wanglab/gogpt-training-data huggingface dataset:
Protein: Protein WHI4 (Q07655)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has a partially redundant function to WHI3, a dosage-dependent modulator of cell size.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Protein WHI3
Sequence:
MSLVHNQTNLNESKFLIERAFSSSSETVPLSKEATYPMPTAYSFSAVRSNSETNIKRENPQGFAKEPIMTSMLHNLTMSTGKGNGNDVNSLAPHDVDVGPYCLLLRNLPKDITLRECYCIFSLATGVSSIELKRDDREPFNDNEKVVVVKFGSLSLVTHYANILNSKSEIFGPSFPFRSHIDVVNEQTQLPVSFQEHVSSGTTNSSPKNYQLSSSAQNEIQNQSFNTISYGKTSSSPLGPSAAKPRPSLLSERSLRFSFNDPFGLETISQRKESVPFLRNSISQHDLSNVTTTPVPAGMPPQKDAGKSLLLLEKDEINESIWNGDELVNDVGNSSFGASLQEPPMSSTPVMEWNASSTANIPLFQLSSQENHQSNLLPPSHHSISQDVPHIQSQPNLNNSGVIHSATSLPHYHLLNQINASTKTQSIQQSVSNVPSNLDLNLQTENGHPQSSAPNGSSIFNNQKVNQGFLVSEQDTSTISRQKECSSTASASAFSKNNETNVAGSTTISQADLSLLAKVPPPANPADQNPPCNTLYVGNLPPDATEQELRQLFSNQQGFRRLSFRNKMNSHGHGNGHGHGPICFVEFEDVSFATRALAELYGSQLPHPRPSLNNKGGIRLSFSKNPLGVRGSNSRSKSGYSFNGSYGKS
Protein: Stringent starvation protein B (Adapter protein SspB) (Specificity-enhancing factor SspB) (P0AFZ3)
Organism: Escherichia coli (strain K12)
Function: Enhances recognition of ssrA-tagged proteins by the ClpX-ClpP protease; the ssrA degradation tag (AANDENYALAA) is added trans-translationally to proteins that are stalled on the ribosome, freeing the ribosome and targeting stalled peptides for degradation. SspB activates the ATPase activity of ClpX. Seems to act in concert with SspA in the regulation of several proteins during exponential and stationary-phase growth.
Interaction partners:
- Stringent starvation protein A
- ATP-dependent Clp protease ATP-binding subunit ClpX
- Anti-sigma-E factor RseA
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease ATP-binding subunit ClpA
- ATP-dependent Clp protease adapter protein ClpS
- Regulator of RpoS
- Cell division protein FtsB
- Outer membrane protein assembly factor BamE
- DNA polymerase III subunit delta
Sequence:
MDLSQLTPRRPYLLRAFYEWLLDNQLTPHLVVDVTLPGVQVPMEYARDGQIVLNIAPRAVGNLELANDEVRFNARFGGIPRQVSVPLAAVLAIYARENGAGTMFEPEAAYDEDTSIMNDEEASADNETVMSVIDGDKPDHDDDTHPDDEPPQPPRGGRPALRVVK
Protein: Nuclear autoantigenic sperm protein (Q5T626)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAMESTATAAVAAELVSADKIEDVPAPSTSADKVESLDVDSEAKKLLGLGQKHLVMGDIPAAVNAFQEAASLLGKKYGETANECGEAFFFYGKSLLELARMENGVLGNALEGVHVEEEEGEKTEDESLVENNDNIDETEGSEEDDKENDKTEEMPNDSVLENKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESENYVQAVEEFQSCLNLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFSKSIEVIENRMAVLNEQVKEAEGSSAEYKKEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVESSTSGFTPGGGGSSVSMIASRKPTDGASSSNCVTDISHLVRKKRKPEEESPRKDDAKKAKQEPEVNGGSGDAVPSGNEVSENMEEEAENQAESRAAVEGTVEAGATVESTAC
Protein: Nitric oxide synthase (EC 1.14.13.39) (B3VK56)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004468}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004468}. Cell projection, dendritic spine {ECO:0000256|ARBA:ARBA00004552}.
Interaction partners:
Sequence:
MEDHMFGVQQIQPNVISVRLFKRKVGGLGFLVKERVSKPPVIISDLIRGGAAEQSGLIQAGDIILAVNGRPLVDLSYDSALEVLRGIASETHVVLILRGPEGFTTHLETTFTGDGTPKTIRVTQPLGPPTKAVDLSHQPPAGKEQPLAVDGASGPGNGPQHAYDDGQEAGSLPHANGLAPRPPGQDPAKKATRVSLQGRGENNELLKEIEPVLSLLTSGSRGVKGGAPAKAEMKDMGIQVDRDLDGKSHKPLPLGVENDRVFNDLWGKGNVPVVLNNPYSEKEQPPTSGKQSPTKNGSPSKCPRFLKVKNWETEVVLTDTLHLKSTLETGCTEYICMGSIMHPSQHARRPEDVRTKGQLFPLAKEFIDQYYSSIKRFGSKAHMERLEEVNKEIDTTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLRSAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKPPRGRFDVLPLLLQANGNDPELFQIPPELVLEVPIRHPKFEWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMNLDMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEMLNYRLTPSFEYQPDPWNTHVWKGTNGTPTKRRAIGFKKLAEAVKFSAKLMGQAMAKRVKATILYATETGKSQAYAKTLCEIFKHAFDAKVMSMEEYDIVHLEHETLVLVVTSTFGNGDPPENGEKFGCALMEMRHPNSVQEERKSYKVRFNSVSSYSDSQKSSGDGPDLRDNFESAGPLANVRFSVFGLGSRAYPHFCAFGHAVDTLLEELGGERILKMREGDELCGQEEAFRTWAKKVFKAACDVFCVGDDVNIEKANNSLISNDRSWKRNKFRLTFVAEAPELTQGLSNVHKKRVSAARLLSRQNLQSPKSSRSTIFVRLHTNGSQELQYQPGDHLGVFPGNHEDLVNALIERLEDAPPVNQMVKVELLEERNTALGVISNWTDELRLPPCTIFQAFKYYLDITTPPTPLQLQQFASLATSEKEKQRLLVLSKGLQEYEEWKWGKNPTIVEVLEEFPSIQMPATLLLTQLSLLQPRYYSISSSPDMYPDEVHLTVAIVSYRTRDGEGPIHHGVCSSWLNRIQADELVPCFVRGAPSFHLPRNPQVPCILVGPGTGIAPFRSFWQQRQFDIQHKGMNPCPMVLVFGCRQSKIDHIYREETLQAKNKGVFRELYTAYSREPDKPKKYVQDILQEQLAESVYRALKEQGGHIYVCGDVTMAADVLKAIQRIMTQQGKLSAEDAGVFISRMRDDNRYHEDIFGVTLRTYEVTNRLRSESIAFIEESKKDTDEVFSS
Protein: Actin-binding LIM protein 2 (abLIM-2) (Actin-binding LIM protein family member 2) (Q8BL65)
Organism: Mus musculus (Mouse)
Function: May act as scaffold protein. May stimulate ABRA activity and ABRA-dependent SRF transcriptional activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17194709}. Note=In skeletal muscle, sarcomeric or cosarcomeric localization.
Interaction partners:
- Actin-binding Rho-activating protein
Sequence:
MSAVSQPQAAHAPLEKPASTAILCNTCGNVCKGEVLRVQNKYFHIRCFVCKACGCDLAEGGFFVRQGEHICTRDYQRLYGTRCFSCDRFIEGEVVSALGKTYHPDCFVCAVCRLPFPPGDRVTFNGKECMCQKCSPPTLLGNSAHVAQGLRSCGGCGLEIKNGQALVALDKHWHLGCFKCKTCGKLLNAEYISKDGLPYCEADYHSKFGIRCDGCEKYITGRVLEAGEKHYHPSCALCVRCGQMFSEGEEMYLQGSSIWHPACRQAARTEDKSKETRTSSESIVSVPASSTSGSPSRVIYAKLGDEILDYRDLAALPKNKAIYNIDRPDMISYSPYISHSAVGDRQSYGEGDQDDRSYKQCRTSSPSSAGSVSLGHYTPTSRSPQHYSRPGSESGRSTPSLSVHSDSRPPSSTYQQAPRHFHVPDTGVKDNIYRKPPIYKQHAARRLDVEDSSFDQDSRKKTTWLLLKGDADTRTNSPDLDSQSLSLSSGTDQEPLQRMAGDSLYSRFPYSKPDTLPGPRKDGLDLRNANLAPCGADPDASWGTREYKIYPYDSLIVTNRIRVKLPKDVDRTRLERHLSPEEFQEVFGMSIEEFDRLALWKRNDLKKKALLF
Protein: Nitrogen metabolite repression protein nmrA (Negative-acting nitrogen regulatory protein nmrA) (Nitrogen metabolite regulation protein) (Q5AU62)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: May be a redox sensor protein. Has much higher affinity for NAD(P) than for NAD(P)H. Has similar affinity for NAD and NADP. Negative transcriptional regulator involved in the post-transcriptional modulation of the GATA-type transcription factor areA, forming part of a system controlling nitrogen metabolite repression (By similarity). Interferes with the interaction between areA and target DNA. Overexpression leads to areA inhibition.
Subcellular location: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:17854403}.
Interaction partners:
- Nitrogen regulatory protein areA
- Nitrite reductase [NAD
Sequence:
MAQQKKTIAVVNATGRQAASLIRVAAAVGHHVRAQVHSLKGLIAEELQAIPNVTLFQGPLLNNVPLMDTLFEGAHLAFINTTSQAGDEIAIGKDLADAAKRAGTIQHYIYSSMPDHSLYGPWPAVPMWAPKFTVENYVRQLGLPSTFVYAGIYNNNFTSLPYPLFQMELMPDGTFEWHAPFDPDIPLPWLDAEHDVGPALLQIFKDGPQKWNGHRIALTFETLSPVQVCAAFSRALNRRVTYVQVPKVEIKVNIPVGYREQLEAIEVVFGEHKAPYFPLPEFSRPAAGSPKGLGPANGKGAGAGMMQGPGGVISQRVTDEARKLWSGWRDMEEYAREVFPIEEEANGLDWML
Protein: Putative amino-acid ABC transporter permease protein YhdX (P45767)
Organism: Escherichia coli (strain K12)
Function: Probably part of the binding-protein-dependent transport system YdhWXYZ for an amino acid; probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
Interaction partners:
- Inner membrane amino-acid ABC transporter permease protein YhdY
- Uncharacterized amino-acid ABC transporter ATP-binding protein YhdZ
- Glutamate/aspartate import ATP-binding protein GltL
- Glutamine transport ATP-binding protein GlnQ
- Arginine ABC transporter permease protein ArtM
- L-cystine transport system ATP-binding protein TcyN
- Histidine/lysine/arginine/ornithine transport system permease protein HisQ
- Putative ABC transporter arginine-binding protein 2
- ABC transporter arginine-binding protein 1
- Glutamate/aspartate import permease protein GltK
Sequence:
MSHRRSTVKGSLSFANPTVRAWLFQILAVVAVVGIVGWLFHNTVTNLNNRGITSGFAFLDRGAGFGIVQHLIDYQQGDTYGRVFIVGLLNTLLVSALCIVFASVLGFFIGLARLSDNWLLRKLSTIYIEIFRNIPPLLQIFFWYFAVLRNLPGPRQAVSAFDLAFLSNRGLYIPSPQLGDGFIAFILAVVMAIVLSVGLFRFNKTYQIKTGQLRRTWPIAAVLIIGLPLLAQWLFGAALHWDVPALRGFNFRGGMVLIPELAALTLALSVYTSAFIAEIIRAGIQAVPYGQHEAARSLGLPNPVTLRQVIIPQALRVIIPPLTSQYLNIVKNSSLAAAIGYPDMVSLFAGTVLNQTGQAIETIAMTMSVYLIISLTISLLMNIYNRRIAIVER
Protein: Syntabulin (Golgi-localized syntaphilin-related protein) (Syntaxin-1-binding protein) (Q9NX95)
Organism: Homo sapiens (Human)
Function: Part of a kinesin motor-adapter complex that is critical for the anterograde axonal transport of active zone components and contributes to activity-dependent presynaptic assembly during neuronal development.
Subcellular location: [Isoform 1]: Cytoplasm, cytoskeleton. Cytoplasmic vesicle. Note=Colocalizes with syntaxin vesicles along microtubules in neuronal processes.; SUBCELLULAR LOCATION: [Isoform 3]: Golgi apparatus membrane; Single-pass membrane protein.; SUBCELLULAR LOCATION: [Isoform 4]: Golgi apparatus membrane; Single-pass membrane protein.; SUBCELLULAR LOCATION: [Isoform 5]: Golgi apparatus membrane; Single-pass membrane protein.
Interaction partners:
- Kinesin-1 heavy chain
- Syntaxin-binding protein 5
- Protein bassoon
- Syntaxin-1A
- Synaptosomal-associated protein 25
- Syntaphilin
Sequence:
MGPLRESKKEHRVQHHDKEISRSRIPRLILRPHMPQQQHKVSPASESPFSEEESREFNPSSSGRSARTVSSNSFCSDDTGCPSSQSVSPVKTPSDAGNSPIGFCPGSDEGFTRKKCTIGMVGEGSIQSSRYKKESKSGLVKPGSEADFSSSSSTGSISAPEVHMSTAGSKRSSSSRNRGPHGRSNGASSHKPGSSPSSPREKDLLSMLCRNQLSPVNIHPSYAPSSPSSSNSGSYKGSDCSPIMRRSGRYMSCGENHGVRPPNPEQYLTPLQQKEVTVRHLKTKLKESERRLHERESEIVELKSQLARMREDWIEEECHRVEAQLALKEARKEIKQLKQVIETMRSSLADKDKGIQKYFVDINIQNKKLESLLQSMEMAHSGSLRDELCLDFPCDSPEKSLTLNPPLDTMADGLSLEEQVTGEGADRELLVGDSIANSTDLFDEIVTATTTESGDLELVHSTPGANVLELLPIVMGQEEGSVVVERAVQTDVVPYSPAISELIQSVLQKLQDPCPSSLASPDESEPDSMESFPESLSALVVDLTPRNPNSAILLSPVETPYANVDAEVHANRLMRELDFAACVEERLDGVIPLARGGVVRQYWSSSFLVDLLAVAAPVVPTVLWAFSTQRGGTDPVYNIGALLRGCCVVALHSLRRTAFRIKT
Protein: Testis-expressed protein 29 (Q8N6K0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEYVLEVKNSPRHLLKQFTVCDVPLYDICDYNVSRDRCQELGCCFYEGVCYKKAVPIYIHVFSALIVIIAGAFVITIIYRVIQESRKEKAIPVDVALPQKSSEKAELASSSSKLGLKPASPGPPSAGPSMKSDEDKDDVTGTITEAEETED
Protein: Splicing factor Cactin (B6KG46)
Organism: Toxoplasma gondii (strain ATCC 50861 / VEG)
Function: Plays a role in pre-mRNA splicing by facilitating excision of a subset of introns (By similarity). Involved in the regulation of G1 progression and stage differentiation of tachyzoites. May play a role in gene expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:22486860}. Note=Localizes in the nucleus throughout the entire tachyzoite cell cycle. {ECO:0000269|PubMed:22486860}.
Interaction partners:
- Cwf18 pre-mRNA splicing factor protein
- Pre-mRNA-processing factor 17
Sequence:
MGKKRRKHDGSGSSRSPSPDRIREARNPSQAEVAGFRAPPSGKPAMTVKQLREERQKLLHEHFGYSNTNNPFGDRLLAEPFVWKKKNQLLQAAGQKGKTTVAALIHSSKSKVQEIENVKRRREEREKEEELMQQQREELQREKEREHYEEYAQKEELFHRSNQLKKTEIRLEQNRAQLIDLIVKGLRIIKGERFEKMDVLPGPPHEVLETYKNEPVTVAMLEDLIADVKLHIDVDTTVVDADFQDFWKSLLVLAREALERAKKRKDVLDQLARNSSPQMAAEAAAQLADTVCPQIRDADTGIVLSVAHEIEGLLGGKSAAELDELEAQIRSKFEEEDIDVAYWEGILNKIPSFRARAVCLQTWHMMTQSAADAEREMAREKALKEEEEAKAARAKGEELEGLLLEEADARKLARAQQIKQDAIKVARSVEKDVNPNADGSFSPELEPYDEGEVPPPVRGPYSPQLWPFDEFRHAEILAPDDDEDRRAILKKTLIQKERLKRAGLEEDPEPTPEAAENDASLDVLDPAAKVTTYEEFVKKEKKNLEADEEVMASSSEHKLTMHYTWEEKYRPRKPRFFNRVKTGYSWNKYNTTHYDHDNPPPKVVQGYKFNIFYPDLIDKTKAPTWFLEPSDTPDTVIIRFHAGPPYEDIAFKILNQEWQLERFRGFRNVFDRGIMQLYFSFKRYIYRR
Protein: Diaminopimelate decarboxylase 2, chloroplastic (DAP decarboxylase 2) (DAPDC 2) (EC 4.1.1.20) (Q94A94)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Diaminopimelate epimerase, chloroplastic
- Alpha-aminoadipic semialdehyde synthase
- aspartate-semialdehyde dehydrogenase
- Diaminopimelate decarboxylase 1, chloroplastic
- LL-diaminopimelate aminotransferase, chloroplastic
- Aspartokinase 1, chloroplastic
- Aspartokinase 2, chloroplastic
- 4-hydroxy-tetrahydrodipicolinate synthase 2, chloroplastic
- Aspartokinase 3, chloroplastic
- 4-hydroxy-tetrahydrodipicolinate synthase 1, chloroplastic
Sequence:
MAAVTQFLSQPSSIRGTLNQYQLNQTSLSRIPFLSLKSTLKPLKRLSVKAAVSQNSTKTLTKESASSFDHCFKKSSDGFLYCEGTKVQDIMETVEKRPFYLYSKPQITRNLEAYKEALEGVRSVIGYAIKANNNLKILEHLRSLGCGAVLVSGNELRLALLAGFDPTKCIFNGNGKSLEDLVLAAQEGVFVNVDSEFDLNNIVEASRISGKQVNVLLRINPDVDPQVHPYVATGNKNSKFGIRNEKLQWFLDEVKAHPKELKLVGAHCHLGSTITKVDIFRDAAVLMIEYIDEIRRQGFEVSYLNIGGGLGIDYYHAGAVLPTPMDLINTVRELVLSRDLNLIIEPGRSLIANTCCFVNHVTGVKTNGTKNFIVIDGSMAELIRPSLYDAYQHIELVSPTPPEAEVTKFDVVGPVCESADFLGKDRELPTPPQGAGLVVHDAGAYCMSMASTYNLKMRPPEYWVEEDGSITKIRHAETFDDHLRFFEGL
Protein: Isoflavone 4'-O-methyltransferase (GeHI4'OMT) (EC 2.1.1.46) (2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase) (EC 2.1.1.212) (S-adenosyl-L-methionine:2,7,4'-trihydroxyisoflavanone 4'-O-methyltransferase) (Q84KK6)
Organism: Glycyrrhiza echinata (Licorice)
Function: 2-hydroxyisoflavanone 4'-O-methyltransferase involved in the biosynthesis of formononetin. Can use 2,7,4'-trihydroxyisoflavanone, (+)-6a-hydroxymaackiain or medicarpin as substrate, but not daidzein or (-)-6a-hydroxymaackiain.
Interaction partners:
Sequence:
MAFSTNGSEEIELYHAQIHLYKHVYNFVSSMALKSAMELGIADVIHNHGKPITLPELASALKLHPSKVGILYRFLRLLTHNGFFAKTTVPSQNGKDGEEEEETAYALTPPSKLLVKGKPTCLASIVRGALHPSSLDMWRSSEKWFKEDKELTLFESATGESFWDFLNKDSESGTLSMFQEAMAADSQMFKLALKECRHVFEGLESLVDVGGGTGGVTKLIHEEFPHLKCTVFDQPQVVGNLSGNENLKFVGGDMFKSIPPADAVLLKWVLHDWNDELSLKILKNSKEAISGKGKEGKVIIIDISIDEASGDRELTELQLDYDLVMLTMFNGKEREKKEWEKLISDAGFSSYKITPICGFKSLIEVFP
Protein: Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform (AtA beta) (PP2A, subunit A, beta isoform) (Q38950)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The A subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Involved during developmental process such as seedling and floral developments. Seems to act as a negative regulator of PP2A catalytic activity. Associates with the serine/threonine-protein phosphatase PP2A catalytic subunit C and regulatory subunit B' to positively regulates beta-oxidation of fatty acids and protoauxins in peroxisomes by dephosphorylating peroxisomal beta-oxidation-related proteins.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22404109, ECO:0000269|PubMed:25489022}. Nucleus {ECO:0000269|PubMed:22404109}. Peroxisome {ECO:0000269|PubMed:25489022}. Note=Interacts with B'THETA in the cytosol and peroxisomal import occurs by a piggybacking transport. {ECO:0000269|PubMed:25489022}.
Interaction partners:
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase PP2A-4 catalytic subunit
- Serine/threonine-protein phosphatase 2A activator
- Phytochrome-associated serine/threonine-protein phosphatase 1
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B' delta isoform
- Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' eta isoform
- Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' alpha isoform
- Serine/threonine-protein phosphatase PP2A-5 catalytic subunit
- Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' theta isoform
Sequence:
MSMIDEPLYPIAVLIDELKNDDIQLRLNSIRRLSTIARALGEERTRKELIPFLSENNDDDDEVLLAMAEELGVFIPYVGGVEYAHVLLPPLETLSTVEETCVREKAVESLCRVGSQMRESDLVDHFISLVKRLAAGEWFTARVSACGVFHIAYPSAPDMLKTELRSLYTQLCQDDMPMVRRAAATNLGKFAATVESAHLKTDVMSMFEDLTQDDQDSVRLLAVEGCAALGKLLEPQDCVQHILPVIVNFSQDKSWRVRYMVANQLYELCEAVGPEPTRTELVPAYVRLLRDNEAEVRIAAAGKVTKFCRILNPEIAIQHILPCVKELSSDSSQHVRSALASVIMGMAPVLGKDATIEHLLPIFLSLLKDEFPDVRLNIISKLDQVNQVIGIDLLSQSLLPAIVELAEDRHWRVRLAIIEYIPLLASQLGVGFFDDKLGALCMQWLQDKVHSIRDAAANNLKRLAEEFGPEWAMQHIVPQVLEMVNNPHYLYRMTILRAVSLLAPVMGSEITCSKLLPVVMTASKDRVPNIKFNVAKVLQSLIPIVDQSVVEKTIRPGLVELSEDPDVDVRFFANQALQSIDNVMMSS
Protein: Transcobalamin-1 (TC-1) (Haptocorrin) (HC) (Protein R) (Transcobalamin I) (TC I) (TCI) (P20061)
Organism: Homo sapiens (Human)
Function: Binds vitamin B12 with femtomolar affinity and protects it from the acidic environment of the stomach.
Subcellular location: Secreted.
Interaction partners:
- E3 ubiquitin-protein ligase CBL
- Lactotransferrin
- Neutrophil collagenase
- Cobalamin binding intrinsic factor
- Neutrophil gelatinase-associated lipocalin
- Ankyrin repeat and KH domain-containing protein 1
Sequence:
MRQSHQLPLVGLLLFSFIPSQLCEICEVSEENYIRLKPLLNTMIQSNYNRGTSAVNVVLSLKLVGIQIQTLMQKMIQQIKYNVKSRLSDVSSGELALIILALGVCRNAEENLIYDYHLIDKLENKFQAEIENMEAHNGTPLTNYYQLSLDVLALCLFNGNYSTAEVVNHFTPENKNYYFGSQFSVDTGAMAVLALTCVKKSLINGQIKADEGSLKNISIYTKSLVEKILSEKKENGLIGNTFSTGEAMQALFVSSDYYNENDWNCQQTLNTVLTEISQGAFSNPNAAAQVLPALMGKTFLDINKDSSCVSASGNFNISADEPITVTPPDSQSYISVNYSVRINETYFTNVTVLNGSVFLSVMEKAQKMNDTIFGFTMEERSWGPYITCIQGLCANNNDRTYWELLSGGEPLSQGAGSYVVRNGENLEVRWSKY
Protein: Sec24b protein (Q3UDH4)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
Sequence:
PPPPPSQHQQQQQQQQQQQQQQQSHSGYSSLPWSGPALPPAQDSLIRNQMGSLATANSHPTNNENVQPPKSSSVVSTVLPGPSSTRMPPAPSHPVGPVPSAPPPPEQMQTKGMQYGDYGNNQASSTATPLSSASDDEEEQEEDEEAGVDSSSTTSSASPLPNSYDALEGGSYPDMHSSSASSPVPDHALEPSPTLAQALSAAPTPPAAQPAKVAKPFGYGYPALQPAYQNAAPPPMPAAHPSGPAYTGYPQHYPGVNQLSSGLGGLSLQSSPQPESLRPVNLTQEKNILPPTPIWAPVPNLSAELSKLNCSPDSFRCTLTSIPQTQALLNKAKLPLGLLLHPFRDLTQLPVITSNTIVRCRSCRTYINPFVSFIDQRRWKCNLCYRVNDVPEEFLYNPLTRSYGEPHKRPEVQNSTVEFIASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTVLCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPTPDSLLVNLYESKELIKDLLNALPSMFINTRETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRSSTKVVHHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIFYYPSFHSTHNPSRAEKLQKDLKRYLTRKIGFEAVMRIRCTKGLSMHTFHGNFFVRSNDLLSLANINPDAGFAVQLSIEESLTDTALVCFQTALLYTSSKGERRIRVHTLCLPVVSSLADVYAGVDVQAAVCLLANMAVDRSVSSSLSDARDALVNAVVDPLSAYSSAVASVPRSTLTAPSSLKLLPLYVLALLKQKAFRTGTSTRLDDRAYAMCQMKSQPLVHLMKMIHPNLYRIDRLTDEGAIHVNDRVVPQPPLQKLSAEKLTREGAFLMDCGSVFYIWVGKGCDSNFIENVLGYPDFASIPQKMTHLPELDTLPSERTRSFVTWLRDSRPLSPVLHLVKDESPAKTDFFQHLLEDRTEAALSYYEFLIHIQQQVCK
Protein: Glycerol-3-phosphate dehydrogenase [NAD(+)], cytoplasmic (GPD-C) (GPDH-C) (EC 1.1.1.8) (P13707)
Organism: Mus musculus (Mouse)
Function: Has glycerol-3-phosphate dehydrogenase activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P21695}.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase 1, mitochondrial
- Glycerol-3-phosphate acyltransferase 2, mitochondrial
- Glycerol-3-phosphate acyltransferase 4
- Glycerol-3-phosphate acyltransferase 3
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
- Glycerol-3-phosphate dehydrogenase 1-like protein
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Triokinase/FMN cyclase)
Sequence:
MAGKKVCIVGSGNWGSAIAKIVGSNAGRLAHFDPRVTMWVFEEDIGGRKLTEIINTQHENVKYLPGHKLPPNVVAIPDVVQAATGADILVFVVPHQFIGKICDQLKGHLKANTIGISLIKGVDEGPNGLKLISEVIGERLGIPMSVLMGANIASEVAEEKFCETTIGCKDPAQGQLLKDLMQTPNFRITVVQEVDTVEICGALKNIVAVGAGFCDGLGFGDNTKAAVIRLGLMEMIAFAKLFCSGTVSSATFLESCGVADLITTCYGGRNRKVAEAFARTGKSIEQLEKEMLNGQKLQGPQTARELHSILQHKGLVDKFPLFTAVYKVCYEGQPVGEFIRCLQNHPEHM
Protein: Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (Gamma-glutamylcysteine synthetase) (Q6FLG3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Glutathione synthetase
- Candida glabrata strain CBS138 chromosome K complete sequence
- Glutathione hydrolase
- Candida glabrata strain CBS138 chromosome C complete sequence
- Branched-chain-amino-acid aminotransferase
- Branched-chain-amino-acid aminotransferase
- cystathionine gamma-lyase
- Candida glabrata strain CBS138 chromosome F complete sequence
- Homocysteine/cysteine synthase
- Cystathionine beta-lyase
Sequence:
MGLLSLGTPLPWEESRNYSEHIRNEGVEQLLYVFKSAGGRDGDPLLWGDEVEYMMVELEAGKQVATLDVVHDRILDELNERDLELCNVNDVKFHPEYGRFMLEATPKSAYPGYVAEYVEYNMQQRRLVAEYKLAQYAEEEHLKGKRLVPLTLTVFPRMGCPDFLNIPNAWDHKNTASRSLFLPDEVINRHARFPNLTSSIRTRRGEKVCINIPILKDRNTPELDDSIKPRDWFVPEDKESRLASKPGHIYLDAMGFGMGCSCLQMTYQAPNIEKARFLYDTLVNFAPVFLAVSAATPGFKGWVADQDVRWNVISGAVDDRTPQERSVPPLLPEYNIDGFGGILKENRKKVQQIPKSRYSVVDLYLGGNENKSFNRRYNDTDVPVNEKVLKRLLENEKYPLDYDLAKHFAHLYIRDPISTFEELLDQDNSTSTNHFENIQSTNWQTLRFKPPTQEATPDNHNVPGWRVEFRPLDIQLLDFENAAFSNMMYMIVDFVLQNTDKINPYVPMSQVWENMIRAHHRDAAIKEKFYWRTTFDSKEKLQFGDESEELSLDEIFHNKNNGIFPVFINTILKQRNFIQKEWQEMKDQPQNRRLYYYFKIISDRASGRLPTAAKFLKNFILTHPDYRHDSKISQQINYDLIEMCDRITHLDDSRGELSAFVGEEIAKFLLNNKLSTGN
Protein: Secreted protein CSS1 (Condition specific secretion protein 1) (Haze protective factor 1') (P40442)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Secreted protein that may be involved in cell wall organization and biosynthesis.
Subcellular location: Secreted {ECO:0000269|PubMed:26928762}.
Interaction partners:
- Haze protective factor 1
- Uncharacterized protein YOL160W
Sequence:
MFNRLNKFQAALALALYSQSALGQYYSNSTSISSNSSSTSVVSSSSGSVSISSSIAETSSSATDILSSITQSASSTSGVSSSVGPSSSSVVSSSVSQSSSSVSDVSSSVSQSSSSASDVSSSVSQSASSTSDVSSSVSQSSSSASDVSSSVSQSSSSASDVSSSVSQSASSASDVSSSVSQSASSTSDVSSSVSQSSSSASDVSSSVSQSSSSASDVSSSVSQSASSTSDVSSSVSQSASSTSGVSSSGSQSVSSASGSSSSFPQSTSSASTASGSATSNSLSSITSSASSASATASNSLSSSDGTIYLPTTTISGDLTLTGKVIATEGVVVAAGAKLTLLDGDKYSFSADLKVYGDLLVKKSKETYPGTEFDISGENFDVTGNFNAEESAATSASIYSFTPSSFDNSGDISLSLSKSKKGEVTFSPYSNSGAFSFSNAILNGGSVSGLQRRDDTEGSVNNGEINLDNGSTYVIVEPVSGKGTVNIISGNLYLHYPDTFTGQTVVFKGEGVLAVDPTETNATPIPVVGYTGKNQIAITADITALSYDGTTGVLTATQGNRQFSFAIGTGFSSSDFSVSEGIFAGAYAYYLNYNGVVATSAASSSTASGASASVTGSTSFGASVTGSTASTSFGASVTGSTASTSFGASVTGSTSVYTTTLDYVNATSTVVVSCSETTDSNGNVYTITTTVPCSSTTATITSCDETGCHVSTSTGAVVTETVSSKSYTTATVTHCDDNGCNTKTVTSECSKETSATTASPKSYTTVTVTHCDDNGCNTKTVTSEAPEATTTTTVSSQSYTTATVTHCDDNGCKTKTVTSEAPEATTTTVSPKTYTTATVTQCDDNGCSTKTVTSECPEETSATTTSPKSYTTVTVTHCDDNGCNTKTVTSEAPEATTTTVSPKTYTTATVTQCDDNGCSTKTVTSEAPKETSETSETSAAPKDIHYCHWLLNGDDNGCNVKIITSKIPEATSTVTQLVLLQSHTLLSLLRVLKQPH
Protein: Autoinducer 2 import system permease protein LsrD (AI-2 import system permease protein LsrD) (P0AFS1)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Probably responsible for the translocation of the substrate across the membrane (Probable).
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Autoinducer 2 import system permease protein LsrC
- Autoinducer 2 import ATP-binding protein LsrA
- Autoinducer 2-binding protein LsrB
- (4S)-4-hydroxy-5-phosphonooxypentane-2,3-dione isomerase (Autoinducer 2-degrading protein LsrG) (AI-2-degrading protein LsrG) (Phospho-(S)-4,5-dihydroxy-2,3-pentanedione isomerase) (Phospho-AI-2 isomerase)
- 3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase
- Autoinducer-2 kinase
- Transcriptional regulator LsrR
- D-allose-binding periplasmic protein
- Ribose import binding protein RbsB
- Ribose import ATP-binding protein RbsA
Sequence:
MRIRYGWELALAALLVIEIVAFGAINPRMLDLNMLLFSTSDFICIGIVALPLTMVIVSGGIDISFGSTIGLCAIALGVLFQSGVPMPLAILLTLLLGALCGLINAGLIIYTKVNPLVITLGTLYLFAGSALLLSGMAGATGYEGIGGFPMAFTDFANLDVLGLPVPLIIFLICLLVFWLWLHKTHAGRNVFLIGQSPRVALYSAIPVNRTLCALYAMTGLASAVAAVLLVSYFGSARSDLGASFLMPAITAVVLGGANIYGGSGSIIGTAIAVLLVGYLQQGLQMAGVPNQVSSALSGALLIVVVVGRSVSLHRQQIKEWLARRANNPLP
Protein: UPF0336 protein Rv0635 (P9WFK1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- (3R)-hydroxyacyl-ACP dehydratase subunit HadB
- UPF0336 protein Rv0637
- Large ribosomal subunit protein bL33B
- DNA-directed RNA polymerase subunit alpha
Sequence:
MALSADIVGMHYRYPDHYEVEREKIREYAVAVQNDDAWYFEEDGAAELGYKGLLAPLTFICVFGYKAQAAFFKHANIATAEAQIVQVDQVLKFEKPIVAGDKLYCDVYVDSVREAHGTQIIVTKNIVTNEEGDLVQETYTTLAGRAGEDGEGFSDGAA