wanglab/gogpt-training-data huggingface dataset:
Protein: Acyl carrier protein, mitochondrial (ACP) (CI-SDAP) (NADH-ubiquinone oxidoreductase 9.6 kDa subunit) (P52505)
Organism: Bos taurus (Bovine)
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis. Accessory and non-catalytic subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain. Accessory protein, of the core iron-sulfur cluster (ISC) assembly complex, that regulates, in association with LYRM4, the stability and the cysteine desulfurase activity of NFS1 and participates in the [2Fe-2S] clusters assembly on the scaffolding protein ISCU (By similarity). The core iron-sulfur cluster (ISC) assembly complex is involved in the de novo synthesis of a [2Fe-2S] cluster, the first step of the mitochondrial iron-sulfur protein biogenesis. This process is initiated by the cysteine desulfurase complex (NFS1:LYRM4:NDUFAB1) that produces persulfide which is delivered on the scaffold protein ISCU in a FXN-dependent manner. Then this complex is stabilized by FDX2 which provides reducing equivalents to accomplish the [2Fe-2S] cluster assembly. Finally, the [2Fe-2S] cluster is transferred from ISCU to chaperone proteins, including HSCB, HSPA9 and GLRX5 (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:1907568, ECO:0000305|PubMed:18721790}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH-ubiquinone oxidoreductase chain 3
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 10
- NADH dehydrogenase 1 alpha subcomplex subunit 3
- NADH dehydrogenase 1 alpha subcomplex subunit 8
Sequence:
MAVRVLCACVRRLPTAFAPLPRLPTLAAARPLSTTLFAAETRTRPGAPLPALVLAQVPGRVTQLCRQYSDAPPLTLEGIKDRVLYVLKLYDKIDPEKLSVNSHFMKDLGLDSLDQVEIIMAMEDEFGFEIPDIDAEKLMCPQEIVDYIADKKDVYE
Protein: Succinate-semialdehyde dehydrogenase, mitochondrial (EC 1.2.1.24) (Aldehyde dehydrogenase family 5 member A1) (NAD(+)-dependent succinic semialdehyde dehydrogenase) (Q8BWF0)
Organism: Mus musculus (Mouse)
Function: Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- 4-aminobutyrate aminotransferase, mitochondrial
- Citrate synthase, mitochondrial
- Citrate synthase
- Malate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
- Isocitrate dehydrogenase cytoplasmic
- Isocitrate dehydrogenase, mitochondrial
- Pyruvate carboxylase, mitochondrial
- ATP-citrate synthase
- Isocitrate dehydrogenase subunit alpha, mitochondrial
Sequence:
MATCFLLRSFWAARPALPPPGRFRPEPAGTPRRSYASGPGGLHADLLRGDSFVGGRWLPAPATFPVYDPASGAKLGTVADCGVPEARAAVRAAYDAFNSWKGVSVKERSLLLRKWYDLMIQNKDDLAKIITAESGKPLKEAQGEILYSALFLEWFSEEARRIYGDIIYTSAKDKRGLVLKQPVGVAAIITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPYSALALAQLANQAGIPAGVYNVIPCSRNKAKEVGEVLCTDPLVSKISFTGSTATGKILLHHAANSVKRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNAGQTCVCSNRFLVQRGIHDSFVTKFAEAMKKSLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVAKGATVVTGGKRHQSGGNFFEPTLLSNVTRDMLCITEETFGPLAPVIKFDKEEEAVAIANAAEVGLAGYFYSQDPAQIWRVAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLEVKYVCYGGL
Protein: DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18) (E5KPM5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQAGLLGNAFDGHQLLRPLIFCQDHLREGPPIGRGDSQGEELEPQLPSSLSSIPYGFCDHCWTKDVDDPPLVTHPSPGSRDGHMTQAWPVKVVSPLATVIGHVMQASLLAL
Protein: Stabilin-2 (Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 2) (FEEL-2) (Hyaluronan receptor for endocytosis) [Cleaved into: 175 kDa stabilin-2 (175 kDa hyaluronan receptor for endocytosis)] (Q8CFM6)
Organism: Rattus norvegicus (Rat)
Function: Phosphatidylserine receptor that enhances the engulfment of apoptotic cells. Hyaluronan receptor that binds to and mediates endocytosis of hyaluronic acid (HA). Acts also, in different species, as a primary systemic scavenger receptor for heparin (Hep), chondroitin sulfate (CS), dermatan sulfate (DS), nonglycosaminoglycan (GAG), acetylated low-density lipoprotein (AcLDL), pro-collagen propeptides and advanced glycation end products (AGE). May serve to maintain tissue integrity by supporting extracellular matrix turnover or it may contribute to maintaining fluidity of bodily liquids by resorption of hyaluronan. Counter receptor which plays an important role in lymphocyte recruitment in the hepatic vasculature. Binds to both Gram-positive and Gram-negative bacteria and may play a role in defense against bacterial infection. The proteolytically processed 175 kDa form also functions as an endocytosis receptor for heparin internalization as well as HA and CS.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8WWQ8}. Cell membrane {ECO:0000269|PubMed:15572036}; Single-pass type I membrane protein {ECO:0000269|PubMed:15572036}.
Interaction partners:
- Extracellular link domain-containing 1
- Oncoprotein-induced transcript 3 protein
- PTB domain-containing engulfment adapter protein 1
- T-cell immunoglobulin and mucin domain containing 4
Sequence:
SLPSLLTRLEQMPDYSIFRGYIIHYNLASAIESADAYTVFVPNNEAIENYIREKKATSLKEDILRYHVVLGEKLLKNDLHNGMHRETMLGFSYLLAFFLRNDQLYVNEAPINYTNVATDKGVIHGLEKVLEIQKNRCDNNDTIIVRGECGKCSQQAPCPLETKPLRETRKCIYSIYFMGKRSVFIGCQPQCVRTIITRACCAGFFGPQCQACPGRGQNVCSGNGFCLDGVNGTGTCQCGLGFNGTACETCTEGKYGIHCDQACSCVHGRCSQGPLGDGSCDCDVGWRGVKCDMEITTDNCNGTCHTSANCLLDPDGKASCKCAAGFRGNGTVCTAINACETSNGGCSTKADCKRTTPGNRVCVCKAGYTGDGIVCLEINPCLENHGGCDRNAECTQTGPNQAVCNCLPKYTGDGKVCSLINVCLTNNGGCSPFAFCNYTEQDQRICTCKPDYTGDGIVCRGSIYGELPKNPSTSQYFFQLQEHAVRELAGPGPFTVFAPLSSSFNHEPRIKDWDQQGLMSQVLRYHVVGCQQLLLDNLKVTTSATTLQGEPVSISVSQDTVFINNEAKVLSSDIISTNGVIHVIDKLLSPKNLLITPKDALGRVLQNLTTVAANHGYTKFSKLIQDSGLLSVITDSIHTPVTVFWPTDKALEALPPEQQDFLFNQDNKDKLKSYLKFHVIRDSKALASDLPRSASWKTLQGSELSVRCGTGSDIGELFLNEQMCRFIHRGLLFDVGVAYGIDCLLMNPTLGGRCDTFTTFDIPGECGSCIFTPKCPLKSKPKGVKKKCIYNPLPFRRNVEGCQNLCTVVIQTPRCCHGYFMPDCQACPGGPDTPCNNRGMCRDLYTPMGQCLCHTGFNGTACELCWHGRFGPDCQPRSCSEHGQCDEGITGSGECLCETGWTAASCDTPTAVFAVCTPACSVHATCTENNTCVCNLNYEGDGITCTVVDFCKQNNGGCAKVAKCSQKGTQVSCSCKKGYKGDGYSCIEIDPCADGVNGGCHEHATCRMTGPGKHKCECKSHYVGDGVDCEPEQLPLDRCLQDNGQCHPDASCADLYFQDTTVGVFHLRSPLGQYKLTFDKAKEACAKEAATIATYNQLSYAQKAKYHLCSAGWLESGRVAYPTTYASQKCGANVVGIVDYGSRANKSEMWDVFCYRMKDVNCTCKAGYVGDGFSCSGNLLQVLMSFPSLTNFLTEVLAFSKSSARGQAFLKHLTDLSIRGTLFVPQNSGLPGNKSLSGRDIEHHLTNVNVSFYNDLVNGTFLRTMLGSQLLITFSQDQLHQETRFVDGRSILQWDIIAANGILHIISEPLRAPPTAATAAHSGLGTGIFCAVVLVTGAIALAAYSYFRLKQRTTGFQRFDQKRTLMSWLLASSSPRISQTLCMRPQRRHPQSPPVTPSQTLENRIWRTATLWGHCGPDMRSQQATTVTVPR
Protein: Leucine-rich repeat transmembrane neuronal protein 1 (Q8K377)
Organism: Mus musculus (Mouse)
Function: Exhibits strong synaptogenic activity, restricted to excitatory presynaptic differentiation, acting at both pre- and postsynaptic level.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Accumulates extensively in the endoplasmic reticulum of transfected nonneuronal cells. {ECO:0000269|PubMed:17667961, ECO:0000269|Ref.5}.
Interaction partners:
- Neurexin-3
- Neurexin-1
- Neurexin-2
- Neuroligin-1
- Calsyntenin-3
Sequence:
MDFLLLGLCLHWLLRRPSGVVLCLLGACFQMLPAAPSGCPGQCRCEGRLLYCEALNLTEAPHNLSGLLGLSLRYNSLSELRAGQFTGLMQLTWLYLDHNHICSVQGDAFQKLRRVKELTLSSNQITELANTTFRPMPNLRSVDLSYNKLQALAPDLFHGLRKLTTLHMRANAIQFVPVRIFQDCRSLKFLDIGYNQLKSLARNSFAGLFKLTELHLEHNDLIKVNFAHFPRLISLHSLCLRRNKVAIVVSSLDWVWNLEKMDLSGNEIEYMEPHVFETVPYLQTLQLDSNRLTYIEPRILNSWKSLTSITLAGNLWDCGRNVCALASWLSNFQGRYDANLQCASPEYAQGEDVLDAVYAFHLCEDGAEPTSGHLLSVAVTNRSDLTPPESSATTLVDGGEGHDGTFEPITVALPGGEHAENAVQIHKVVTGTMALIFSFLIVVLVLYVSWKCFPASLRQLRQCFVTQRRKQKQKQTMHQMAAMSAQEYYVDYKPNHIEGALVIINEYGSCTCHQQPARECEV
Protein: Probable catechol O-methyltransferase 2 (EC 2.1.1.6) (Q8NKC1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Vacuole {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable catechol O-methyltransferase 1
- Alcohol dehydrogenase
- Copper amine oxidase-like protein cao2
- Alcohol dehydrogenase 4
- Copper amine oxidase 1
- Probable S-
- Putative S-
- Ornithine decarboxylase antizyme
- Large ribosomal subunit protein eL38B
- Uncharacterized protein C19F5.03
Sequence:
MFAQALHWLTTSKLRYALALPFLFFILYTKTKKSKEQELENYIFSLPREKLDQIRGKPDEVINVIDEYVEQGHFLMNIGKLKGKIISEKIQQVKPKVMIELGGYVGYSAILFGKQLTDPSAHYYSLEVNPKFAKIASKIIDLAGLSNKVTIIVGKATDSLVELRRSLPNVIPSFEYLDFVFIDHWKDLYVPDLRVMETLDLIGQGSIIAADNILRPGVPEYVKYVQGSLDYRKEYDSTVSNVNGPQFIGKWNIIYKSKTIKVDDGKREKDAVEITEYIEAK
Protein: O-phosphoseryl-tRNA(Sec) selenium transferase (EC 2.9.1.2) (Selenocysteine synthase) (Selenocysteinyl-tRNA(Sec) synthase) (Sep-tRNA:Sec-tRNA synthase) (A0A3S7WQS5)
Organism: Leishmania donovani
Function: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis.
Subcellular location: Cytoplasm {ECO:0000255|PIRNR:PIRNR017689, ECO:0000269|PubMed:26586914}.
Interaction partners:
Sequence:
MDDRSLKLAEDFVSARYIEAGRESLRATARIMRSILAQRCCPDEGLTDAAIELILRQLSLMDTNNLAHHVGGGEREGRVVSALVRMRHFHLTHGIGRSGDLFSEQPKAAGSSLLYKITNVLMLDLIRQAGAPSTAAAVVVPMATGMTLALVLRCVAKTHMKELMKEAEAVQLQRTVTKDSTSATSAAPVQEPPMSEADRDRHDRTSLPVPATPRYVIWPRIDQKTALKCIDAAGLVPVPVQLRPAVPLARSAAPCVSTNRDSLDRGQDSIGSPSTPTSSSSLFLECHVDDVAAAVNAVGGPSQVVCVLSTTSCFAPRLPDNTVAIAQYCKKAGIPYVVNNAYGVQSRRIMTRLDAAQRLGRVDFVVQSGDKNFLVPVGGSIICSGDKERCKAVAALYAGRASMSPIVDLFITALSLGRRGMQTLWSDRYKCRARLIRQLRVFARERREVLLVDDSDDDKADEDTVGGSQRTSNAVVPRNDISVAVTMRAYGLPAAEASSSGAQLGSEQAGRVTNWAAARALGAQLFRSAVTGPRVITPAPSTPTTIAGCTFRNYGMHQDREPPCPLLVIACGIGMSESEVDALMARLRDLWPVPA
Protein: Cobalt transport protein CbiQ (Energy-coupling factor transporter transmembrane protein CbiQ) (ECF transporter T component CbiQ) (D5AUZ7)
Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Function: Part of the energy-coupling factor (ECF) transporter complex CbiMNOQ involved in cobalt import. The complex confers cobalt uptake upon expression in E.coli; can also transport nickel with a very low affinity.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cobalt import ATP-binding protein CbiO
- Cobalt transport protein CbiN
- Cobalt transport protein CbiM
- Fused nickel transport protein NikMN
- Nickel import ATP-binding protein NikO
- Nickel transport protein NikQ
- DUF4198 domain-containing protein
- Biotin transport ATP-binding protein BioM
- Cobalamin biosynthesis protein CbiG
- Precorrin-6Y C5,15-methyltransferase
Sequence:
MSIASIDRVAAQGRWRNRPLAEKCLIGLGFLALAVTVPPFPGAVLVTVAILAFTFLGARVPLRFWAAVAVLPLGFLTTGAAVLLIQIGPDGIGLAPQGPAKAAALVMRASAATCCLLFLATTTPAADLLSGLRRWRVPAELIEIALLTYRFVFILAEEAAAMTTAQRARLGHATRRRWLRSTAQVIAALLPRALDRARRLETGLAARNWQGEMRVLSTRPAASPLVLGLILTLQAAILAAGVLL
Protein: Voltage-dependent L-type calcium channel subunit (Q9FFC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Seipin-2
- REF/SRPP-like protein At1g67360
- REF/SRPP-like protein At3g05500
- Seipin-1
- Transmembrane 9 superfamily member 8
- Alpha/beta-Hydrolases superfamily protein
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- ACD11 homolog protein
- Oleosin 18.5 kDa
- Non-specific lipid transfer protein GPI-anchored 5
Sequence:
MAQDHDETENKTFADVVGGDDVGEIVNGGTKNGYRKPDSVEKEDDEDLKSLYSLICLTIGSILFPDSKTGDASSFLERVRNSVAENGPKLREASERTGREILLWTRRGSSLRALLVITMGTIVLLTTMALVVFTLFFVAATANAIIISLLISLAVAGGFLALFFLCLTGVYIGALSVAAFVISTATVSAVVSVLIASGWIGFFYAVWLGTRGSLRLAKQSVSVVGSAISGNTISRHQHQDREVNIESTN
Protein: Sphinganine hydroxylase BasA (Eurofung) (Q5BFP0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- DAGKc domain-containing protein
- Ceramide synthase BarA
- Ceramide synthase LagA
- Alkaline phytoceramidase
- Ceramide very long chain fatty acid hydroxylase
- Cytochrome P450, putative
- Sphingolipid delta
- Neutral ceramidase
Sequence:
MATNTTLLYDLPPLPAYQLTPRPSLVDGIPDNILALILPVVAYWAVSMFFHVIDVYDLFPQYRLHTPAEVLTRNRASRWDVVRDVVLQQVVQTLAGLILAYFDEQEYIGREEYDVAVWARRIRFVQRGLPYLLALFGLDASGVAANFSRNGHKMLAGAVAGGYYPGATQSIVSSGGIETVVPAFTNWEMSLAAFIYWYFIPALQFTWGICVVDTWQYFLHRAMHLNRWLYVHFHSRHHRLYVPYAYGALYNHPVEGLLLDTVGAGIGFLTSGMTHRQSMWFFTFSTIKTVDDHCGYAFPWDPLQHATTNNAAYHDIHHQSWGIKTNFSQPFFTFWDRLFNTQWKGEVKLRYERSREAAEKKLSEGGMQQDSDMENSSSDFAQPNGEAAVVSPEEPSDRDARTRLRKKTASFSPSVDSLKGVNHGVPSSVL
Protein: Protein S100 (S100 calcium-binding protein) (A0A060WZ60)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- SAP domain-containing protein
- Uncharacterized protein
- SAP domain-containing protein
- SAP domain-containing protein
- RNA helicase
- ATP-dependent RNA helicase
- RNA helicase
- RNA helicase
Sequence:
MGSKLESAMEGLIRVFHSYSSKEGDKYKLSKVELKNLLQGELSDFLAASKDPMVVEKIMSDLDENKDGEVDFQEFVILVAALTVACNEFFVESLNE
Protein: Zinc finger protein SNAI2 (Protein slug-alpha) (Protein snail homolog 2) (Snail protein homolog Slug) (xSlu) (Q91924)
Organism: Xenopus laevis (African clawed frog)
Function: Probable transcriptional repressor. Acts downstream of snai1 in the specification of the neural crest and neural crest migration.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MPRSFLVKKHFNSAKKPNYGELDNHTVIISPFLYERYPVSVLPQPDIYSSVAYSPITVWTGLLHPPLPSDLSPLSGYPSSLGRVSPPPQSDTSSKDHSGSESPISDEEERLQTKLSDSHAIEAEKFQCSLCSKTYSTFSGLAKHKQLHCDAQSRKSFSCKYCEKEYVSLGALKMHIRTHTLPCVCKICGKAFSRPWLLQGHIRTHTGEKPFSCPHCNRAFADRSNLRAHLQTHSDVKKYQCKNCSKTFSRMSLLHKHEESGCCVAH
Protein: Synaptosomal-associated protein 25 (SNAP-25) (Super protein) (SUP) (Synaptosomal-associated 25 kDa protein) (P60881)
Organism: Rattus norvegicus (Rat)
Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P60879}. Cell membrane {ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:23341457}; Lipid-anchor {ECO:0000250|UniProtKB:P60879}. Synapse, synaptosome {ECO:0000269|PubMed:1281490}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P60879}. Note=Membrane association requires palmitoylation (By similarity). Expressed throughout cytoplasm, concentrating at the perinuclear region (By similarity). Colocalizes with KCNB1 at the cell membrane (PubMed:12403834). Colocalizes with PLCL1 at the cell membrane (PubMed:23341457). {ECO:0000250|UniProtKB:P60879, ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:1281490, ECO:0000269|PubMed:23341457}.
Interaction partners:
Sequence:
MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG
Protein: 60S acidic ribosomal protein P0 (Q386V3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 40S ribosomal protein S14
- 40S ribosomal protein S23, putative
- 60S ribosomal protein L6, putative
- 40S ribosomal protein S24
- 40S ribosomal protein S17, putative
- 60S ribosomal protein L10, putative
- 60S ribosomal protein L37a, putative
- 40S ribosomal protein S33, putative
- 60S ribosomal protein L35, putative
- 40S ribosomal protein S25
Sequence:
MPSVSQEKRDYEDRLNGCLTKYSRVLFCLMDNVRSQQVHGVRRDLRGKGELVMGKKTLQKKIVEKRAEGNKATDADKLFHQVCTDKQLLCGNTSMIFTNSEVSDITSVLDSHRVQAPARVGAIAPCDVIVPAGNTGMEPKATAFFQALNIATKISKGTVEIVSDKKVLSTGDKVDNSTATLLQKLDISPFYYQVEVQSVWDRGVLFTREDLSVTDAVVEKYLLEGISNISAMSLGAGIPTAATLPHMIVDAFKTLLGASVATNYEFEEYDGKNLRTAALEGKLGGGEAAAPAAAAAAAAPAAAPAAAAAEEEEDDDDFGMGALF
Protein: Rho GTPase-activating protein 6 (Rho-type GTPase-activating protein 6) (Rho-type GTPase-activating protein RhoGAPX-1) (O43182)
Organism: Homo sapiens (Human)
Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. Could regulate the interactions of signaling molecules with the actin cytoskeleton. Promotes continuous elongation of cytoplasmic processes during cell motility and simultaneous retraction of the cell body changing the cell morphology.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10699171}.
Interaction partners:
- Holocytochrome c-type synthase
- Transforming protein RhoA
Sequence:
MSAQSLLHSVFSCSSPASSSAASAKGFSKRKLRQTRSLDPALIGGCGSDEAGAEGSARGATAGRLYSPSLPAESLGPRLASSSRGPPPRATRLPPPGPLCSSFSTPSTPQEKSPSGSFHFDYEVPLGRGGLKKSMAWDLPSVLAGPASSRSASSILCSSGGGPNGIFASPRRWLQQRKFQSPPDSRGHPYVVWKSEGDFTWNSMSGRSVRLRSVPIQSLSELERARLQEVAFYQLQQDCDLSCQITIPKDGQKRKKSLRKKLDSLGKEKNKDKEFIPQAFGMPLSQVIANDRAYKLKQDLQRDEQKDASDFVASLLPFGNKRQNKELSSSNSSLSSTSETPNESTSPNTPEPAPRARRRGAMSVDSITDLDDNQSRLLEALQLSLPAEAQSKKEKARDKKLSLNPIYRQVPRLVDSCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVSLEEEHSVHDVAALLKEFLRDMPDPLLTRELYTAFINTLLLEPEEQLGTLQLLIYLLPPCNCDTLHRLLQFLSIVARHADDNISKDGQEVTGNKMTSLNLATIFGPNLLHKQKSSDKEFSVQSSARAEESTAIIAVVQKMIENYEALFMVPPDLQNEVLISLLETDPDVVDYLLRRKASQSSSPDMLQSEVSFSVGGRHSSTDSNKASSGDISPYDNNSPVLSERSLLAMQEDAAPGGSEKLYRVPGQFMLVGHLSSSKSRESSPGPRLGKDLSEEPFDIWGTWHSTLKSGSKDPGMTGSSGDIFESSSLRAGPCSLSQGNLSPNWPRWQGSPAELDSDTQGARRTQAAAPATEGRAHPAVSRACSTPHVQVAGKAERPTARSEQYLTLSGAHDLSESELDVAGLQSRATPQCQRPHGSGRDDKRPPPPYPGPGKPAAAAAWIQGPPEGVETPTDQGGQAAEREQQVTQKKLSSANSLPAGEQDSPRLGDAGWLDWQRERWQIWELLSTDNPDALPETLV
Protein: mRNA export factor mex67 (AFU_orthologue AFUA_1G05110) (Q5B9P3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nucleoporin NSP1
- Nuclear transport factor 2 domain protein, putative
- WD40 repeat protein poxJ
- RNA annealing protein Yra1, putative
- RNA binding protein, putative
- Nuclear cap-binding protein subunit 2
- Peptidase S59 domain-containing protein
- Nonsense-mediated mRNA decay protein Upf3, putative
- Nuclear pore complex protein An-Nup159
- Nuclear pore complex protein An-Sac3
Sequence:
MKRGRSSRGRTSTRANTGDRGGIRKRGAPPTKVDRDGDLAMGAGAGAIRGQKTRSGSGRPASSATRANTALDRSISQIQKALSSSNAQANIRQGGRSSPTEQVAVRGWKESKAASNRDGGVESLVAFLEKKLTSPDSKSGPRVKISKSRVEGDALIVSIRPESLERMLQLNGFTFAGAPLTIEKYDQETAPLLNHSIPAQNGTTPSTADTKSKMTAILGRRYYQQSKLLDLSKLGTDPDLVAMGIFGTTSTESKFFPALMKVWELNFDNATARRDAVESVSLADNQLSNISVVTTLSQTFPDLKNLDLSNNNFADAQALIGWRWKFRKLQFLDLTGNPFSADPNFKDTMLKWYPELKTLNNTQVRTDEEIAAQKKTPIPVQAPHFHDEGQIAENFIRAFFTGYDNNRAEIVSGFYDNNSTFSLNVNTSAPRALQTEPAPWDPYLKKSRNLLKISHLPARMSRTYTGVEKIKELWTTLPPTRHPDIAAHPEEWLIECFPIPGLPDISGQSSTGVGGFLIMVHGKFEEDNSGKVETRSFDRTFIIGPGAGVGGIRVISDVLCLRAYGGNEAWQLEPPPVAAQPAAAPVAARVAAPAAPAGYGLPAPGKADVQVQQEQLVMQLSAKTMMTLQYSELALSGNNWNMDAALKNFEELKTQGQLPPDAFLPGVTA
Protein: Probable cytosolic oligopeptidase A (EC 3.4.24.70) (Thimet metalloendopeptidase 2) (Zincin-like metalloproteases family protein 2) (Q949P2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Oligopeptidase that may be involved in the degradation of proteasome-generated peptides (By similarity). Binds salicylic acid.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:24043784}.
Interaction partners:
- Presequence protease 1, chloroplastic/mitochondrial
- Presequence protease 2, chloroplastic/mitochondrial
- SIT4 phosphatase-associated family protein
- At1g07990/T6D22_5
- SIT4 phosphatase-associated family protein
- Tripeptidyl-peptidase 2
- Subtilisin-like protease SBT4.15
- Subtilisin-like protease SBT1.8
- Serine carboxypeptidase-like 26
- Alpha/beta-Hydrolases superfamily protein
Sequence:
MASEDTLSSNPLLQNFDFPPFDSVDAHHVRPGIRALLQQLEAELEQLEKAVEPSWPKLVEPLEKIIDRLSVVWGMINHLKAVKDTPELRAAIEEVQPEKVKFQLRLGQSKPIYNAFKAIRESPDWNSLSEARQRLVEAQIKEAVLSGIALEDDKREEFNKIEQELEKLSHKFSENVLDATKKFEKLITDKKEIEGLPPSALGLFAQAAVSKGHETATADTGPWLITLDAPSYLPVMQHAKNRALREEVYRAYLSRASSGDLDNTAIIDQILKLRLEKAKLLGYRNYAEVSMATKMATVEKADELLEKLRSASWDPAVQDIEDLKSFAKNQGAAEADSLTHWDITFWSERLRESKYDINEEELRPYFSLPKVMDALFGLAKTLFGIDVVPADGVAPVWNSDVRFYCVKDSSGNPTAYFYFDPYSRPSEKRDGAWMDEVFSRSRVMAQKGSSVRLPVAQMVCNQTPPVGDKPSLMTFREVETVFHEFGHALQHMLTKEDEGLVAGIRNIEWDAVELPSQFMENWCYHRDTLMSIAKHYQTGETLPENVYKKLLAARTFRAGSLSLRQLKFATVDLELHTKYMPGGAETIYEVDQRVSIKTQVIPPLPEDRFLCSFSHIFAGGYAAGYYSYKWAEVLSADAFSAFEDAGLDDIKAVKETGQRFRNTILALGGGKAPLKVFVEFRGREPSPEPLLRHNGLLAASA
Protein: GDH/6PGL endoplasmic bifunctional protein [Includes: Hexose-6-phosphate dehydrogenase (Glucose 1-dehydrogenase) (GDH) (EC 1.1.1.47) (Glucose-6-phosphate dehydrogenase) (EC 1.1.1.363); 6-phosphogluconolactonase (6PGL) (EC 3.1.1.31)] (O95479)
Organism: Homo sapiens (Human)
Function: Bifunctional enzyme localized in the lumen of the endoplasmic reticulum that catalyzes the first two steps of the oxidative branch of the pentose phosphate pathway/shunt, an alternative to glycolysis and a major source of reducing power and metabolic intermediates for biosynthetic processes (By similarity). Has a hexose-6-phosphate dehydrogenase activity, with broad substrate specificity compared to glucose-6-phosphate 1-dehydrogenase/G6PD, and catalyzes the first step of the pentose phosphate pathway. In addition, acts as a 6-phosphogluconolactonase and catalyzes the second step of the pentose phosphate pathway (By similarity). May have a dehydrogenase activity for alternative substrates including glucosamine 6-phosphate and glucose 6-sulfate (By similarity). The main function of this enzyme is to provide reducing equivalents such as NADPH to maintain the adequate levels of reductive cofactors in the oxidizing environment of the endoplasmic reticulum. By producing NADPH that is needed by reductases of the lumen of the endoplasmic reticulum like corticosteroid 11-beta-dehydrogenase isozyme 1/HSD11B1, indirectly regulates their activity.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000305|PubMed:18628520}.
Interaction partners:
- Glucose-6-phosphate isomerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Glucose-6-phosphate 1-dehydrogenase
- 6-phosphogluconolactonase
- Probable gluconokinase
- Glyceraldehyde-3-phosphate dehydrogenase
- RNA-binding protein 45
- Hexokinase-4
- L-lactate dehydrogenase A chain
- Transaldolase
Sequence:
MWNMLIVAMCLALLGCLQAQELQGHVSIILLGATGDLAKKYLWQGLFQLYLDEAGRGHSFSFHGAALTAPKQGQELMAKALESLSCPKDMAPSHCAEHKDQFLQLSQYRQLKTAEDYQALNKDIEAQLQHAGLREAGRIFYFSVPPFAYEDIARNINSSCRPGPGAWLRVVLEKPFGHDHFSAQQLATELGTFFQEEEMYRVDHYLGKQAVAQILPFRDQNRKALDGLWNRHHVERVEIIMKETVDAEGRTSFYEEYGVIRDVLQNHLTEVLTLVAMELPHNVSSAEAVLRHKLQVFQALRGLQRGSAVVGQYQSYSEQVRRELQKPDSFHSLTPTFAAVLVHIDNLRWEGVPFILMSGKALDERVGYARILFKNQACCVQSEKHWAAAQSQCLPRQLVFHIGHGDLGSPAVLVSRNLFRPSLPSSWKEMEGPPGLRLFGSPLSDYYAYSPVRERDAHSVLLSHIFHGRKNFFITTENLLASWNFWTPLLESLAHKAPRLYPGGAENGRLLDFEFSSGRLFFSQQQPEQLVPGPGPAPMPSDFQVLRAKYRESPLVSAWSEELISKLANDIEATAVRAVRRFGQFHLALSGGSSPVALFQQLATAHYGFPWAHTHLWLVDERCVPLSDPESNFQGLQAHLLQHVRIPYYNIHPMPVHLQQRLCAEEDQGAQIYAREISALVANSSFDLVLLGMGADGHTASLFPQSPTGLDGEQLVVLTTSPSQPHRRMSLSLPLINRAKKVAVLVMGRMKREITTLVSRVGHEPKKWPISGVLPHSGQLVWYMDYDAFLG
Protein: Vacuolar protein sorting-associated protein 29 (Vesicle protein sorting 29) (F8VXU5)
Organism: Homo sapiens (Human)
Subcellular location: Endosome membrane {ECO:0000256|ARBA:ARBA00004481}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004481}.
Interaction partners:
Sequence:
MSRCALRGRDLALAIAGTVSFHGLLRLFRAGHRLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERIEYKKP