wanglab/gogpt-training-data huggingface dataset:
Protein: Protein DETOXIFICATION 48 (AtDTX48) (Multidrug and toxic compound extrusion protein 48) (MATE protein 48) (Protein ABNORMAL SHOOT 4) (Protein BUSH-AND-CHLOROTIC-DWARF 1) (Protein BCD1) (Protein ZRIZI) (Q9SLV0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as a multidrug and toxin extrusion transporter. Contributes to iron homeostasis during stress responses and senescence. Could be involved in specifying the lateral organ initiation rate. May act as a negative regulator of hypocotyl cell elongation in the light.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:22150160}; Multi-pass membrane protein {ECO:0000269|PubMed:22150160}. Late endosome membrane {ECO:0000269|PubMed:26160579}; Multi-pass membrane protein {ECO:0000269|PubMed:26160579}.
Interaction partners:
- Protein DETOXIFICATION 46, chloroplastic
- Protein DETOXIFICATION 43
- Protein DETOXIFICATION 42
- Protein DETOXIFICATION 44, chloroplastic
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 8
- Protein DETOXIFICATION 47, chloroplastic
- Uncharacterized protein
Sequence:
MCNSKPSSASSSLLSCKDKTHISKLETCDTDNPHYSEFRDTDSLDLKRWPSFLEGLEEVKAIGKISGPTAMTGLLMYSRAMISMLFLGYLGELELAGGSLSIGFANITGYSVISGLSMGMEPICGQAYGAKQMKLLGLTLQRTVLLLLSCSVPISFSWLNMRRILLWCGQDEEISSVAQQFLLFAIPDLFLLSLLHPLRIYLRTQNITLPVTYSTAVSVLLHVPLNYLLVVKLEMGVAGVAIAMVLTNLNLVVLLSSFVYFTSVHSDTWVPITIDSLKGWSALLSLAIPTCVSVCLEWWWYEFMIILCGLLANPRATVASMGILIQTTALVYVFPSSLSLGVSTRISNELGAKRPAKARVSMIISLFCAIALGLMAMVFAVLVRHHWGRLFTTDAEILQLTSIALPIVGLCELGNCPQTTGCGVLRGCARPTLGANINLGSFYFVGMPVAILFGFVFKQGFPGLWFGLLAAQATCASLMLCALLRTDWKVQAERAEELTSQTPGKSPPLLPIASSKSRSTSGTEDMMRTMLV
Protein: Ribonuclease P/MRP protein subunit RPP1 (EC 3.1.26.5) (RNA-processing protein RPP1) (RNaseP/MRP 32.2 kDa subunit) (P38786)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribonuclease P/MRP protein subunit POP5
- Ribonucleases P/MRP protein subunit POP3
- Ribonucleases P/MRP protein subunit POP6
- Ribonuclease P protein subunit RPR2
- Ribonuclease MRP protein subunit RMP1
- Ribonucleases P/MRP protein subunit POP7
- Ribonucleases P/MRP protein subunit POP1
- Ribonucleases P/MRP protein subunit POP8
- RNases MRP/P 32.9 kDa subunit
- Ribonuclease MRP protein subunit SNM1
Sequence:
MLVDLNVPWPQNSYADKVTSQAVNNLIKTLSTLHMLGYTHIAINFTVNHSEKFPNDVKLLNPIDIKRRFGELMDRTGLKLYSRITLIIDDPSKGQSLSKISQAFDIVAALPISEKGLTLSTTNLDIDLLTFQYGSRLPTFLKHKSICSCVNRGVKLEIVYGYALRDVQARRQFVSNVRSVIRSSRSRGIVIGSGAMSPLECRNILGVTSLIKNLGLPSDRCSKAMGDLASLVLLNGRLRNKSHKQTIVTGGGSGNGDDVVNDVQGIDDVQTIKVVKRSMDAEQLGHASKRHKP
Protein: Pcr1 (TyeA) (TyeA family type III secretion system gatekeeper subunit) (O30532)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MAYGPSELTGAVIALLEKRWVGVAEVQALLEPLPLADVARQIHFFRELKRLYRLLPVEVFGDDEQRQNLLNACQMALDLAIEREEEQQHGLG
Protein: Vinculin (A0A3B6UES5)
Organism: Oscarella pearsei (Sponge)
Function: Actin filament (F-actin)-binding protein which may play a role in cell-cell adhesion.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:29880641}. Cell projection, filopodium {ECO:0000269|PubMed:29880641}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:29880641}. Note=Localizes to points of cell-cell contact in the pinacoderm. Localizes to the base of the microvillar collar in choanocytes. Detected in filopodial extensions in migratory cells of the mesohyl. Colocalizes with F-actin. {ECO:0000269|PubMed:29880641}.
Interaction partners:
Sequence:
MPVKFHTKTLESVIDPVAQQVGQLVLFHEQAESGLLKEDLTPLVQGVGIAVTNLVQVAASMVETSNDEDFKAELPPSMQEVQQAAVFLSDAARLLKADQGSPEGKRKLLDGARGVINGMSDLLMCADRSEVRKMVKVCRSVQEYLDVAKVIDVEADLATFLQNLTPGMTSMMKVVEQRHPELTNLAHAQMLKSELGTVREQIPILISSIRVCCLVIVKDGSSGMKDAAFGRDYVIQKLFIAIEEIIRVLQLTTTFEEEEVGGAGAASAASLAHMFHQAQDALASGDISRSTLDAVRKCISEGRRVAALAATDETRAKLLAAADELDQILKELEELQAKGLGDSRQARALAHAAAVKLQELEQEIRKALAERVATDFVNVGGPIKALEDAALASPSDPNRQANFAQKAKEFEAHTARLADTAELVASSGGCSDAVAAELRKEAAKLRDISTAVVPAARVVLENPGNQAAKDYLRTVKEKWLEAAESMGRSVDGVIDSLEFMKVSEARIQADVKEAKRIALAEEDSMKLIAKASSVARQANRVIQVAKVEADNSENPEFVAKLSSASESLAKSISPMVIEAKAVVTSPQNKDIQRKFCSSADKVVEGVAAVRSVIEDNWVPPRPPLPELEEEEEPPELPPPPEDPASLLPAEMQEAEEMLRAPLPPKDQNPIHHAAASVFREADQWDEKGNDLISLVKQMARKMAMMSKYTRGESGEVRSKADLIRMAKEIALNAQELLKLARQIANACMDKRAKTNLLQLLDRIPTISTQLKILATVKATSMGGGDARADADATDMLVGNAENLMRTVKDVIRASEAACIRLRPDSPIASILWRKKGGQGRRISVSY
Protein: Cytochrome b-c1 complex subunit 10 (Complex III subunit 10) (Complex III subunit XI) (Ubiquinol-cytochrome c reductase complex 6.4 kDa protein) (O14957)
Organism: Homo sapiens (Human)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. QCR10 has a role in CIII assembly and RIP1 stability.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P37299}; Single-pass membrane protein {ECO:0000250|UniProtKB:P37299}.
Interaction partners:
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit 9
- Cytochrome c oxidase subunit 7A1, mitochondrial
Sequence:
MVTRFLGPRYRELVKNWVPTAYTWGAVGAVGLVWATDWRLILDWVPYINGKFKKDN
Protein: Histone H3.1t (H3/t) (H3t) (H3/g) (Histone H3.4) (Q16695)
Organism: Homo sapiens (Human)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H4-like protein type G
- WD repeat-containing protein 5
- Histone H4
- Chromobox protein homolog 5
- Histone H2A type 2-C
- Histone H2B type 2-E
- Histone H2A type 2-A
- Chromobox protein homolog 3
- Lysine-specific demethylase 4A demethylase 4A) demethylase 4A)
- DNA
Sequence:
MARTKQTARKSTGGKAPRKQLATKVARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLMREIAQDFKTDLRFQSSAVMALQEACESYLVGLFEDTNLCVIHAKRVTIMPKDIQLARRIRGERA
Protein: Ubiquitin carboxyl-terminal hydrolase 22 (EC 3.4.19.12) (Deubiquitinating enzyme 22) (Ubiquitin thioesterase 22) (Ubiquitin-specific-processing protease 22) (Q5DU02)
Organism: Mus musculus (Mouse)
Function: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:27013495}. Cytoplasm {ECO:0000269|PubMed:35900990}.
Interaction partners:
- Ataxin-7-like protein 3
- Transcription and mRNA export factor ENY2
- Histone acetyltransferase KAT2A
- SAGA-associated factor 29
- Ataxin-7
- Transcriptional adapter 3
- Transcription initiation factor TFIID subunit 10
- Transformation/transcription domain-associated protein
- Transcription initiation factor TFIID subunit 12
- SPT3, SAGA and STAGA complex component
Sequence:
MVARPEPEVEAMDAELAVPPPGCSHLGSFKVDNWKQNLRAIYQCFVWSGTAEARKRKAKSCVCHVCGIHLNRLHSCLYCVFFGCFTKKHIHDHAKSKRHNLAIDLMYGGIYCFLCQDYIYDKDIEIIAKEEQRKAWKMQGVGEKFSTWEPTKRELELLKHNPKRRKITSNCTIGLRGLINLGNTCFMNCIVQALTHTPLLRDFFLSDRHRCEMQSPSSCLVCEMSSLFQEFYSGHRSPHIPYKLLHLVWTHARHLAGYEQQDAHEFLIAALDVLHRHCKGDDNGKKANNPNHCNCIIDQIFTGGLQSDVTCQVCHGVSTTIDPFWDISLDLPGSSTPFWPLSPGSEGSVVNGESHASGTTTLTDCLRRFTRPEHLGSSAKIKCSGCHSYQESTKQLTMKKLPIVACFHLKRFEHSAKLRRKITTYVSFPLELDMTPFMASSKESRMNGQYQQPLDSLNNDNKYSLFAVVNHQGTLESGHYTSFIRQHKDQWFKCDDAIITKASIKDVLDSEGYLLFYHKQFLEYE
Protein: Cathepsin D (EC 3.4.23.5) [Cleaved into: Cathepsin D light chain; Cathepsin D heavy chain] (Q05744)
Organism: Gallus gallus (Chicken)
Function: Acid protease active in intracellular protein breakdown. In chicken it is a key enzyme for yolk formation as it is capable of catalyzing intra oocytic break down of protein components of both vitellogenin and VLDL.
Subcellular location: Lysosome.
Interaction partners:
- Apoptosis regulator Bcl-2
- Cathepsin B
- Bcl-2-like protein 1
- Lysosome-associated membrane glycoprotein 1
- BH3-interacting domain death agonist
- Uncharacterized protein
- Procathepsin L
- Angiotensinogen
- Uncharacterized protein
- Pept_C1 domain-containing protein
Sequence:
MAPRGLLVLLLLALVGPCAALIRIPLTKFTSTRRMLTEVGSEIPDMNAITQFLKFKLGFADLAEPTPEILKNYMDAQYYGEIGIGTPPQKFTVVFDTGSSNLWVPSVHCHLLDIACLLHHKYDASKSSTYVENGTEFAIHYGTGSLSGFLSQDTVTLGNLKIKNQIFGEAVKQPGITFIAAKFDGILGMAFPRISVDKVTPFFDNVMQQKLIEKNIFSFYLNRDPTAQPGGELLLGGTDPKYYSGDFSWVNVTRKAYWQVHMDSVDVANGLTLCKGGCEAIVDTGTSLITGPTKEVKELQTAIGAKPLIKGQYVISCDKISSLPVVTLMLGGKPYQLTGEQYVFKVSAQGETICLSGFSGLDVPPPGGPLWILGDVFIGPYYTVFDRDNDSVGFAKCV
Protein: Herpes virus entry mediator (Tumor necrosis factor receptor superfamily, member 14 (Herpesvirus entry mediator)) (Q71F55)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MEPLPGWGSAPWSQAPTDNTFRLVPCVFLLNLLQRISAQPSCRQEEFLVGDECCPMCNPGYHVKQVCSEHTGTVCAPCPPQTYTAHANGLSKCLPCGVCDPDMGLLTWQECSSWKDTVCRCIPGYFCENQDGSHCSTCLQHTTCPPGQRVEKRGTHDQDTVCADCLTGTFSLGGTQEECLPWTNCSAFQQEVRRGTNSTDTTCSSQVVYYVVSILLPLVIVGVGIAGFLICTRRHLHTSSVAKELEPFQQEQQENTIRFPVTEVGFAETEEETASN
Protein: Cation/H(+) symporter 13 (Protein CATION/H+ EXCHANGER 13) (AtCHX13) (O22920)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-affinity potassium transporter that plays a role in K(+) acquisition. May operate as a K(+)/H(+) symporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18676662}; Multi-pass membrane protein {ECO:0000269|PubMed:18676662}.
Interaction partners:
- Uncharacterized protein F7J8_130
- K
- Heavy metal-associated isoprenylated plant protein 42
- Calcium-binding EF hand family protein
- Leucine-rich repeat protein kinase family protein
- K
- F-actin-capping protein subunit alpha
- K
- Potassium transporter 5
- Probable magnesium transporter NIPA2
Sequence:
MELSMFGREDTNSSQWGEVHGPFMLEEIVCQAQNMLTSRGIFMKSNPLKYALPLLLLQMSVIIVTSRLIFRVLQPLKQGMISAQVLTGVVLGPSFLGHNVIYMNMFLPAGGKIIIQTLSNVGFVIHLFLLGLKIDGSIIRKAGSKAILIGTASYAFPFSLGNLTIMFISKTMGLPSDVISCTSSAISLSSMTSFPVTTTVLAELNILNSELGRLATHCSMVCEVCSWFVALAFNLYTRDRTMTSLYALSMIIGLLLVIYFVFRPIIVWLTQRKTKSMDKKDVVPFFPVLLLLSIASLSGEAMGVHAAFGAFWLGVSLPDGPPLGTELAAKLEMFASNLFLPCFIAISGLQTNFFEITESHEHHVVMIEIILLITYGCKFLGTAAASAYCQTQIGDALCLAFLMCCQGIIEVYTTIVWKDAQVVDTECFNLVIITILFVTGISRFLVVYLYDPSKRYKSKSKRTILNTRQHNLQLRLLLGLYNVENVPSMVNLLEATYPTRFNPISFFTLHLVELKGRAHALLTPHHQMNKLDPNTAQSTHIVNAFQRFEQKYQGALMAQHFTAAAPYSSINNDICTLALDKKATLIVIPFHKQYAIDGTVGQVNGPIRTINLNVLDAAPCSVAIFIDRGETEGRRSVLMTNTWQNVAMLFIGGKDDAEALALCMRMAEKPDLNVTMIHFRHKSALQDEDYSDMSEYNLISDFKSYAANKGKIHYVEEIVRDGVETTQVISSLGDAYDMVLVGRDHDLESSVLYGLTDWSECPELGVIGDMLTSPDFHFSVLVVHQQQGDDLLAMDDSYKLPNVEHQKIGDTGIQQRFSAEEGFTTIDLGKR
Protein: N-alpha-acetyltransferase 60 (hNaa60) (EC 2.3.1.259) (Histone acetyltransferase type B protein 4) (HAT4) (EC 2.3.1.48) (N-acetyltransferase 15) (N-alpha-acetyltransferase F) (NatF) (Q9H7X0)
Organism: Homo sapiens (Human)
Function: N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol. Displays N-terminal acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:21981917, ECO:0000269|PubMed:25732826, ECO:0000269|PubMed:38480682}; Peripheral membrane protein {ECO:0000269|PubMed:25732826}; Cytoplasmic side {ECO:0000269|PubMed:25732826}. Note=Probably forms an intramembrane hairpin-like structure in the membrane. {ECO:0000305|PubMed:25732826}.
Interaction partners:
- N-alpha-acetyltransferase 10
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 50
- N-alpha-acetyltransferase 40
- N-alpha-acetyltransferase 80
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
- N-alpha-acetyltransferase 11
- N-alpha-acetyltransferase 30
- Zinc finger protein 597
Sequence:
MTEVVPSSALSEVSLRLLCHDDIDTVKHLCGDWFPIEYPDSWYRDITSNKKFFSLAATYRGAIVGMIVAEIKNRTKIHKEDGDILASNFSVDTQVAYILSLGVVKEFRKHGIGSLLLESLKDHISTTAQDHCKAIYLHVLTTNNTAINFYENRDFKQHHYLPYYYSIRGVLKDGFTYVLYINGGHPPWTILDYIQHLGSALASLSPCSIPHRVYRQAHSLLCSFLPWSGISSKSGIEYSRTM
Protein: Protein kinase D2 (M0QZC2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MLFGLVRQGLKCDDCKFNCHKRCATRVPNDCLGEALINGDVPMEEATDFSEADKSALMDESEDSGVIPGSHSENALHASEEEEGEGGKAQSSLG
Protein: Uncharacterized protein YhiN (P37631)
Organism: Escherichia coli (strain K12)
Interaction partners:
Sequence:
MERFDAIIIGAGAAGMFCSALAGQAGRRVLLIDNGKKPGRKILMSGGGRCNFTNLYVEPGAYLSQNPHFCKSALARFTQWDFIDLVNKHGIAWHEKTLGQLFCDDSAQQIVDMLVDECEKGNVTFRLRSEVLSVAKDETGFTLDLNGMTVGCEKLVIATGGLSMPGLGASPFGYKIAEQFGLNVLPTRAGLVPFTLHKPLLEELQVLAGVAVPSVITAENGTVFRENLLFTHRGLSGPAVLQISSYWQPGEFVSINLLPDVDLETFLNEQRNAHPNQSLKNTLAVHLPKRLVERLQQLGQIPDVSLKQLNVRDQQALISTLTDWRVQPNGTEGYRTAEVTLGGVDTNELSSRTMEARKVPGLYFIGEVMDVTGWLGGYNFQWAWSSAWACAQDLIAAKSS
Protein: Glucosyltransferase 3 (EC 2.4.1.-) (B5A7L9)
Organism: Streptococcus parasanguinis
Function: Required for polymorphic O-glycosylation of the serine-rich repeat protein Fap1. Catalyzes the second step in glycosylation of the serine-rich repeat protein in this bacteria. Transfers glucose from UDP-glucose to the terminal GlcNAc moiety of 3-O-(N-acetyl-alpha-D-glucosaminyl)-L-seryl-[protein] which results from the first glycosylation step of Fap1; does not use other sugar nucleotides as substrates.
Interaction partners:
Sequence:
MRVYITNINGQSIQSTAQLCQNTVTDVAVSLGYRELGIYCYQIHTDSESELSKRLDGIVAGLRHGDVVIFQTPTWNTTEFDEKLMNKLKLYDIKIVLFIHDVVPLMFSGNFYLMDRTIAYYNKADVVVAPSQKMIDKLRDFGMNVSKTVVQGMWDHPTQAPMFPAGLKREIHFPGNPERFSFVKEWKYDIPLKVYTWQNVELPQNVHKINYRPDEQLLMEMSQGGFGLVWMDDKDKEYQSLYCSYKLGSFLAAGIPVIVQEGIANQELIENNGLGWIVKDVEEAIMKVKNVNEDEYIELVKNVRSFNPILRKGFFTRRLLTESVFQAICD
Protein: Probable mitochondrial-processing peptidase subunit beta, mitochondrial (EC 3.4.24.64) (Beta-MPP) (Complex III subunit I) (Core protein I) (Cytochrome b-c1 complex subunit 1, mitochondrial) (Ubiquinol-cytochrome c oxidoreductase core protein 1) (Q42290)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (By similarity). Preferentially, cleaves after an arginine at position P2 (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}. Mitochondrion inner membrane {ECO:0000269|PubMed:18189341}; Peripheral membrane protein {ECO:0000250|UniProtKB:P07256}; Matrix side {ECO:0000250|UniProtKB:P07256}.
Interaction partners:
- Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
- Cytochrome b-c1 complex subunit 7-2, mitochondrial
- Probable mitochondrial-processing peptidase subunit alpha-1, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome c1 1, heme protein, mitochondrial
- Cytochrome c1 2, heme protein, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 9
- Cytochrome b-c1 complex subunit 7-1, mitochondrial
- Cytochrome b-c1 complex subunit Rieske-2, mitochondrial
Sequence:
MAMKNLLSLARRSQRRLFLTQATRSSSSFSAIDSVPASASPTALSPPPPHLMPYDHAAEIIKNKIKKLENPDKRFLKYASPHPILASHNHILSAPETRVTTLPNGLRVATESNLSAKTATVGVWIDAGSRFESDETNGTAHFLEHMIFKGTDRRTVRALEEEIEDIGGHLNAYTSREQTTYYAKVLDSNVNQALDVLADILQNSKFEEQRINRERDVILREMQEVEGQTDEVVLDHLHATAFQYTPLGRTILGPAQNVKSITREDLQNYIKTHYTASRMVIAAAGAVKHEEVVEQVKKLFTKLSSDPTTTSQLVANEPASFTGSEVRMIDDDLPLAQFAVAFEGASWTDPDSVALMVMQTMLGSWNKNVGGGKHVGSDLTQRVAINEIAESIMAFNTNYKDTGLFGVYAVAKADCLDDLSYAIMYEVTKLAYRVSDADVTRARNQLKSSLLLHMDGTSPIAEDIGRQLLTYGRRIPTAELFARIDAVDASTVKRVANKYIYDKDIAISAIGPIQDLPDYNKFRRRTYWNRY
Protein: Keratin-associated protein 9-3 (Keratin-associated protein 9.3) (Ultrahigh sulfur keratin-associated protein 9.3) (Q9BYQ3)
Organism: Homo sapiens (Human)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated proteins (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
- Keratin-associated protein 9-4
- Keratin-associated protein 3-1
- Keratin-associated protein 17-1
- Keratin-associated protein 9-8
- Keratin-associated protein 4-1
- Keratin-associated protein 4-5
- Keratin-associated protein 4-3
- Keratin-associated protein 1-3
- Keratin-associated protein 3-2
- Keratin-associated protein 4-8
Sequence:
MTHCCSPCCQPTCCRTTCWQPTTVTTCSSTPCCQPSCCVSSCCQPCCHPTCCQNTCCRTTCCQPICVTSCCQPSCCSTPCCQPTCCGSSCGQSSSCAPVYCRRTCYHPTSVCLPGCLNQSCGSNCCQPCCRPACCETTCCRTTCFQPTCVYSCCQPSCC
Protein: Small ribosomal subunit protein eS6A (40S ribosomal protein S6-A) (RP9) (S10) (YS4) (P0CX37)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. eS6 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}.
Interaction partners:
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein uS8B
- Small ribosomal subunit protein uS8A
- U3 small nucleolar RNA-associated protein MPP10
- Small ribosomal subunit protein eS7A
- Small ribosomal subunit protein uS17A
- Small ribosomal subunit protein uS4A
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL24A
- Small ribosomal subunit protein eS30A
Sequence:
MKLNISYPVNGSQKTFEIDDEHRIRVFFDKRIGQEVDGEAVGDEFKGYVFKISGGNDKQGFPMKQGVLLPTRIKLLLTKNVSCYRPRRDGERKRKSVRGAIVGPDLAVLALVIVKKGEQELEGLTDTTVPKRLGPKRANNIRKFFGLSKEDDVRDFVIRREVTKGEKTYTKAPKIQRLVTPQRLQRKRHQRALKVRNAQAQREAAAEYAQLLAKRLSERKAEKAEIRKRRASSLKA
Protein: Rho guanine nucleotide exchange factor 9 (Collybistin) (Rac/Cdc42 guanine nucleotide exchange factor 9) (Q3UTH8)
Organism: Mus musculus (Mouse)
Function: Acts as guanine nucleotide exchange factor (GEF) for CDC42. Promotes formation of GPHN clusters (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9QX73}. Postsynaptic density {ECO:0000269|PubMed:27609886}.
Interaction partners:
- Gephyrin
- Cell division control protein 42 homolog
- Neuroligin-2
- Gamma-aminobutyric acid receptor subunit alpha-2
- Gamma-aminobutyric acid receptor subunit gamma-2
- IQ motif and SEC7 domain-containing protein 3
- Glycine receptor subunit beta
- Gamma-aminobutyric acid receptor subunit alpha-1
Sequence:
MYDLITGDSIVSAEAVWDHVTMANRELAFKAGDVIKVLDASNKDWWWGQIDDEEGWFPASFVRLWVNQEDGVEEGPSDVQNGHLDPNSDCLCLGRPLQNRDQMRANVINEIMSTERHYIKHLKDICEGYLKQCRKRRDMFSDEQLKVIFGNIEDIYRFQMGFVRDLEKQYNNDDPHLSEIGPCFLEHQDGFWIYSEYCNNHLDACMELSKLMKDSRYQHFFEACRLLQQMIDIAIDGFLLTPVQKICKYPLQLAELLKYTAQDHSDYRYVAAALAVMRNVTQQINERKRRLENIDKIAQWQASVLDWEGEDILDRSSELIYTGEMAWIYQPYGRNQQRVFFLFDHQMVLCKKDLIRRDILYYKGRIDMDKYEVIDIEDGRDDDFNVSMKNAFKLHNKETEEVHLFFAKKLEEKIRWLRAFREERKMVQEDEKIGFEISENQKRQAAMTVRKASKQKGVNSARSVPPSYPPPQDPLNQGQYLVPDGIAQSQVFEFTEPKRSQSPFWQNFSRLTPFKK
Protein: Lipoprotein signal peptidase (EC 3.4.23.36) (Prolipoprotein signal peptidase) (Signal peptidase II) (SPase II) (P00804)
Organism: Escherichia coli (strain K12)
Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:1894646, ECO:0000269|PubMed:6368552}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00161, ECO:0000269|PubMed:1894646, ECO:0000269|PubMed:6368552}.
Interaction partners:
- Isoleucine--tRNA ligase
- Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
- Apolipoprotein N-acyltransferase
- Signal peptidase I
- Outer-membrane lipoprotein carrier protein
- Outer-membrane lipoprotein LolB
- FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerase
- Bifunctional riboflavin kinase/FMN adenylyltransferase
- Major outer membrane lipoprotein Lpp
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
Sequence:
MSQSICSTGLRWLWLVVVVLIIDLGSKYLILQNFALGDTVPLFPSLNLHYARNYGAAFSFLADSGGWQRWFFAGIAIGISVILAVMMYRSKATQKLNNIAYALIIGGALGNLFDRLWHGFVVDMIDFYVGDWHFATFNLADTAICVGAALIVLEGFLPSRAKKQ