLKGQRFPDRRGRV
Protein: Antithrombin-III (ATIII) (Serpin C1) (P32261)
Organism: Mus musculus (Mouse)
Function: Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin (By similarity).
Subcellular location: Secreted, extracellular space {ECO:0000250}.
Interaction partners:
- Prothrombin
- Coagulation factor X
- Coagulation factor IX
- Coagulation factor XII
- Plasminogen
- Coagulation factor XI
- Fibrinogen beta chain
- Vitamin K-dependent protein C
- Fibrinogen alpha chain
- Protein AMBP
Sequence:
MYSPGAGSGAAGERKLCLLSLLLIGALGCAICHGNPVDDICIAKPRDIPVNPLCIYRSPGKKATEEDGSEQKVPEATNRRVWELSKANSRFATNFYQHLADSKNDNDNIFLSPLSISTAFAMTKLGACNDTLKQLMEVFKFDTISEKTSDQIHFFFAKLNCRLYRKANKSSDLVSANRLFGDKSLTFNESYQDVSEVVYGAKLQPLDFKENPEQSRVTINNWVANKTEGRIKDVIPQGAINELTALVLVNTIYFKGLWKSKFSPENTRKEPFYKVDGQSCPVPMMYQEGKFKYRRVAEGTQVLELPFKGDDITMVLILPKPEKSLAKVEQELTPELLQEWLDELSETMLVVHMPRFRTEDGFSLKEQLQDMGLIDLFSPEKSQLPGIVAGGRDDLYVSDAFHKAFLEVNEEGSEAAASTSVVITGRSLNPNRVTFKANRPFLVLIREVALNTIIFMGRVANPCVN
Protein: RT1 class I, A2 (RT1 class Ia, A2n) (RT1 class Ia, locus A2) (Q6MGB8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MMEPCTLLLLLAVALTPTQTRAGSHSLRYFVTAVSRPGLGEPRYMEVGYVDDTQFVRYDSDAENPRYEPRAPWMEREGPEYWERETQNAKRNEQVYRVDLRTALRYYNQSEGGSHTIQRMYGCDMGSDGSLLRGYYQDAYDGRDYIALNEDLKTWTAADFAAQITRSKWDQAGVAERLRAYLEGTCVEWLRRYLELGKETLLRSDPPEAHVTLHPRPEGDVTLRCWALGFYPADITLTWQLNGEDLTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVEHEGLPEPLSQRWEPSPSTNSNMETTVIYVVLGAIIGTLAIIGIVVAVVRKRRRNTGGKGDYTPAPGRDSSQSSDVSLPDCKA
Protein: WD repeat protein mio zinc-ribbon like domain-containing protein (Q57XW5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- WD repeat protein mio zinc-ribbon like domain-containing protein
- Vacuolar membrane-associated protein Iml1 N-terminal domain-containing protein
- Ras-family member, GTP-binding protein, putative
- Small GTPase, putative
- Protein transport protein sec13, putative
- Protein transport protein Sec13, putative
- PA26 p53-induced protein
Sequence:
MKYFACRLDDHNGFGLLIGHTLSYFTARRATTKGFSTATPKSAGSGTDGEDAFNFHVQYTVTLPHVFGFAPKCFSMANYSLYGVDMAIIGGSNGVLGVVVMHDGSIVYAPDRSPEVMNANNQRSATTTSVWALSCAARSLPSVRMLDTASTLKQVAGATSSPPFPQPMPLADRGVGTVTWIQNDALVFVGFTSGQVEWYRVTTRIRQPESKEKSSELINIGTVGRPTRSGCVTGAFPANGDMFAGMTNPSGANHRTSDSFPHHQSTWVNRQSRREGAPQLGSKEEHKDGWFVDICSHYSSNYFAETGGFVTSEYFPATGLVLAAAERALYVFTRKQPETTLCCVPRTGCTYISCHPSLPLVACLGCGNKTPNINGDPGEGSCALQVLEWTDEGEMCPVTEICVLTPSSDSSARCCSHLNCSWNQGAELQLAVCNMKECAIQLLNLSRAEEWVHCETVPTARRRWYEIIFNRELHHPLRSLVNAEFILPRVLEQDRKLAKPPAFASDPAAGCHERKGSHPRDSLETKRGSTATLSKEAPPALLAPNPVQDGEGCLVKNTVAGDERSTQSRTSEIAPCRAVPSVSTVPHVIVVNTVGEIAVTPLHTETKVAFFGLNSIVAGIGATVCAIKTPAKETSISGCCAGAPTATITLSVPFPSRSVPVTAREEQARASMADTIDIEEHMRKRLAAGFGVPAAANVEALTKLNGTSAYDVDERVLFSYIAIMEKVGLVRCDGPVPSIVELLTLRGAPNTTQLTDMGLLPHNTAVVCRSSTSQNDSRRLLLLHLLNWIPSRSESPQRNQQTPATRADVERAVVVDVLHRQRLRAATFLRQQLHIDSNYSIVAGLIENYDKVASAMNDCAGEVREPFLQRLSPWLRVVFTFEADKMAVYKNEALPFWDRVAIALILEHDTKLLVELLRNTFAPLCNMVQELLLFGGISAKTCQLMQTIVDCTGDFQLAACLFARIGVHATATRGTVREGESAFNRNGVHDDSSWFKESSTGRRDEVNTVANYWALWSGAYRSFLDNEREFVKRVVFDQQCQNCSKLLYSGEHGTRTKIEVLERSNSTGHAAGGPVTTLQLPVANQRRCYVCSSSVRLGPLMARSSYAHCAVCGHGGHIHHLQAWFLAHQKCAAAGCGCHCAVDGHVS
Protein: Pannexin (B3DLA5)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU010713}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- Uncharacterized protein.
Sequence:
MAIAHIATEYVFSDFLLKDPPESKYKGLRLELAVDKLVSCIAVGLPLLLISLAFAQEITLGSQISCFAPTSFSWRQAAYVDSFCWAAVQQKHLSQSDSGNVPLWLHKFFPYILLLVAVLLYLPNLFWRFTAAPHLSSDLKFVMEELDKCYNRDIKDIKAANNLNSSDKRDGLNSPVVSENLQQSLWEIPLSHYKYPIVEQYLKTKNNSYGLIIKYLICRVVTLIIVFTACIYLGYYISLFSLTDEFTCNIRTGILRNDTALPPLVQCKLIAVGVFRLLSYINLIIYVLIMPFIIYAMLVPFRKTANVLKVYEVLPTFSVQQAPSKTYDDHSLFLLFLEENVSELKSYKFLKVLENIKNTGENFDTIQYLTSLGTVKTDTVDGKLAFKCTSEVPNNTEQNEVELTVQPSSDNAKTEEKKVRQRLLDSSC
Protein: Sulfite reductase [ferredoxin], chloroplastic (PsSiR) (EC 1.8.7.1) (Q75NZ0)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: Essential protein with sulfite reductase activity required in assimilatory sulfate reduction pathway during both primary and secondary metabolism and thus involved in development and growth.
Subcellular location: Plastid, chloroplast stroma, chloroplast nucleoid. Plastid, chloroplast stroma. Plastid stroma.
Interaction partners:
Sequence:
MTTSFAAAALRDPKLQIPNYHGLRSSSAASSLSRNALSVPSSTRSSSLIRAVSTPAKSETATEKKRSKVEIFKEQSNFIRYPLNEDMLTDAPNLSEAATQLIKFHGSYQQYNRDERGSRTYSFMIRTKNPCGKVSNQLYLTMDDLADQFGIGTLRLTTRQTFQLHGVVKKDLKTVMGSIIRNMGSSLGACGDLNRNVLAPAAPIVSKDYLFAQETSENIAALLTPQSGFYYDVWVDGERFMSAEPPEVIQARNDNSHGTNFTDSPEPIYGTQFLPRKFKIAVTVPTDNSVDILTNDIGVVVVTGDGGEPQGFNLYVGGGMGRTHRMETTFPRLAEPLGYVPKEDILYAVKAIVVTQRENGRRDDRRYSRMKYLIDSWGIDKFRNVVEEYYGKKFEPFRSLPEWEFKSYLGWHQQGDGGLFCGLHVDNGRIAGKMKTALREVIEKYHLNVRLTPNQNLILTDIRAAWKRPITTILSQAGLLLPRYVDPLNITAMACPAFPLCPLAITEAERGIPSILKRIRDMFEKVGLKYNESVVVRITGCPNGCARPYMAELGLVGDGPNSYQIWLGGSSNQTSIARSFMDKVKPQDLEKVLEPLFYHWKQKRQSKESFGDFTVRLGFEKLKEFIEKWEGPAVPPTRHNLKLFTDKDTYEAMDGLAKLQNKNAHQLAMEVVRNYIASNLNGKGE