wanglab/gogpt-training-data huggingface dataset:
Protein: Jacalin-related lectin 33 (O04311)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sugar-binding protein showing significant affinity for (Glc alpha(1-4)Glc)(3) maltohexaose, (Glc alpha(1-6)Glc)(3) isomaltohexaose, Gal alpha(1-4)Gal beta(1-4)Glc, GalNAc alpha(1-3)(Fuc alpha(1-2)) and Gal beta(1-3)(Fuc alpha(1-4))GlcNAc beta(1-3)Gal beta(1-4)Glc.
Interaction partners:
- AAA-ATPase At3g28600
- Beta-glucosidase 23
- GDSL esterase/lipase 22
- 1-aminocyclopropane-1-carboxylate oxidase homolog 4
- 1-aminocyclopropane-1-carboxylate oxidase homolog 9
- Pentatricopeptide repeat-containing protein At1g79490, mitochondrial
- Ulp1 protease family protein
- Protein-S-isoprenylcysteine O-methyltransferase A
- TSA1-like protein
- Glucosidase 2 subunit beta
Sequence:
MAQKVEAGGGAGGASWDDGVHDGVRKVHVGQGQDGVSSINVVYAKDSQDVEGGEHGKKTLLGFETFEVDADDYIVAVQVTYDNVFGQDSDIITSITFNTFKGKTSPPYGLETQKKFVLKDKNGGKLVGFHGRAGEALYALGAYFATTTTPVTPAKKLSAIGGDEGTAWDDGAYDGVKKVYVGQGQDGISAVKFEYNKGAENIVGGEHGKPTLLGFEEFEIDYPSEYITAVEGTYDKIFGSDGLIITMLRFKTNKQTSAPFGLEAGTAFELKEEGHKIVGFHGKASELLHQFGVHVMPLTN
Protein: Ataxin 3 (G3V2G2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIRVQQMHRPKLIGEELAQLKEQRVHKTDLERVLEANDGSGMLDEDEEDLQRALALSRQEIDMEDEEADLRRAIQLSMQGSSRNISQDMTQTSGTNLTSEELRKRREAYFEKQQQKQQQQQQQQQQGDLSGQSSHPCERPATSSGALGSD
Protein: Radial spoke head protein 9 homolog (Q8T3V7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, kinocilium {ECO:0000256|ARBA:ARBA00037822}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
- GH13165p
- AT19426p
- GH13213p
- Dynein, axonemal, intermediate chain 2, isoform C
- AP complex subunit beta
- AP-1 complex subunit gamma
- Spag1 axonemal dynein assembly factor
- Putative inner dynein arm light chain, axonemal
- AT09290p
- Dynein axonemal assembly factor 5
Sequence:
MNLEFFTEGLDCLMYCGMKLSPEQRILIENSLIALQNDNRFTGMYLWGRITATKNDYYIAFGYTNDCLKDRKYFYSLDQFQWQLLPFVQSPKIFQATILAREPFIGDPSLMTYVKLDPTFDIVGNQVAGISRPEVVKLKEEERLAAIVFIITEECAICPRGAFYKMTDGRVIPNQMFRGLNDLQIDNQSYYQLYRLPRNDLKVNLAKRSDYNYAIDFLDTIDCVIPLCQAFALNMQRNEGLVIIKSCLWLGMTFFHKINSHKHGFLYLGDGKKNFDLLFMY
Protein: Nuclear pore complex protein Nup85 (J3QLV0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nuclear pore complex {ECO:0000256|ARBA:ARBA00004567, ECO:0000256|RuleBase:RU365073}.
Interaction partners:
Sequence:
LDWVRLHVCEVDSLSADVLGSENPSKHDSFWNLGRLDEARQMLSKEADASPASAGICRIMGDLMRTMPILSPGNTQTLTELELKWQHWHEECERYLQDSTFATSPHLESLLKIMLGDEAALLEQKELLSNWYHFLVTRLLYSNPTVKPIDLHYYAQSSLDLFLGGESSPEPLDNILLAAFEFDIHQVIKEC
Protein: Cation/acetate symporter ActP (Acetate permease) (Acetate transporter ActP) (P32705)
Organism: Escherichia coli (strain K12)
Function: Transports acetate. Also able to transport glycolate.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:16079137}; Multi-pass membrane protein {ECO:0000269|PubMed:16079137}.
Interaction partners:
- Inner membrane protein YjcH
- Acetyl-coenzyme A synthetase
- Succinate-acetate/proton symporter SatP
- Fatty acid oxidation complex subunit alpha
Sequence:
MKRVLTALAATLPFAANAADAISGAVERQPTNWQAIIMFLIFVVFTLGITYWASKRVRSRSDYYTAGGNITGFQNGLAIAGDYMSAASFLGISALVFTSGYDGLIYSLGFLVGWPIILFLIAERLRNLGRYTFADVASYRLKQGPIRILSACGSLVVVALYLIAQMVGAGKLIELLFGLNYHIAVVLVGVLMMMYVLFGGMLATTWVQIIKAVLLLFGASFMAFMVMKHVGFSFNNLFSEAMAVHPKGVDIMKPGGLVKDPISALSLGLGLMFGTAGLPHILMRFFTVSDAREARKSVFYATGFMGYFYILTFIIGFGAIMLVGANPEYKDAAGHLIGGNNMAAVHLANAVGGNLFLGFISAVAFATILAVVAGLTLAGASAVSHDLYANVFKKGATEREELRVSKITVLILGVIAIILGVLFENQNIAFMVGLAFAIAASCNFPIILLSMYWSKLTTRGAMMGGWLGLITAVVLMILGPTIWVQILGHEKAIFPYEYPALFSITVAFLGIWFFSATDNSAEGARERELFRAQFIRSQTGFGVEQGRAH
Protein: Interferon gamma (IFN-gamma) (C6KJC5)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|PIRNR:PIRNR001936}.
Interaction partners:
Sequence:
MTCQTYNLFVLSVIMIYYGHTASSLNLVQLQDDIDKLKADFNSSHSDVADGGPIIVEKLKNWTERNEKRIILSQIVSMYLEMLENTDKSKPHIKHISEELYTLKNNLPDGVKKVKDIMDLAKLPMNDLRIQRKAANELFSILQKLVDPPSFKRKRSQSQRRYNC
Protein: Arfaptin (LD44124p) (Q9VGQ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- ADP-ribosylation factor-like protein 1
- ADP-ribosylation factor 6
- Rho GTPase activating protein at 18B, isoform C
Sequence:
MTDRERSIHEMLKDAPSLNDSCGAVHTGTEGGSGILGSASSHSIAGGGGGGGNVGVGVGGPFGAPSSLPLRNHSAPTTPMSPSSPPSGNGILSPTDSGSGSIIRTSASKIDSLKNWSISTYKCTRQIMLEKLGKSQRTVDSELEAQIEQLRETQRKYLSILRLTRAFSSHFQHVVVTQHALADSFADLAQKNPELQKEFTCNSETQRNLTKNGELLLNALNFFISSVNTLCNKTIDDTLLTIRQYETARIEFDAYRMDLENTKPELTPSAVALEETQRSYAQHKEQYEKLRSDVAVKMQFLDENRIKVMHKQLILLHNAIAAYFSGNAMALESTLKQFNIKLKSPNAVTGSWLEQ
Protein: Phospholipase B-like 1 (EC 3.1.1.-) (LAMA-like protein 1) (Lamina ancestor homolog 1) (Phospholipase B domain-containing protein 1) [Cleaved into: Phospholipase B-like 1 chain A; Phospholipase B-like 1 chain B; Phospholipase B-like 1 chain C] (Q6P4A8)
Organism: Homo sapiens (Human)
Function: In view of the small size of the putative binding pocket, it has been proposed that it may act as an amidase or a peptidase (By similarity). Exhibits a weak phospholipase activity, acting on various phospholipids, including phosphatidylcholine, phosphatidylinositol, phosphatidylethanolamine and lysophospholipids.
Subcellular location: Lysosome {ECO:0000250}.
Interaction partners:
Sequence:
MTRGGPGGRPGLPQPPPLLLLLLLLPLLLVTAEPPKPAGVYYATAYWMPAEKTVQVKNVMDKNGDAYGFYNNSVKTTGWGILEIRAGYGSQTLSNEIIMFVAGFLEGYLTAPHMNDHYTNLYPQLITKPSIMDKVQDFMEKQDKWTRKNIKEYKTDSFWRHTGYVMAQIDGLYVGAKKRAILEGTKPMTLFQIQFLNSVGDLLDLIPSLSPTKNGSLKVFKRWDMGHCSALIKVLPGFENILFAHSSWYTYAAMLRIYKHWDFNVIDKDTSSSRLSFSSYPGFLESLDDFYILSSGLILLQTTNSVFNKTLLKQVIPETLLSWQRVRVANMMADSGKRWADIFSKYNSGTYNNQYMVLDLKKVKLNHSLDKGTLYIVEQIPTYVEYSEQTDVLRKGYWPSYNVPFHEKIYNWSGYPLLVQKLGLDYSYDLAPRAKIFRRDQGKVTDTASMKYIMRYNNYKKDPYSRGDPCNTICCREDLNSPNPSPGGCYDTKVADIYLASQYTSYAISGPTVQGGLPVFRWDRFNKTLHQGMPEVYNFDFITMKPILKLDIK
Protein: Common salivary protein 1 (M0R7K9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Prolactin-inducible protein homolog
- BPI fold containing family A, member 2F
Sequence:
MFQLEAMLPLLILAFLGTPAVLTQSRYHGSETGKHFCIVAPEGEPVTGIWASLKNNILSSIRLKFGNNWSQEYGSSGRAEIEVKLNPDETVLGFSGSFYIFMHQIIITTSQPRELIIGPLTGRYVYTSYPENPNHVFRGICGYYVTGGLKGMRYLWGNVNGTCTE
Protein: Calreticulin (CRP55) (Calregulin) (Endoplasmic reticulum resident protein 60) (ERp60) (HACBP) (grp60) (P27797)
Organism: Homo sapiens (Human)
Function: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:10358038, ECO:0000269|PubMed:11149926}. Cytoplasm, cytosol {ECO:0000269|PubMed:11149926}. Secreted, extracellular space, extracellular matrix {ECO:0000305}. Cell surface {ECO:0000269|PubMed:10358038}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P28491}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000250|UniProtKB:Q8K3H7}. Cytolytic granule {ECO:0000269|PubMed:8418194}. Note=Also found in cell surface (T cells), cytosol and extracellular matrix (PubMed:10358038). During oocyte maturation and after parthenogenetic activation accumulates in cortical granules. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex (By similarity). In cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation (By similarity). {ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7, ECO:0000269|PubMed:8418194}.
Interaction partners:
- Tapasin
- Beta-2-microglobulin
- Protein disulfide-isomerase A3
- Calnexin
- Endoplasmin
- Prolow-density lipoprotein receptor-related protein 1
- HLA class I histocompatibility antigen, A alpha chain
- Endoplasmic reticulum chaperone BiP
- Protein disulfide-isomerase
- Thrombospondin-1
Sequence:
MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDEEKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQTDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL
Protein: Wall-associated receptor kinase 1 (EC 2.7.11.-) (Q39191)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein kinase that may function as a signaling receptor of extracellular matrix component. Binding to pectin may have significance in the control of cell expansion, morphogenesis and development. Required during plant's response to pathogen infection and in plant defense against heavy metal toxicity. Phosphorylates the oxygen-evolving enhancer protein 2 (OEE2) in an GRP-3-dependent manner.
Subcellular location: Membrane {ECO:0000269|PubMed:8702686}; Single-pass type I membrane protein {ECO:0000269|PubMed:8702686}.
Interaction partners:
- Glycine-rich protein 3
- Precursor of elicitor peptide 1
- Protein phosphatase 2C 70
- Peroxiredoxin-2F, mitochondrial
- Protein LURP1
- Elongation factor Tu, chloroplastic
Sequence:
MKVQEGLFLVAIFFSLACTQLVKGQHQPGENCQNKCGNITIEYPFGISSGCYYPGNESFSITCKEDRPHVLSDIEVANFNHSGQLQVLLNRSSTCYDEQGKKTEEDSSFTLENLSLSANNKLTAVGCNALSLLDTFGMQNYSTACLSLCDSPPEADGECNGRGCCRVDVSAPLDSYTFETTSGRIKHMTSFHDFSPCTYAFLVEDDKFNFSSTEDLLNLRNVMRFPVLLDWSVGNQTCEQVGSTSICGGNSTCLDSTPRNGYICRCNEGFDGNPYLSAGCQDVNECTTSSTIHRHNCSDPKTCRNKVGGFYCKCQSGYRLDTTTMSCKRKEFAWTTILLVTTIGFLVILLGVACIQQRMKHLKDTKLREQFFEQNGGGMLTQRLSGAGPSNVDVKIFTEDGMKKATNGYAESRILGQGGQGTVYKGILPDNSIVAIKKARLGDSSQVEQFINEVLVLSQINHRNVVKLLGCCLETEVPLLVYEFITNGTLFDHLHGSMIDSSLTWEHRLKIAIEVAGTLAYLHSSASIPIIHRDIKTANILLDVNLTAKVADFGASRLIPMDKEELETMVQGTLGYLDPEYYNTGLLNEKSDVYSFGVVLMELLSGQKALCFKRPQSSKHLVSYFATATKENRLDEIIGGEVMNEDNLKEIQEAARIAAECTRLMGEERPRMKEVAAKLEALRVEKTKHKWSDQYPEENEHLIGGHILSAQGETSSSIGYDSIKNVAILDIETGR
Protein: Sperm associated antigen 9 (A0A8I6B484)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MNPGCMLLFVFGFVGGAVVINSAILVSLSVLLLVHFSISTGVPALTQNLPRILRKERPISLGIFPLPAGDGLLTPDTQKGGETPGSEQWKFQELSQPRSHTSLKDELSDISQGGSKATTPASTANSDVSAIPPDTPSKEDNEGLVKGTDTPNKAEISKHIEVQVAQETRNVSTDSAENEEKSEVQAIIESTPELDMDKDLSGYKGSSTPTKGIENKAFDRNTESLFEELSSAGSGLIGDVDEGADLLDHSFFGMGREVENLILENTQLLETKNALNVVKNDLIAKVDELTCEKDVLQGELEAVKQAKLKLEEKNRELEEELRKARAEAEDARQKAKDDDDSDIPTAQRKRFTRVEMARVLMERNQYKERLMELQEAVRWTEMIRASRENPAMQEKKRSSIWQFFSRLFSSSSNAAKKPEPPVNLKYNAPTSHVTPSVKKRSSTLSQLPGDKSKAFDFLSEETEASLASRREQKREQYRQVKAHVQKEDGRVQAFGWSLPQKYKQVANGQGENKMKNLPVPVYLRPLDEKDASMKLWCAVGVNLSGGKTRDGGSVVGASVFYKDVSALESEGSKQRSASQSSLDKLDQELKEQQKELKNQEELSSQVWICTSTHSTTKVIIIDAVQPGNILDSFTVCNSHVLCIASVPGARETDYPAGEELSDSGQVDRASLCGSMTSNSSAEMDSLLGGITVVGCSTEGVTGAAASPSTNGASPVIEKPPEVEAENSEIDENIPTAEEATEATEGNAGSTEDAVDISQPGVYTEHVFTDPLGVQIPEDLSPVFQSSNDSDVYKDQISVLPNEQDLAREEAQKMSSLLPTMWLGAQNGCLYVHSSVAQWRKCLHSIKLKDSILSIVHVKGIVLVALADGTLAIFHRGLDGQWDLSNYHLLDLGRPHHSIRCMTVVHDKVWCGYRNKIYVVQPKAMKIEKSFDAHPRKESQVRQLAWVGDGVWVSIRLDSTLRLYHAHTYQHLQDVDIEPYVSKMLGTGKLGFSFVRITALMVSCNRLWVGTGNGVIISIPLTETNKTSGTPGNRPGSVIRVYGDENSDKVTPGTFIPYCSMAHAQLCFHGHRDAVKFFVAVPGQVVSPQSSSSGADLTADKAGSSAQEPSSQTPLKSMLVISGGEGYIDFRMGDEGGESELLGEDLPLEPSVTKAERSHLIVWQVMCGNE
Protein: Galactose-1-phosphate uridylyltransferase isoform 2 (A0A0S2Z4I0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRSGTDPQQRQQASEADAAAATFRANDHQHIRYNPLQDEWVLVSAHRMKRPWQGQVEPQLLKTVPRHDPLNPLCPGAIRANGEVNPQYDSTFLFDNDFPALQPDAPSPGPSDHPLFQAKSARGVCKVMCFHPWSDVTLPLMSVPEIRAVVDAWASVTEELGAQYPWVQGVVRRELTWCLLANRAPYPYLIDL
Protein: Malic enzyme (Q2QBM1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKPDSKLDKYAQRDRLGLWGTGDNEVVGSLSGFTRLLDKRYSKGLAFTHEERQQLGIHGMLPYVVREPSEQVEHCRALLARLDQDLDKYMYLISLSERNERLFYNVLSSDIAYMMPLVYTPTVGLACQRYSLIHQNAKGMFISIKDKGHIYDVLKNWPETDVRAIVVTDGERILGLGDLGANGMGIPVGKLSLYTALAGIKPSQCLPITLDVGTNTESILEDPLYIGLRERRATGDLYDEFIDEFMHACVRRFGQNCLIQFEDFANANAFRLLSKYRDSFCTFNDDIQGTASVAVAGLLASLKIKKTQLKDNTLLFLGAGEAALGIANLCLMAMKVEGLTEEEAKARIWMVDSRGVITRDRPKGGLTEHKLHFAQLHEPIDTLAEAVRKVRPNVLIGAAAQGGAFNQEILELMADINETPIIFALSNPTSKAECTAEEAYTYTKGRCIFASGSPFAPVTYNNKKFYPGQGNNSYIFPGVALGVLCAGMLNIPEQVFLVAAERLAELVSKDDLAKGSLYPPLSSIVSCSMAIAERIVEYAYKNGLATVRPEPVNKLAFIKAQMYDLDYPRSVPATYKM
Protein: Synaptopodin 2-like b (A0A2R8RTS6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MRSFTLPGEVEHEGHIYAELHRGESLQDKQVKEARSKCRTIASLLTDAPNPHSKGVLMFKKRRQRAKKYTLTCFGSVDGESNSNTEGETEDESLFPGSESELDEDGFSAAPDPTWDSGYLDVLDKRTSACIVPDREAEISPGLNATSGKGAQLFEQQRKRAEEHVSNLNTFSMPQHQGDSTLTYTPVAPYTPQSTSSLSTSMVNGEPLVVSRTSVVLSSPGQTPMPSLTGALPEQIDSSAASSVHNRTARPFAPGCVSNRAATAPVVFRPSPAKKAGSQSQAVSVATLPAAFSPVVSEGKKAISTSSLYIPARPATYNGPSSLLSPSSVISSPFSPPPSNAPLYSPTYSSTSAPFSPTTSHVTSLSLPSGMAQTYSQPQAMPFSPPHPTVSSQFQPPPPVNVPAQPFSSSFMNAPGFPNVPVHPPTSLNMQPSPSHKVSFNPYISVASTTPETPNAPIAQQYPLSNSTDGISSREQRLSVPAGRTGILQEACRRSTKKPMFSAQEEKKAPSFNPELLSLVQNFDDRSRSGVEAGFESGPEEDFLNLGAEACNFMQAQKNRLPPPVAPKPGHPAPEMPQMRGKGAELFARRQSRMDRYVVDKQPKSPAQPRDPSPTPSLPGNWKYSPNIRAPPPINYNPLLSPSCPLVAQRSTKANDATKVGVKTMHGHNKQGIKALDFVSKQPYQLNPSLFSYGANPQNNTTCQQQQQNGVGITGQFLNPPKQVPIKAGRVYEIKRFSTPTPMSAPTSLTPTVIAPRSATTLGEPMWRSDVTSPPPVAPRPAAPFSPPPPAPTAALPALPKISSAANSGPITQPNQGQAYTPFQTAKQFKSAPELSPLSAGVRSSGSASGLNLRVPRPRFCTSSMGLQPNVWRPGSIHY
Protein: Pro-adrenomedullin [Cleaved into: Adrenomedullin (AM); Proadrenomedullin N-20 terminal peptide (ProAM N-terminal 20 peptide) (PAMP) (ProAM-N20)] (P35318)
Organism: Homo sapiens (Human)
Function: AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels.
Subcellular location: Secreted {ECO:0000269|PubMed:8387282}.
Interaction partners:
- Receptor activity-modifying protein 3
- Receptor activity-modifying protein 2
- Calcitonin gene-related peptide type 1 receptor
- Receptor activity-modifying protein 1
- Islet amyloid polypeptide
- Calcitonin receptor
- Calcitonin gene-related peptide 2
- Calcitonin
- G-protein coupled receptor 182
- Mas-related G-protein coupled receptor member X2
Sequence:
MKLVSVALMYLGSLAFLGADTARLDVASEFRKKWNKWALSRGKRELRMSSSYPTGLADVKAGPAQTLIRPQDMKGASRSPEDSSPDAARIRVKRYRQSMNNFQGLRSFGCRFGTCTVQKLAHQIYQFTDKDKDNVAPRSKISPQGYGRRRRRSLPEAGPGRTLVSSKPQAHGAPAPPSGSAPHFL
Protein: DNA polymerase alpha subunit B (DNA polymerase alpha 70 kDa subunit) (P33611)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis (By similarity). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, an accessory subunit POLA2 and two primase subunits, the catalytic subunit PRIM1 and the regulatory subunit PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1 (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- DNA primase large subunit
- DNA primase small subunit
- DNA polymerase alpha catalytic subunit
- DNA polymerase delta catalytic subunit
- DNA polymerase delta subunit 2
- DNA polymerase epsilon subunit 2
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase zeta catalytic subunit
- DNA replication licensing factor MCM4
- Replication factor C subunit 3
Sequence:
MAVSTQQLAEELQIFGLDYEDSLLEKLAELCVLYRQTEDGMVSELIAFCTSAGKTCLTVDILNSFEYEVLNKKLSKAWHSASKDSGHAGTRDIVSIQELIEAEEEEETLLSSYTTPSKGPLKRVSSTPETPLTKRSVAARSPRQLLSPSSFSPSATPSQKYTSRTNRGEVVTTFGSAQGLSWSGRGGSGSVSLKVVGDPEPLTGSYKAMFQQLMGVREVLTSKIEELGSELKEHHKIEAFTPLLVPAQEPVILLGQIGCDSNGKLNSKSVILEGDQEHSYGAQIPVDLSELKEYSLFPGQVVIMEGFNTTGRRLTATKLYEGVPLPFYQPTEEEGASEQTMVVVACGPYTTSDSITYDPLLDLIAIINRDQPDVCILFGPFLDAKHEQVENCKLTSPFEDVFKQCLRTVIEGTRSSGSHLVFVPSLRDVHHEPVYPQPPFTFSELSREDKKRVQFVSEPCSLSINGVMFGLTSTDLLFHIGAEEIFSSSGTSDRFSRVLKHILTQRSYYPLYPPHEDMAIDYENFYTYAQLPVTPDVFIVPSELRYFVKDIFGCVCVNPGRLTKGQVGGTFGRLYLRRQPKAMDGGGRQGLSVAAQVVRI
Protein: Serine/threonine-protein kinase sck1 (EC 2.7.11.1) (P50530)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Protein kinase that is part of growth control pathway which is at least partially redundant with the cAMP pathway. Required for trehalase activation.
Interaction partners:
- Serine/threonine-protein kinase tor2
- Serine/threonine-protein kinase tor1
- Target of rapamycin complex 1 subunit mip1
- Serine/threonine-protein kinase cek1
- Serine/threonine-protein kinase ppk18
- Serine/threonine-protein kinase sck2
- Mitogen-activated protein kinase spm1
- Target of rapamycin complex subunit wat1
- Serine/threonine-protein kinase ksg1
- cAMP-dependent protein kinase catalytic subunit
Sequence:
MTEIFGKLHRSSNSENTNQASPSTIQSHSTQPVLSNDHSTKVNDYEGKEGASSNGYDPVFMSDRMKMRYNEITAQLHKEQSLKEDKESGSNSSESNGITPMGTYSEKPKLLQSRTPPSSCYIRHDTVVPKDKNGQHAFGRLYVRLHQGRDLNVKSVNAQPYAVITFEKTQVMVPPPFKDIDGGIPISIPSKNRPLAGSASGSSSGLHSELMLADVRCPHWDFETVFDVTKMKSQMVVSVYDKYEDDKFLGSVKITPIFLHEYVQEAWYKLEPLDLTKSLEGEIKVETIYEHIEHVRYGPEDFTALRLIGKGTFGQVYLVRKNDTNRIYAMKKISKKLIVRKKEVTHTLGERNILVRTSLDESPFIVGLKFSFQTASDLYLITDYMSGGELFWHLQHEGRFPEQRAKFYIAELVLALEHLHKHDIIYRDLKPENILLDADGHIALCDFGLSKANLSANATTNTFCGTTEYLAPEVLLEDKGYTKQVDFWSLGVLVFEMCCGWSPFYAPDVQQMYRNIAFGKVRFPKGVLSSEGRSFVRGLLNRNPNHRLGAVADTTELKEHPFFADINWDLLSKKKVQPPFKPNVQNDLDVSNFDKEFTNTNVKNINIVSNVDPANASTPLSNTIQDRFRGFTFVNKSIDEQFQNLGLQENEETDNLHACRTTTHSSVNSINSHGNPRTVDANDPVADTVFGETFEA
Protein: Uncharacterized protein (Q38DN4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MADVSADSDAQVELERLNDVIDKYTCQVEHIDNLLQELEEENNSDSVSRQIAEYQSALESHPENIPAEDALEVITRLENTLKIVQRRNHLLEKENGTQNRLLEERSNVLLNATKTFDHIVDVTGWHDKFLFDAEDLRSKVADIREMSNIEAVVQKELRVAQGIIKKKEAALRQLEELVEQGKEQEAVLNNVYNDIRVKERDCSEVEMQLVRLRKSVAKTDEALAVFDLHNQNASLAYMESDRDYLRDSVAEMKSTTRRQDNVIKAQLTRQQQLQTRLDVIMKSLREMKLDKKYERNIPKSALVPSASREEPEDVSKILPESECIPVPTYRLLHKNNEMLRVIVMRKNMLVLEKNAVIEALEAGLAKYGSALITTYKEQQDLRQNKDMELIELMDDLQQQHSNYLEKLEELRLQNAALKKKMYRSTRQHAPLKGTRPMR
Protein: KIAA0355 protein (A1A512)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGEHNLLNPKAIEASLQGCCSEAEAQQTGRRQTPPQPMQCELPTVPVQIGSHFLKGVSFNESAADNLKLKTHTMLQLMKEAGCYNGITSRDDFPVTEVLNQVCPSTWRGACKTAVQLLFGQAGLVVVDTAQIENKEAYAPQISLEGSRIVVQVPSTWCLKEDPATMSLLQRSLDPEKTLGLVDVLYTAVLDLNRWRAGREQALSFF
Protein: dihydropyrimidinase (EC 3.5.2.2) (Q9V3N7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSTSPKPVKKVPIHLQSAQNRVYIKNGEIVNHDKSFKADVYIEDGIIKFVGPSSEITIPGGVRTIDASGLMIIPGGIDPHTHMQLPFGGAVAVDDFYHGTKAAVAGGTTMIIDFVLPNKHESMIEAYDKWRSWADPKVCCDYGLHVGITWWSKSVSEEIGILCKELGVNSFKTFMAYKGLYQLNDSDLLDVFERIRHLNGVAMVHAENGDIIAKNTQRLLAEGINGPEGHELSRPEEVEAEAVHRACVLAHQMKTPLFVSGLTSKSSAELVGRARRSGYCVFGETLASSLGRSMSAVPKGDRIYAITSPPIRESAETPRQLMKSLAYDDLQLTGSDNCTFNKEHKALGKGDFTKIPNGVNGVEDRMSLVWEKGVHAGLLDPCRFVAVTSTNAAKIFNIYPQKGRIAVGSDADIVIWNPNATRTISKDTHHHACDFNIFEGMTVHGVCEFVLVRGRICAERGNVRVAEGFGRFIPTPVRPPFVYDIIEGKVQSQPEEQHEEKQNGSMAKRFAELDIQIPVQEPISAMLAGNLAMPAEGSLCSTPSVRGRVDGKRDLQESSFSISEELDRSGVRACIKVKNPPGGKSSGFW
Protein: FA core complex associated protein 24 (K7EKQ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSEQYFPALQKFTVLDLGMVLLPVASQMEASCLVIQLVQEQTKEPSKNPLLGKKRALLLSEPSLLRTVQQIPGVGKVKAPLLLQKFPSIQQLSNASIGELEQVVGQAVAQQIHAFFTQPR
Protein: At3g15900 (Homoserine O-acetyltransferase) (Q9LSC1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cystathionine beta-lyase, chloroplastic
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- Homocysteine S-methyltransferase 3
- Aspartokinase 3, chloroplastic
- Aspartokinase 2, chloroplastic
- Aspartokinase 1, chloroplastic
Sequence:
MSGSVFVPGMAIGVPTLSRSSSVHRSLEPTKKMTMSSVKFVTSFRNPSNCSGTKRSFRVMASDDRSEQADNGQGIQEDLNYLLKIGVGSVAGAAIIKYGSVLFPQITRPNLTLALFIIIAPVVISVILLSLSSSSSSKKQN
Protein: UDP-glycosyltransferase 76C1 (EC 2.4.1.-) (Cytokinin-N-glucosyltransferase 1) (Q9FI99)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the N-glucosylation of cytokinins. Catalyzes the formation of both the 7-N and the 9-N-glucosides.
Interaction partners:
- UDP-glycosyltransferase 76C2
Sequence:
MEKRNERQVILFPLPLQGCINPMLQLAKILYSRGFSITIIHTRFNAPKSSDHPLFTFLQIRDGLSESQTQSRDLLLQLTLLNNNCQIPFRECLAKLIKPSSDSGTEDRKISCVIDDSGWVFTQSVAESFNLPRFVLCAYKFSFFLGHFLVPQIRREGFLPVPDSEADDLVPEFPPLRKKDLSRIMGTSAQSKPLDAYLLKILDATKPASGIIVMSCKELDHDSLAESNKVFSIPIFPIGPFHIHDVPASSSSLLEPDQSCIPWLDMRETRSVVYVSLGSIASLNESDFLEIACGLRNTNQSFLWVVRPGSVHGRDWIESLPSGFMESLDGKGKIVRWAPQLDVLAHRATGGFLTHNGWNSTLESICEGVPMICLPCKWDQFVNARFISEVWRVGIHLEGRIERREIERAVIRLMVESKGEEIRGRIKVLRDEVRRSVKQGGSSYRSLDELVDRISIIIEPLVPT
Protein: NAD(P)H-hydrate epimerase (EC 5.1.99.6) (NAD(P)HX epimerase) (Q6FT51)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03159}. Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03159}.
Interaction partners:
- ATP-dependent RNA helicase DHH1
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome B complete sequence
- ATP-dependent
- pyridoxal 5'-phosphate synthase
- Candida glabrata strain CBS138 chromosome M complete sequence
Sequence:
MSALKVVSSKLAAEIDQELMGPQVGFTLQQLMELAGFSVAQAVSREFPLSSKLNDNKHVFVIAGPGNNGGDGLVCARHLKLFGYNPIVFYPKRSERTEFYKQLVHQLNFFKVPVLGQDDDETRWLSYLEPEKTLCIVDAIFGFSFKPPMREPFQSIMSQLKKIENDIPIISVDVPTGWDVDEGPISEQCIVPKVLVSLTVPKLCSNYLKEKTTKHYVGGRFVPRDFANKYGFEPFAYEGTDQVLKL
Protein: Defective in cullin neddylation protein (M9MRX5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAERHIRLEDGFSQKRCMAWFQEYTTPDEPETLGPDGMEKFCEDIGVEPENIVMLVLAYKMGATQMGFFSQQEWLKGLTELDCDSAAKMVVKLDYLRSILNDPNSFKSIYRYAYDFAKDSDQRCMDILTAKAMLQLLLGKHWPLYPQFAQFLEQSKYKAINKDQWCNILEFSRTISIDLSNYDIDGAWPVMLDEFVEWLRLQRSQVTSTTGSS