wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 56 kDa subunit (EC 2.4.1.15) (General glucose sensor subunit 1) (Glycogen metabolism control protein GLC6) (Trehalose synthase complex catalytic subunit TPS1) (Trehalose-6-phosphate synthase) (UDP-glucose-glucosephosphate glucosyltransferase) (Q00764)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Synthase catalytic subunit of the trehalose synthase complex that catalyzes the production of trehalose from glucose-6-phosphate and UDP-alpha-D-glucose in a two step process. Can function independently of the complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Trehalose synthase complex regulatory subunit TSL1
- Trehalose-phosphatase
- Trehalose synthase complex regulatory subunit TPS3
- Glycogen [starch] synthase isoform 2
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen [starch] synthase isoform 1
- 1,4-alpha-glucan-branching enzyme
- Glycogenin-1
- Probable UTP--glucose-1-phosphate uridylyltransferase
- Glycogenin-2
Sequence:
MTTDNAKAQLTSSSGGNIIVVSNRLPVTITKNSSTGQYEYAMSSGGLVTALEGLKKTYTFKWFGWPGLEIPDDEKDQVRKDLLEKFNAVPIFLSDEIADLHYNGFSNSILWPLFHYHPGEINFDENAWLAYNEANQTFTNEIAKTMNHNDLIWVHDYHLMLVPEMLRVKIHEKQLQNVKVGWFLHTPFPSSEIYRILPVRQEILKGVLSCDLVGFHTYDYARHFLSSVQRVLNVNTLPNGVEYQGRFVNVGAFPIGIDVDKFTDGLKKESVQKRIQQLKETFKGCKIIVGVDRLDYIKGVPQKLHAMEVFLNEHPEWRGKVVLVQVAVPSRGDVEEYQYLRSVVNELVGRINGQFGTVEFVPIHFMHKSIPFEELISLYAVSDVCLVSSTRDGMNLVSYEYIACQEEKKGSLILSEFTGAAQSLNGAIIVNPWNTDDLSDAINEALTLPDVKKEVNWEKLYKYISKYTSAFWGENFVHELYSTSSSSTSSSATKN
Protein: Itgb2 protein (Q4KLK5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGVPIPGADLSATLPHHTRCESGYIGKNCECQTQGRSSQELEGNCRKDNSSIVCSGLGDCICGQCVCHTSDIPNKVIFGQYCECDNFNCERYDGQVCGGLKRGSCSCGQCNCKEGFEGSACQCQRSTTGCLNARLVECSGRGRCQCNRCICEKGYQPPLCEECPGCPLPCSTYVFCAECLKFDKGPFQKNCSVQCANVTLQTVPFKKKPCKERDSEGCWITYTLQQKDGNAYNIHVDDDRECVKGPNVAAIIGGTVAGVVLIGVLLLVIWKALTHLTDLNEYRRFEKEKLKSQWNNDNPLFKSATTTVMNPKFAES
Protein: Lymphocyte transmembrane adapter 1 (Linker for activation of X cells) (Membrane-associated adapter protein LAX) (Q8BHB3)
Organism: Mus musculus (Mouse)
Function: Negatively regulates TCR (T-cell antigen receptor)-mediated signaling in T-cells and BCR (B-cell antigen receptor)-mediated signaling in B-cells.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.
Interaction partners:
- T-cell receptor-associated transmembrane adapter 1
- Ras-related protein Rab-8A
- Growth factor receptor-bound protein 2
Sequence:
MYSTPAPPEVTRRNSEPSTRQGTLGSLQGEKGQIIFPGFVVLLTIILVIIAACILWSWKKQKKRPVPYFQVAPSLTLPPPRHRAKNIYDFLPRQQTELGRHQLSGFSTESLLSRASDSPEPEAPQANGSLQMHRVSVHTVEYSVNIYDNGTVPQMCRHLASSTHHVCVRTSRSNPSISSKESNDYVNIPTVEDTCETLTRIESTPENHLGLPSALRLEFAEGGHAGCGNATDHDGFWAPGPKCSDSLSDGDDLSQTSNDYVNMTGLDLENIQENRPRGAFQCCRDYENVPWVDTNESQLPTLEEVASSTVDHREPVWRTLSSVYHMAFQPSAQSEDSAMVHREEQSSEDSSDYETVLVAELEGRDWKQGPGTQHPSDEGTPGDLAGKLCEVVYPAGSLATETSDEDA
Protein: AP-4 complex subunit beta-1 (AP-4 adaptor complex subunit beta) (Adaptor-related protein complex 4 subunit beta-1) (Beta subunit of AP-4) (Beta4-adaptin) (Q9WV76)
Organism: Mus musculus (Mouse)
Function: Component of the adaptor protein complex 4 (AP-4). Adaptor protein complexes are vesicle coat components involved both in vesicle formation and cargo selection. They control the vesicular transport of proteins in different trafficking pathways. AP-4 forms a non clathrin-associated coat on vesicles departing the trans-Golgi network (TGN) and may be involved in the targeting of proteins from the trans-Golgi network (TGN) to the endosomal-lysosomal system (By similarity). It is also involved in protein sorting to the basolateral membrane in epithelial cells and the proper asymmetric localization of somatodendritic proteins in neurons. AP-4 is involved in the recognition and binding of tyrosine-based sorting signals found in the cytoplasmic part of cargos, but may also recognize other types of sorting signal (By similarity).
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q9Y6B7}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y6B7}.
Interaction partners:
- AP-4 complex subunit epsilon-1
- AP-4 complex subunit sigma-1
- AP-4 complex subunit mu-1
- Intersectin-2
- AP-2 complex subunit mu
- AP-2 complex subunit sigma
- AP-2 complex subunit alpha-1
- AP-2 complex subunit alpha-2
- AP-5 complex subunit mu-1
- AP-4 complex accessory subunit Tepsin
Sequence:
MPYLGSEDVVKELKKALCNPHIQADRLRYRNVIQRVIRHMTQGLDMSDVFMEMVKASATVDIVQKKLVYLYMGTYAPLKPDLALLAINTLCKDCSDPNPMVRGLALRSMCSLRMPGVQEYIQQPVVNGLRDKASYVRRVAVLGCAKMHNLHGDSEVDGALVNELYSLLRDQDPIVVVNCLRSLEEILKQEGGVVINKPIAHHLLNRMSKLDQWGQAEVLNFLLRYQPRSEEELFDILNLLDSYLKSSSTGVVMGATKLFLILAKKFPHVQTDVLVRVKGPLLAACSSESRELCFAALCHVRQVLHSLPGHFSSHYKKFFCSYSEPHYIKLQKVEVLCELVNDENVQQVLEELRGYCTDVAADFAQAAIFAIGSIAKTYTDQCVQILTELLGLRQEHITTVVVQTFRDLVWLCPQCTEAVCQALPGCEENIQDSEGKQALIWLLGVHGEKIPNAPYVLEDFVDNVKSETFPAVKMELLTALMRLVLSRPAECQDMLGRLLHYCIEEEKDMAVRDRGLFYYRLLLVGIDKVKQILCSPKSDPSLGLLEDQPERPVNSWASDFNTLAPVYGRAHWATISKCQQVERHRLELPHNASFATSGHLISEENKEGAQEPDSDTLMLVPNLQLTAEYFEKTWLSLRVSYQQVFPWQGEVQPDTLQMALKVVNIQTIAMSRAGAQPWKAYLSAQDDTGGLFLAELLLKPENSEMQISVKQSKARTESLHGFVSVLETVIGTVGDIKS
Protein: Arginase (PFA) (PfArg) (EC 3.5.3.1) (Q8I384)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes the hydrolysis of L-arginine into urea and L-ornithine, which is a precursor for polyamine biosynthesis. May play a role in parasite intra-hepatic development during the host liver stage (By similarity).
Interaction partners:
- Ornithine aminotransferase
- Spermidine synthase
- S-adenosylmethionine decarboxylase/ornithine decarboxylase
- Glutamine synthetase, putative
- Gametocyte-specific protein
- Glutamyl-tRNA
- nicotinamidase
- carbamoyl-phosphate synthase
- Eukaryotic translation initiation factor 5A
- Adenylosuccinate lyase
Sequence:
MLDTIESYIKSHKEKENLYVKKNVSIIGSPLAAGQPLGGVQLACDDLRKLGLHNVIDVLGWKYEDIGNIDNGDNEMKQEKKTNNYINNNDNNNDNNNDNNNDNNNNCYIPNGVIKEKKHDLSNNKMNGYVNHNFYGNYEENNVISTNDKYKNNCYYDNIRNIKEIGIFSKNLFDTMSNELRKKNFVLNIGGDHGVAFSSILSSLQMYQNLRVIWIDAHGDINIPETSPSGNYHGMTLAHTLGLFKKKVPYFEWSENLTYLKPENTAIIGIRDIDAYEKIILKKCNINYYTIFDIEKNGIYNTICTALEKIDPNSNCPIHISLDIDSVDNVFAPGTGTVAKGGLNYREINLLMKILAETKRVVSMDLVEYNPSLDEVDKKVHGDSLPILDNATKTGKLCLELIARVLGYDIV
Protein: Uncharacterized protein C14C4.04 (O13711)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Acetyl-CoA acetyltransferase
- Secretory component protein psh3
- Large ribosomal subunit protein bL33m
- Small ribosomal subunit protein uS9m
- Large ribosomal subunit protein mL43
- Small ribosomal subunit protein bS16m
- Probable acetyl-coenzyme A synthetase
- Small ribosomal subunit protein mS29
- Large ribosomal subunit protein bL36m
- Large ribosomal subunit protein uL29m
Sequence:
MSMPIVREVNSDGSMLQPFSNPLWVPTPVGRSGRKHRTLKMCIVLPDTGYDVTQVCDPWQFFVKEGFMVNFATLTGIVAQADQRLLSGVKSWFIGATYKTKDIYERMSTTKEFLSPSNMSDMSFTFENFDLVYVPGGQDPAVLELVESPRLSSLLADYIPLCARVSGTRVLATMAQGAIAVQRAAPNLEIKSTTTPLYMERASYLFGASNPPAYTYTYIPESKYVPGPKTAHWVYSDEKFFYASGRYSGDVELLCKALRNLVASALH
Protein: Ethylene receptor 2 (OsETR2) (EC 2.7.13.3) (OsPK1) (Q7XX84)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Ethylene receptor related to bacterial two-component regulators. Acts as negative regulator of ethylene signaling. May delay the transition from the vegetative stage to the floral stage by up-regulating GI (GIGANTEA) and RCN1 and cause starch accumulation in stems by down-regulating the alpha-amylase AMY3D.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P49333}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Os05g0539800 protein
- Expressed protein
- Os01g0711600 protein
- Os05g0235450 protein
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Probable ethylene response sensor 1
- Os09g0566100 protein
- Probable ethylene response sensor 2
- Protein ETHYLENE-INSENSITIVE 2
Sequence:
MPPIPSLWIRVFFSWLLLSLPAAAAADFSHCGGCDDGDGGGGIWSTDNILQCQRVSDFLIAMAYFSIPLELLYFATCSDLFPLKWIVLQFGAFIVLCGLTHLITMFTYEPHSFHVVLALTVAKFLTALVSFATAITLLTLIPQLLRVKVRENFLRIKARELDREVGMMKRQEEASWHVRMLTHEIRKSLDRHTILYTTMVELSKTLELQNCAVWMPSESGSEMILTHQLRQMETEDSNSLSIAMDNPDVLEIKATKDAKVLAADSALGIASRGKLEAGPVAAIRMPMLKASNFKGGTPEVMETSYAILVLVLPEDGSLGWGEEELEIVEVVADQVAVALSHAAVLEESQLMREKLAAQHRDLLRAKHETTMATEARNSFQTAMYDGMRRPMHSILGLVSMMQQENMNPEQRLVMDAIVKTSSVASTLMNDVMQTSTVNREYLSLVRRAFNLHSLVKEAISVVRCLTGCKGIDFEFEVDNSLPERVVGDEKRVFHIVLHMVGTLIQRCNAGCLSLYVNTYNEKEERHNQDWMLRRANFSGSYVCVKFEIRIRESRGNLLSSSSSRRLQGPNSTSSEMGLSFNMCKKIVQMMNGNIWSVSDSKGLGETIMLALQFQLQHVTPVSGASSDLFRSAPIPNFNGLQVILVDSDDTNRAVTHKLLEKLGCLVLSVTSGIQCINSFASAESSFQLVVLDLTMRTMDGFDVALAIRKFRGNCWPPLIVALAASTDDTVRDRCQQAGINGLIQKPVTLAALGDELYRVLQNN
Protein: Hid-1 family protein P19A11.07c (Down-regulated in multiple cancers 1 homolog 2) (Q9HDV3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MGSAESKISFRHAILASLNTKPEREIYEFLFTCNLTENDVFSFILAQDIRICRDSNKFDNLAILLQVCVLNIVSIQNKFSEQYPLKKNALLNSFLILTRLLPYLYESTNSSNWVRTYFQKDFSQTVDDLKPLLSELGLNYEIELPNSFSNLTSLLSSTFQLCFQHEFTVSKYASSEESIWSAGIAIPEIAHPPSYDHRLHQSLLSCFLVVLLSNTLYDSIDELDFSVLNSIVSLDAKDIYIRVICSFVNTGFIDSTNWFLNSFNQRRNSLQLYSSWFIILILSDARIKENTHLYANGEGQHIKNHLLELFKKLHRTQDFLIIAESINKFLSNPLKKERQIITFMGDFKRCVVESLCFLFLLLTNQPRFTDELVNFKSSNEMMMNLLFIHVKYSGDTENSYMSSLAGYCLQQLVSHEKLVKAACHIDKSLISPSPSSQFPVFDTSVAIYVIQVLCTLENPSSIEYNIISNILFSIPTIPLKNASPIVELISYVMKPEFFMKSQQNASDCKKLLSSFLYFLINNFNDNLHIIELLQKDKRKFEPIIAWSETEFSEFFVTSNISQSALDNGLVDQAGLDEQKWYEKWFHDLNIPLLRKCLTLRTDKNPFIEQPDEPNVTKKIYRVTYTDALQRWNLVNIWRHIFKETVTLNSGISCPWYGTNVKLFTVREVRQPTILQSRSLGEFQGRLFS
Protein: Membrane metallo-endopeptidase-like 1 (EC 3.4.24.11) (NEP2(m)) (Neprilysin II) (NEPII) (Neprilysin-2) (NEP2) (NL2) [Cleaved into: Membrane metallo-endopeptidase-like 1, soluble form (Neprilysin-2 secreted) (NEP2(s))] (P0C1T0)
Organism: Rattus norvegicus (Rat)
Function: Metalloprotease involved in sperm function, possibly by modulating the processes of fertilization and early embryonic development. Degrades a broad variety of small peptides with a preference for peptides shorter than 3 kDa containing neutral bulky aliphatic or aromatic amino acid residues. Shares the same substrate specificity with MME and cleaves peptides at the same amide bond (By similarity).
Subcellular location: Membrane; Single-pass type II membrane protein. Secreted. Note=A secreted form produced by proteolytic cleavage also exists. {ECO:0000305}.
Interaction partners:
- Insulin-degrading enzyme
- Amyloid-beta precursor protein
- Angiotensin-converting enzyme
- Angiotensin-converting enzyme
- Beta-secretase 1
- Angiotensinogen
- Metalloendopeptidase
- Angiotensin-converting enzyme 2
- Presenilin-1
- Renin
Sequence:
MGKSESSVGMMERADNCGRRRLGFVECGLLVLLTLLLMGAIVTLGVFYSIGKQLPLLNSLLHVSRHERTVVKRVLRDSSQKSDICTTPSCVIAAARILQNMDQSKKPCDNFYQYACGGWLRHHVIPETNSRYSVFDILRDELEVILKGVLEDSSVQHRPAVEKAKTLYRSCMNQSVIEKRDSEPLLNVLDMIGGWPVAMDKWNETMGPKWELERQLAVLNSQFNRRVLIDLFIWNDDQNSSRHVIYIDQPTLGMPSREYYFKEDSHRVREAYLQFMTSVATMLRRDLNLPGETDLVQEEMAQVLHLETHLANATVPQEKRHDVTALYHRMGLEELQERFGLKGFNWTLFIQNVLSSVQVELLPNEEVVVYGIPYLENLEEIIDVFPAQTLQNYLVWRLVLDRIGSLSQRFKEARVDYRKALYGTTMEEVRWRECVSYVNSNMESAVGSLYIKRAFSKDSKSIVSELIEKIRSVFVDNLDELNWMDEESKKKAQEKALNIREQIGYPDYILEDNNRHLDEEYSSLTFSEDLYFENGLQNLKNNAQRSLKKLREKVDQNLWIIGAAVVNAFYSPNRNLIVFPAGILQPPFFSKDQPQALNFGGIGMVIGHEITHGFDDNGRNFDKNGNMLDWWSNFSARHFRQQSQCMIYQYSNFSWELADNQNVNGFSTLGENIADNGGVRQAYKAYLQWLAEGGRDQRLPGLNLTYAQLFFINYAQVWCGSYRPEFAIQSIKTDVHSPLNAQVLGSLQNLPGFSEAFHCPRGSPMHPMNRCRIW
Protein: Nucleolar protein 8 (F8WE42)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
Sequence:
MKVNRETKRLYVGGLSQDISEADLQNQFSRFGEVSDVEIITRKDDQGNPQKVFAYINISVAEADLKKCMSVLNKTKWKGGTLQIQLAKESFLHRLAQEREAAKAKKEESTTGNANLLEKTGGVDFHMKAVPGTEVPGHKNWVVSKFGRVLPVLHLKNQHKRKIIKYDPSKYCHNLKKIGEDFSNTIPISSLTWELEGGNDPMSKKRRGEFSDFHGPPKKIIKVQKDESSTGSLAMSTRPRRVIERPPLTQQQAAQKRTCDSITPSKSSPVPVSDTQKLKNLPFKTSGLETAKKRNSISDDDTDSEDELRMMIAKEENLQRTTQPSINESESDPFEVVRDDFKSGVHKLHSLIGLGIKNRVSCHDSDDDIMRNDREYDSGDTDEIIAMKKNVAKVKNSTEFSQMEKSTKKTSFKNRENCELSDHCIKLQKRKSNVESALSHGLKSLNRKSPSHSSSSEDADSASELADSEGGEEYNAMMKNCLRVNLTLADLEQLAGSDLKVPNEDTKSDGPETTTQCKFDRGSKSPKTPTGLRRGRQCIRPAEIVASLLEGEENTCGKQKPKENNLKPKFQAFKGVGCLYEKESMKKSLKDSVASNNKDQNSMKHEDPSIISMEDGSPYVNGSLGEVTPCQHAKKANGPNYIQPQKRQTTFESQDRKAVSPSSSEKRSKNPISRPLEGKKSLSLSAKTHNIGFDKDSCHSTTKTEASQEERSDSSGLTSLKKSPKVSSKDTREIKTDFSLSISNSSDVSAKDKHAEDNEKRLAALEARQKAKEVQKKLVHNALANLDGHPEDKPTHIIFGSDSECETEETSTQEQSHPGEEWVKESMGKTSGKLFDSSDDDESDSEDDSNRFKIKPQFEGRAGQKLMDLQSHFGTDDRFRMDSRFLETDSEEEQEEVNEKKTAEEEELAEEKKKALNVVQSVLQINLSNSTNRGSVAAKKFKDIIHYDPTKQDHATYERKRDDKPKESK
Protein: Cation channel sperm-associated auxiliary subunit gamma 2 (C6KI89)
Organism: Mus musculus (Mouse)
Function: Auxiliary component of the CatSper complex, a complex involved in sperm cell hyperactivation. Sperm cell hyperactivation is needed for sperm motility which is essential late in the preparation of sperm for fertilization.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Cation channel sperm-associated auxiliary subunit beta
- Cation channel sperm-associated protein 1
- Cation channel sperm-associated auxiliary subunit delta
- Cation channel sperm-associated auxiliary subunit epsilon
- Cation channel sperm-associated protein 4
- Cation channel sperm-associated protein 2
- Cation channel sperm-associated protein 3
- EF-hand calcium-binding domain-containing protein 9
- Cation channel sperm-associated auxiliary subunit zeta
- Cation channel sperm-associated auxiliary subunit TMEM262
Sequence:
MVSRPAMSPVSPVWPRKPNLWAFWVLRLVLLLSLKSWAEDALQHCTWLLVLNKFEKVGLHLSKDRFQDHEPIDTVAKVFQKLTDSPIDPSENYLSFPYYLQINFSCPGQNIEELARKGHLMGMKPMVQINYMYSVNFYRWEMENVQILMEAAPMRSTGYCPAEAMCVLNWYTPMPFKNGSVVSSVDIYTNGIGPFVSKKRFYVNMNGFLKRDASGKSLFAIGYESLVLKSSHFRLSKSRPLWYTVNHAPVFILGGFYDEKSILFSDSNFQDYVLLELSIDSCWVGSFYCPILGFSATIHDAIATESTLFIRQNQLVYYFTGTYITLFDKSHGSSRWVRVLPSECIKRLCPVYASGNGSEYVLALTTGKNEGYIHIGTITDGLVSFEMVPDGWSVCEKLPGKNCSIDWATYIADERNLLLLVKIDSGQFYLVNFNTEFKTLNILYKIPEFIPEAKELDFLVLLDTVTYTNTPMTPKGLFFNTLNNMLYIWGNFILQSYNREEFIFLADFPKESTIKYMVNSFKGQMAVVTENEEIWYFLEGGYDVYQVVPSQGWETYHNLQKMQKSSFHSEDESLVSLFFEDGKLFQLVYLFDVGKERLVKRLLPVGTLMEYNLPKPFTVVNQGNYQAISFTHTCPFKEIHLIDVPKKHHASRTESYVALPPLVSESLGFHNNNTLAVYQGLVYYLLWLHSKYDKPYADPVHDPTWRWWQHKTKDKDYFFYLFSNRLAAEGIYINMNAYQKLYNMSGDYGIPDLFFLDKGNWFTITVVLLSHQDTFTSSDSQGPTINVDKKLAIAVTIADPECLSVTVTQDVLLNRNAVINKIKVIDKKRCSEQGMIGRNIKKTSMMLKVLGAPGNCIQRTYLGGIIQGFKVVPIFIGCPPGKRLAFDVSYTIMHSEEINKHYFDCVIKDAEMPCFLFRDLFQPFFLVQDLVTGDSGSFLGSYVLKVVGGGRTLNTIRDYTEEEIFRYNSPLDTTNSLIWKTKVERTTEDKKFYIMSHESPGVEWLCLENSPCYDIIPQSIYPPEFFFKLLVSNRGVDNSTYCDYKLTFIVHIHGLPLSSKRTSFIVMVSTSFFIALVVFYILFCLVWPHIVKAWVSLRWRINNIMASESYYTYASSTAGFSLQSHSFEGPSRAGSKEDNVQAKTA
Protein: FKBP-type peptidyl-prolyl cis-trans isomerase SlyD (PPIase) (EC 5.2.1.8) (Metallochaperone SlyD) (O83369)
Organism: Treponema pallidum (strain Nichols)
Function: Folding helper with both chaperone and peptidyl-prolyl cis-trans isomerase (PPIase) activities. Chaperone activity prevents aggregation of unfolded or partially folded proteins and promotes their correct folding. PPIases catalyze the cis-trans isomerization of Xaa-Pro bonds of peptides, which accelerates slow steps of protein folding and thus shortens the lifetime of intermediates. Both strategies lower the concentration of intermediates and increase the productivity and yield of the folding reaction.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
- Chaperone protein DnaK
- Heptaprenyl diphosphate synthase component I
- Trigger factor
Sequence:
MKIANECVVNIEYTLRDDTGEIIDSSDVMGALEYVQGHGMIIPGLETALINREEGEEFSVTIPPVGAYGEVQEDLRMTVGRDQFPPNVPIEVGMRFDAGSGGDSRPVTVTDVQGETIIVDGNHPLAGKTLHFEVAVRSVREATDDDLAALLFRESTSGGGCGSGAGGCGSCGAGCH
Protein: Multiple inositol polyphosphate phosphatase 1 (Ddmipp1) (EC 3.1.3.62) (2,3-bisphosphoglycerate 3-phosphatase) (2,3-BPG phosphatase) (EC 3.1.3.80) (Q54ND5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Acts as a phosphoinositide 5- and phosphoinositide 6-phosphatase and regulates cellular levels of inositol pentakisphosphate (InsP5) and inositol hexakisphosphate (InsP6) (By similarity). Also acts as a 2,3-bisphosphoglycerate 3-phosphatase, by mediating the dephosphorylation of 2,3-bisphosphoglycerate (2,3-BPG) to produce phospho-D-glycerate without formation of 3-phosphoglycerate.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Inositol-tetrakisphosphate 1-kinase
- Kinase
- Kinase
- 2,3-bisphosphoglycerate 3-phosphatase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase
- Enolase B
- Probable phosphoglycerate mutase
- Enolase A
- Prolyl endopeptidase
- Cellulose-binding domain-containing protein
Sequence:
MMVKIKNIIILFCIFGLLSNVSSLSSSSSSSQSSDNNGNLSPIQDYDLEFLSKHLTTKTPYWILTKNGDSNSQGDGSSGNSNSNSNSNSNSNSNSDSSNEPPEQCKLISIDFIARHGSRMPVLNSIEKLKEMTTSILEYKEQVNQGFNWIFNYSVPYPSDIAGNLILQGQYEHYNISKRLLKKYPLFFEPMKYKPQSYSITSTAISRTGISASAFSYGLLQGTGSLGVDGFQPVFIETASLDQDILLRFFATCNQYVDQLKNGTLINKDEQTKWNQMVFPNISNEISERLGLSDIWLPTSNVISDIFEACAYEISINNISDHWCSLLSKQNILDWEYSQDLSNYWLKSYGHEINYQIATPLLNDILSGFDIYINNNNNGSSSSSSSSSSNNGDNSGSNGSSGSGSSTSTSSNDNGSTNNNDNKVEPTSILRFGHAETIIPFISLLGLYKDEQKLFANSSTEQIENRKFRTSVVSPYASNIAMFLFDCGSAADGFKILVQHNELPVLVPGCDEIYCDYQQFKSIFKQGIDNFKWNSYCNINDDDSGSSGGDSGNGNGNDSHSKKSSYFLAIFIPITFLVGGTIGGIFTYFSYEKIMQVKNRKKLTQYGNDEFISSPKSKSFSFKPTKFDSRSPLIQ
Protein: Protein FixC (P68644)
Organism: Escherichia coli (strain K12)
Function: Could be part of an electron transfer system required for anaerobic carnitine reduction.
Interaction partners:
- Ferredoxin-like protein FixX
- Protein FixB
- Protein FixA
- Putative metabolite transport protein YaaU
- Ferredoxin-like protein YdiT
- Ferredoxin-like protein YgcO
- Crotonobetainyl-CoA reductase
- Putative electron transfer flavoprotein subunit YdiQ
- Crotonobetaine/carnitine--CoA ligase
- Putative electron transfer flavoprotein subunit YdiR
Sequence:
MSEDIFDAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNVTGGRLYAHSLEHIIPGFADSAPVERLITHEKLAFMTEKSAMTMDYCNGDETSPSQRSYSVLRSKFDAWLMEQAEEAGAQLITGIRVDNLVQRDGKVVGVEADGDVIEAKTVILADGVNSILAEKLGMAKRVKPTDVAVGVKELIELPKSVIEDRFQLQGNQGAACLFAGSPTDGLMGGGFLYTNENTLSLGLVCGLHHLHDAKKSVPQMLEDFKQHPAVAPLIAGGKLVEYSAHVVPEAGINMLPELVGDGVLIAGDAAGMCMNLGFTIRGMDLAIAAGEAAAKTVLSAMKSDDFSKQKLAEYRQHLESGPLRDMRMYQKLPAFLDNPRMFSGYPELAVGVARDLFTIDGSAPELMRKKILRHGKKVGFINLIKDGMKGVTVL
Protein: Isoamylase 3, chloroplastic (OsISA3) (EC 3.2.1.68) (B9G434)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Starch-debranching enzyme that plays a role in the degradation of transitory starch during the night in leaf blades, facilitates the formation of spherical amyloplasts containing compound granules in the endosperm, and affects morphological characteristics of plastids.
Subcellular location: Plastid, chloroplast {ECO:0000255}. Plastid, amyloplast {ECO:0000269|PubMed:21551159}. Note=Localizes in amyloplast stroma of seed endosperm. {ECO:0000269|PubMed:21551159}.
Interaction partners:
- Alpha-1,4 glucan phosphorylase
- Alpha-1,4 glucan phosphorylase
- 4-alpha-glucanotransferase DPE2
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic
- ornithine carbamoyltransferase
- 1,4-alpha-glucan branching enzyme
- Os02g0528200 protein
- Os04g0409200 protein
- Soluble starch synthase 3a, chloroplastic/amyloplastic
Sequence:
MDSIGINRAPLGSSSSAAAVTARRGIALRPARRSVASTNRVGVATIGFGDASGLRACSEKVRRFDSVRSTTARAQNGNAGRSMTEERGCTMSDTEMPFKYSSGKAFPLGVSQVEGGLNFALFSQHASSVILCLKLPGRGTEDEKGADVVEFVLDQQKNKTGDIWHVIVEGLPASGVLYGYRVGGPQGWDQGHRFDSSTVLLDPYAKLVSGRKYFGVAEEKSSQHFGTYDFDSSPFDWGDDYRLPNLPEADLVIYEMNVRAFTADESSGLDSTSRGSYLGLIDKIPHLLELGVNAVELLPVFEYDELEFKRYPNPRDHMVNTWGYSTINFFAPMSRYASAGGGPVAASKELKQMVKELHKAGIEVILDVVYNHTNEADDAHPYMTSFRGIDNKVYYMLDLNKNAELLNFSGCGNTLNCNHPVVKELILDSLRHWVEEYHIDGFRFDLASVLCRGPDGCPLDAPPLIKEIAKDAVLSRCKIIAEPWDCGGLYLVGRFPNWDRWAEWNGKYRDDLRRFIKGDPGMKGVFATRVSGSADLYQVNERKPYHGVNFVIAHDGFTLCDLVSYNLKHNDANGEGGCDGCNDNFSWNCGVEGETNDLNVLSLRSRQMKNFHVALMISQGTPMMLMGDEYGHTRYGNNNSYGHDTCINNFQWEQLEQRRDGHFRFFSEMIKFRHSNPILRRDRFLNKNDVTWHEDCWENQESKFLAFTVHDHNSGGDIYLAFNAHDYFVDAVIPPPPHHKCWNRVVDTNLESPNDIVPEGVPFTGPKYRIAPYSSILLKAKP
Protein: Phosphatidylinositol transfer protein 3 (CRAL-TRIO domain-containing protein pitC) (Random slug protein 5) (Q55CU8)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Has phosphatidylinositol transfer activity (By similarity).
Interaction partners:
Sequence:
MESTASTSDSASAITTGLSEVDINQQSPPIILKEGEIFDPLKNLNEKQLEAFKEIKSNFSDLTDPTDIAFCTDMCFLRYLRARNYIVSKSEKMLRDTLEWRKKFRPQDIQLGGDIREIGSAGCVYVNKRDKKGRPIIFAVPRNDTLKNVPSELKFKNLVYWLEQGFSRMDEPKGIEQFCFIVDYKDFGSGNMDMKTNLEAMHFLLDHCPERMGQSLFLDPPALFWFAWKIISPFLNEVTLSKVRFINSKKVDGKRTFAELLEYVDIENLEQNLGGNLDYNYNIDEYLKENPDPIVDTPPITFSTETDSKKQKKEKKKEEKEKKKEEKEKKKEEKEEKKKEKEEKKKLKKEASFTKQQENADEVD
Protein: 2,3-dimethylmalate dehydratase small subunit (EC 4.2.1.85) (Q0QLE1)
Organism: Eubacterium barkeri (Clostridium barkeri)
Interaction partners:
- 2,3-dimethylmalate dehydratase large subunit
- 3-isopropylmalate dehydratase large subunit
- 3-isopropylmalate dehydrogenase
- Isocitrate dehydrogenase
- 2-isopropylmalate synthase
- Citramalate synthase
- Ketol-acid reductoisomerase
- Acetolactate synthase small subunit
- Dihydroxy-acid dehydratase
- Pyruvate kinase
Sequence:
MKAKGSVFRYGDNVDTDVIIPARFLNTSDPLELAAHCMEDIDADFSSKVNAGDIIVADDNFGCGSSREHAPISIKASGVSCVIANSFARIFYRNAINIGLPILECPEAVAVIEAGDEVEVDFDSGVITDVTKGQSFQGQAFPEFMQTLIAAGGLVNYINATEK
Protein: Cytochrome b5 type B (Cytochrome b5 outer mitochondrial membrane isoform) (Q9CQX2)
Organism: Mus musculus (Mouse)
Function: Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P04166}.
Interaction partners:
- NADH-cytochrome b5 reductase 3
- NADH-cytochrome b5 reductase-like
- NADH-cytochrome b5 reductase 1
- NADPH--cytochrome P450 reductase
- Acyl-CoA desaturase 1
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Peptidyl-prolyl cis-trans isomerase G
- Cytochrome b5 reductase 4
- Mitochondrial amidoxime-reducing component 1
- Neudesin
Sequence:
MATPEASGSGEKVEGSEPSVTYYRLEEVAKRNSAEETWMVIHGRVYDITRFLSEHPGGEEVLLEQAGADATESFEDVGHSPDAREMLKQYYIGDVHPSDLKPKGDDKDPSKNNSCQSSWAYWFVPIVGAILIGFLYRHFWADSKSS
Protein: Paired box 1b (Paired box protein Pax-1) (B0S7C8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQMDQTYGEVNQLGGVFVNGRPLPNAIRIRIVELAQLGIRPCDISRQLRVSHGCVSKILARYNETGSILPGAIGGSKPRVTTPNVVKSIRDYKQGDPGIFAWEIRDRLLADGVCDKYNVPSVSSISRILRNKIGNLSQPSQYDSKTSPPQISYNPVYPYSYPNTMSPTGSKLGSPPAVSVSLSRAWPSVHTVSNILGIRAFMDPAAIAGSESYQPKMEDWTGVNRPSFPSVHGVNGIDKPPLESDIKYTQASSNLSGYVPACAYSATNQYGVYGGHGNYGHWQSQSAGLSHPNTGTMIQSPNLHSALSFKNTSREAVERKSPLSKHQHEGLSAVHGLSDS
Protein: Cofilin-2 (Cofilin, muscle isoform) (P21566)
Organism: Gallus gallus (Chicken)
Function: Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods.
Subcellular location: Nucleus matrix {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin, cytoplasmic 1
- LIM domain kinase 2
- LIM domain kinase 1
- Actin, cytoplasmic 2
- Hematopoietic lineage cell-specific protein
- Src substrate protein p85
- Slingshot protein phosphatase 2.
- WD repeat-containing protein 1
- Profilin
- Profilin
Sequence:
MASGVTVNDEVIKVFNDMKVRKSSTPEEIKKRKKAVLFCLSDDKKQIIVEEAKQILVGDIGDTVEDPYTAFVKLLPLNDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKFTGIKHEWQVNGLDDIKDRSTLGEKLGGNVVVSLEGKPL