wanglab/gogpt-training-data huggingface dataset:
Protein: Fumarate hydratase, mitochondrial (Fumarase) (EC 4.2.1.2) (P14408)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate (By similarity). Experiments in other species have demonstrated that specific isoforms of this protein act in defined pathways and favor one direction over the other (Probable).
Subcellular location: [Isoform Mitochondrial]: Mitochondrion {ECO:0000269|PubMed:2914923}.; SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm, cytosol {ECO:0000269|PubMed:2914923}. Nucleus {ECO:0000250|UniProtKB:P07954}. Chromosome {ECO:0000250|UniProtKB:P07954}. Note=Translocates to the nucleus in response to DNA damage: localizes to DNA double-strand breaks (DSBs) following phosphorylation by PRKDC. {ECO:0000250|UniProtKB:P07954}.
Interaction partners:
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Malate dehydrogenase, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Malate dehydrogenase, cytoplasmic
- Citrate synthase, mitochondrial
- NADP-dependent malic enzyme
- Malic enzyme
- Malic enzyme
Sequence:
MNRAFCLLARSRRFPRVPSAGAVLSGEAATLPRCAPNVVRMASQNSFRIEYDTFGELKVPTDKYYGAQTVRSTMNFKIGGATERMPIPVIKAFGILKRAAAEVNQEYGLDPKIASAIMKAADEVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKKPVHPNDHVNKSQSSNDTFPTAMHIAAALEVHQVLLPGLQKLHDALSAKSKEFAQVIKIGRTHTQDAVPLTLGQEFSGYVQQVQYAMERIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK
Protein: Ketimine reductase mu-crystallin (EC 1.5.1.25) (NADP-regulated thyroid-hormone-binding protein) (I3NI53)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRVPAFLSAAEVEEHLRSSSLLIPPLETALANFSSGPEGGVMQPVRTVVPVTKHRGYLGVMPAYSAAEDALTTKLVTFYEDRGITSVVPSHQATVLLFEPSNGTLLAVMDGNVITAKRTAAVSAIATKFLKPPSSEVLC
Protein: N-acetylaspartate synthetase (NAA synthetase) (EC 2.3.1.17) (N-acetyltransferase 8-like protein) (Protein Shati) (Q3UGX3)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of N-acetylaspartate acid (NAA) from L-aspartate and acetyl-CoA. Promotes dopamine uptake by regulating TNF-alpha expression. Attenuates methamphetamine-induced inhibition of dopamine uptake (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F0}. Microsome membrane {ECO:0000250|UniProtKB:D3ZVU9}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q8N9F0}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:19807691}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Aspartoacylase
- N-acetylaspartylglutamate synthase A
- Beta-citrylglutamate synthase B
- Glutamate carboxypeptidase 2
- Asparagine synthetase
- Putative aspartate aminotransferase, cytoplasmic 2
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Isoaspartyl peptidase/L-asparaginase
- Argininosuccinate synthase
Sequence:
MHCGPPDMVCETKIVATEDHEALPGAKKDALLVAAGAMWPPLPAAPGPAAAPPPAAGPQPHGGTGGAGPPEGRGVCIREFRAAEQEAARRIFYDGILERIPNTAFRGLRQHPRTQLLYALLAALCFAVTRSLLLTCLVPAGLLALRYYYSRKVILAYLECALHTDMADIEQYYMKPPGSCFWVAVLDGNVVGIVAARAHEEDNTVELLRMSVDSRFRGKSIAKALGRRVLEFAMLHNYSAVVLGTTAVKVAAHKLYESLGFRHMGASDHYVLPGMTLSLAERLFFQVRYHRYRLQLREE
Protein: ATP-dependent RNA helicase DDX3Y (EC 3.6.4.13) (DEAD box protein 3, Y-chromosomal) (O15523)
Organism: Homo sapiens (Human)
Function: Probable ATP-dependent RNA helicase. During immune response, may enhance IFNB1 expression via IRF3/IRF7 pathway (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15294876, ECO:0000269|PubMed:15383328}. Nucleus {ECO:0000269|PubMed:15383328}. Note=Shuttles between the nucleus and the cytoplasm in an XPO1-dependent manner.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 9Y
- Histone demethylase UTY demethylase UTY)
- Eukaryotic translation initiation factor 1A, Y-chromosomal
- Lysine-specific demethylase 5D
- Zinc finger Y-chromosomal protein
- Small ribosomal subunit protein eS4, Y isoform 1
- Putative serine/threonine-protein kinase PRKY
- Thymosin beta-4, Y-chromosomal
- Small ribosomal subunit protein eS4, Y isoform 2
- Deleted in azoospermia protein 1
Sequence:
MSHVVVKNDPELDQQLANLDLNSEKQSGGASTASKGRYIPPHLRNREASKGFHDKDSSGWSCSKDKDAYSSFGSRDSRGKPGYFSERGSGSRGRFDDRGRSDYDGIGNRERPGFGRFERSGHSRWCDKSVEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGSNCPPHIENFSDIDMGEIIMGNIELTRYTRPTPVQKHAIPIIKGKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALKAVKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEDLDKRSFLLDILGATGSDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVRHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNEKNMNITKDLLDLLVEAKQEVPSWLENMAYEHHYKGGSRGRSKSNRFSGGFGARDYRQSSGSSSSGFGASRGSSSRSGGGGYGNSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN
Protein: Macrophage receptor MARCO (Macrophage receptor with collagenous structure) (Q60754)
Organism: Mus musculus (Mouse)
Function: Pattern recognition receptor (PRR) which binds Gram-positive and Gram-negative bacteria. Also plays a role in binding of unopsonized particles by alveolar macrophages (By similarity). Binds to the secretoglobin SCGB3A2 (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:7867067}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Apolipoprotein B-100
Sequence:
MGSKELLKEEDFLGSTEDRADFDQAMFPVMETFEINDPVPKKRNGGTFCMAVMAIHLILLTAGTALLLIQVLNLQEQLQMLEMCCGNGSLAIEDKPFFSLQWAPKTHLVPRAQGLQALQAQLSWVHTSQEQLRQQFNNLTQNPELFQIKGERGSPGPKGAPGAPGIPGLPGPAAEKGEKGAAGRDGTPGVQGPQGPPGSKGEAGLQGLTGAPGKQGATGAPGPRGEKGSKGDIGLTGPKGEHGTKGDKGDLGLPGNKGDMGMKGDTGPMGSPGAQGGKGDAGKPGLPGLAGSPGVKGDQGKPGVQGVPGPQGAPGLSGAKGEPGRTGLPGPAGPPGIAGNPGIAGVKGSKGDTGIQGQKGTKGESGVPGLVGRKGDTGSPGLAGPKGEPGRVGQKGDPGMKGSSGQQGQKGEKGQKGESFQRVRIMGGTNRGRAEVYYNNEWGTICDDDWDNNDATVFCRMLGYSRGRALSSYGGGSGNIWLDNVNCRGTENSLWDCSKNSWGNHNCVHNEDAGVECS
Protein: HAUS augmin-like complex subunit 1 (Coiled-coil domain-containing protein 5) (Enhancer of invasion-cluster) (HEI-C) (Q96CS2)
Organism: Homo sapiens (Human)
Function: Contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex.
Subcellular location: Cytoplasm {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15082789, ECO:0000269|PubMed:19369198, ECO:0000269|PubMed:19427217, ECO:0000269|PubMed:30723163}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000305|PubMed:19369198}. Note=Localizes with the spindle poles in mitotic cells. In metaphase, localizes to the mitotic asters and is highly punctate on the microtubule array. During later stages of mitosis, remains on the spindle but is not present at the interzone, and is finally observed at the microtubule bundles proximal to the midbody, clearly excluded from the midbody. In contrast, does not colocalize with the tubulin cytoskeleton in interphase cells. In interphase, localized at the centrosome and diffusely in the cytoplasm. Localizes to mitotic spindle microtubules. {ECO:0000269|PubMed:15082789, ECO:0000269|PubMed:30723163}.
Interaction partners:
- HAUS augmin-like complex subunit 4
- HAUS augmin-like complex subunit 3
- HAUS augmin-like complex subunit 8
- HAUS augmin-like complex subunit 2
- HAUS augmin-like complex subunit 5
- HAUS augmin-like complex subunit 6
- HAUS augmin-like complex subunit 7
- Tubulin gamma-1 chain
- Protein NEDD1
- Pericentriolar material 1 protein
Sequence:
MEPQEERETQVAAWLKKIFGDHPIPQYEVNPRTTEILHHLSERNRVRDRDVYLVIEDLKQKASEYESEAKYLQDLLMESVNFSPANLSSTGSRYLNALVDSAVALETKDTSLASFIPAVNDLTSDLFRTKSKSEEIKIELEKLEKNLTATLVLEKCLQEDVKKAELHLSTERAKVDNRRQNMDFLKAKSEEFRFGIKAAEEQLSARGMDASLSHQSLVALSEKLARLKQQTIPLKKKLESYLDLMPNPSLAQVKIEEAKRELDSIEAELTRRVDMMEL
Protein: PsbP-like protein 1, chloroplastic (OEC23-like protein 4) (PsbP-related thylakoid lumenal protein 2) (P82538)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for efficient repair of photodamaged PSII, but not tightly associated with the complex.
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000269|PubMed:11719511, ECO:0000269|PubMed:18431481}.
Interaction partners:
- Oxygen-evolving enhancer protein 2-1, chloroplastic
- Protein CURVATURE THYLAKOID 1B, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- Chlorophyll a-b binding protein 3, chloroplastic
- Chlorophyll a-b binding protein CP26, chloroplastic
- Putative oxygen-evolving enhancer protein 2-2
- Chlorophyll a-b binding protein 2.2, chloroplastic
- Photosystem II stability/assembly factor HCF136
- Photosystem II 22 kDa protein, chloroplastic
- Light-harvesting complex-like protein 3 isotype 1, chloroplastic
Sequence:
MASLKLSPSSPISISKVGVIPSSKKGLSFLVKAEHHSSSSSSHLQDKCQRRLIVTFGVVAPWISLLSRAPLSFAAESKKGFLAVSDNKDAYAFLYPFGWQEVVIEGQDKVYKDVIEPLESVSVNLVPTSKQTIKEFGPPKQIAETLIKKVLAPPNQKTTLIDASEHDVDGKTYYQFEFTVQARNYTRHALGTITVFNGNFYTLTTGANERRWEKMKDRLHTVVDSFKITV
Protein: Phospholipase (EC 3.1.4.4) (C8V1Q0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Phosphatidate cytidylyltransferase
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Phosphatidylserine decarboxylase family protein
- Phosphatidylserine decarboxylase proenzyme 2
- PAP2 domain protein
- PAP2 domain protein
- diacylglycerol cholinephosphotransferase
- Lipin Smp2, putative
- Phosphatidylethanolamine N-methyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
Sequence:
MSHFKEKIHDLEEHMKDSHISEKAHHLKHRVGKFFNIVNPNHRHDEEHEKETDRKRTAICESNRFGSFAPVRQGNKVKWYVDALDYLWAVSIALEQAKEVIYIEDWWLSPELFLRRPPLTAQEWRLDQVLKRKAEAGVKIYVIVYKEVNQALTCNSAHTKYALRALCPEGSPGHGNINLLRHPDHNIFENAADMTLYWAHHEKFIVIDYNVAFIGGIDLCFGRWDTHQHPLADVHPSNLRMEIFPGQEFNNNRIMDFQSVGEWQSNELSKAEYGRMPWHDVAMGVIGDCVYDIAEHFVLRWNFIKRDKYKRDPTVDWLLLEGRTGKDEDLVGVQRPKFPVGDYVQHPYKPLNTKPMGAQGSCTAQIVRSSADWSSGILVEHSIQNAYKDIINKAEHFVYIENQFFITATGDQQSPILNTIGRSIVDACVRAGKEGRKFRVIIVIPAIPGFAGDLRQNEATGTRAIMDYQYKSINRGEHSIFGQIAAQGVDPTNHIFVFNLRAYDRINKTPALEELEKEAGVTFNDIQRGVAETLTSESVHPSVGKEGDKNEINYGGAEKEREERIARLQKYEERNKAHEAHSTANNKDSVSHTTMLHGGKMSDEVWEGDPEAEKENFIQEELYVHGKVCIVDDRVAICGSANINDRSQLGYHDSELAIVVEDQDFIDSTMDGKPYKAARHAATLRRQLWREHLGLLPAQNYDASEHPNAQPPTICMNEILEGPENDFVTDPMNDNLWKTWTDQATVNTNIYRQLFRTDPDDNIRTFEEYDKYRAKDGYKLGHLYDPFIPVQEVREKLDKIKGHLVWMPLDFLKDAEMAEPGLQVNQYTESIYT
Protein: Cullin family profile domain-containing protein (Q583G1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA damage-binding protein 1
- COP9 signalosome complex subunit 5
- TATA-binding protein interacting
- RING-type domain-containing protein
- RING-type domain-containing protein
- COP9 signalosome complex subunit 3 N-terminal helical repeats domain-containing protein
- Ubiquitin, putative
- Cullin, putative
- COP9 signalosome complex subunit 4
- JAB1/MPN/MOV34 metalloenzyme domain-containing protein
Sequence:
MKTSLPPPLIAEETSSDGLSYEEKLRQAYAAGETKRPQYLSASLRDLFEVTLNRELLLFRNEETETPVTRRKKWLQWYNEIYNSLRCTHNVNALLLYWVTGIVSYELREMERCLAGIREREREKSGEQQLPPQGQGVPDENVTFEGEKSLEAIQHAMELRNVIRRLPALVAFFFAWDMNLGDTSKFEELLHKVIIDNFSEGAELLLLEQLLTWTLRWCRQLQWKGTNSSAKLPPPLRQQLQTALADICQLIMLFSCDARTAERRIIVTALRSVVEGCEMYFNRHALLAMLERKANNVETRQVFVLERWPQYWLSELTILGDIPSVDKEWVKAIMLNMALLWNPESLSGEGMASGVEGSPVDADDTYLFHLLLLTLQPMFDNLFGVPAVDNKEFTPSTANSQSVEALSTERTTSGEKKDPLKLLLEVADVMACIGSPLCRDIHYWDCIGVGPLLTQNVANGNKDIGSFVMASVCRRLLQEQIPLSVNSFLLSNDAPKKQLQRLITYLIRTERVFDCLCGIQALKACLLGTRTSDNDTKGCFYYILETALANHQHQLRGASALVEELLYNVYEYLLRGNETSPATGNGSLSGNEDLRAALRIIQGLSGRTQLFSFYKENLAIRLLSILHPKPHDNAVSTEELRHERLQFEGSMCRYLMELFPGDREAVQHMVQMCEDVKTANEMSEAFNQQQMQDIGNAALSVKLTTSILSPHAWPVYPKLERVPRPLKNTMDGFSAFYQNRHSTRRLIWIRTTFERVTFDIAYPRGKKLVTGSLEHYEIFNCLSEAAGAGVTWENLAKEVEWETAKLQQELRKPIFNGLLVLPQEEEAKVAERADTASQQALRLNPEFTSSHTHFNLLPERSQRKQLTTCTRTNEKAAKGLQETRIGAIQAAVMHRLKTVQHGSYKDLFQFTQESLRHHFQLSDVEFKEVLRRLIDKEYIVRDQEDREQFVYRA
Protein: Coiled-coil domain-containing protein 120 (Q96HB5)
Organism: Homo sapiens (Human)
Function: Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells. Together with CCDC68, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly. Recruits NIN and CEP170 to centrosomes. Also required for neurite growth. Localizes CYTH2 to vesicles to allow its transport along neurites, and subsequent ARF6 activation and neurite growth.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:28422092}. Cytoplasm {ECO:0000269|PubMed:25326380}. Cell projection, neuron projection {ECO:0000269|PubMed:25326380}. Cell projection, growth cone {ECO:0000269|PubMed:25326380}. Endosome {ECO:0000269|PubMed:25326380}. Note=Localizes to the subdistal appendages of mother centrioles and proximal ends of both centrioles in interphase cells (PubMed:28422092). Recruited to subdistal appendages by ODF2 (PubMed:28422092). In differentiating neuroblastoma cells, colocalizes with CYTH2 in both neurite shaft and growth cone areas (PubMed:25326380). Partially colocalizes with endosomes along neurites in differentiating neuroblastoma cells (PubMed:25326380). {ECO:0000269|PubMed:25326380, ECO:0000269|PubMed:28422092}.
Interaction partners:
- Coiled-coil domain-containing protein 68
- Centrosomal protein of 170 kDa
- Centrosomal protein of 128 kDa
- Ninein
- Centriolin
- Outer dense fiber protein 2
- Cytohesin-2
- Dynactin subunit 1
- Kinesin-like protein KIF2A
- Cytohesin-3
Sequence:
MEVKGQLISSPTFNAPAALFGEAAPQVKSERLRGLLDRQRTLQEALSLKLQELRKVCLQEAELTGQLPPECPLEPGERPQLVRRRPPTARAYPPPHPNQAHHSLCPAEELALEALEREVSVQQQIAAAARRLALAPDLSTEQRRRRRQVQADALRRLHELEEQLRDVRARLGLPVLPLPQPLPLSTGSVITTQGVCLGMRLAQLSQEDVVLHSESSSLSESGASHDNEEPHGCFSLAERPSPPKAWDQLRAVSGGSPERRTPWKPPPSDLYGDLKSRRNSVASPTSPTRSLPRSASSFEGRSVPATPVLTRGAGPQLCKPEGLHSRQWSGSQDSQMGFPRADPASDRASLFVARTRRSNSSEALLVDRAAGGGAGSPPAPLAPSASGPPVCKSSEVLYERPQPTPAFSSRTAGPPDPPRAARPSSAAPASRGAPRLPPVCGDFLLDYSLDRGLPRSGGGTGWGELPPAAEVPGPLSRRDGLLTMLPGPPPVYAADSNSPLLRTKDPHTRATRTKPCGLPPEAAEGPEVHPNPLLWMPPPTRIPSAGERSGHKNLALEGLRDWYIRNSGLAAGPQRRPVLPSVGPPHPPFLHARCYEVGQALYGAPSQAPLPHSRSFTAPPVSGRYGGCFY
Protein: Large ribosomal subunit protein uL18z (60S ribosomal protein L5-1) (Ribosomal protein L5 A) (Protein ASYMMETRIC LEAVES1/2 ENHANCER 6) (Protein OLIGOCELLULA 5) (Protein PIGGYBACK 3) (Q8LBI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
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. Seems involved in the regulation of cell proliferation. Essential in leaf polarity establishment, probably having a role for translation in leaf dorsoventral patterning to specify leaf adaxial identity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18305007}. Nucleus {ECO:0000269|PubMed:18305007}. Nucleus, nucleolus {ECO:0000269|PubMed:18305007}. Nucleus, nucleoplasm {ECO:0000269|PubMed:18305007}.
Interaction partners:
- Probable elongation factor 1-gamma 2
- Large ribosomal subunit protein eL28z
- Large ribosomal subunit protein eL24y
- Small ribosomal subunit protein eS6z
- Large ribosomal subunit protein eL32z
- Large ribosomal subunit protein uL3z
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein eL19x
- Large ribosomal subunit protein uL23y
Sequence:
MVFVKSTKSNAYFKRYQVKFRRRRDGKTDYRARIRLINQDKNKYNTPKYRFVVRFTNKDIVAQIVSASIAGDIVKASAYAHELPQYGLTVGLTNYAAAYCTGLLLARRVLKMLEMDDEYEGNVEATGEDFSVEPTDSRRPFRALLDVGLIRTTTGNRVFGALKGALDGGLDIPHSDKRFAGFHKENKQLDAEIHRNYIYGGHVSNYMKLLGEDEPEKLQTHFSAYIKKGVEAESIEELYKKVHAAIRADPNPKKTVKPAPKQHKRYNLKKLTYEERKNKLIERVKALNGAGGDDDDEDDEE
Protein: Multi-heme protein MamP (EC 1.-.-.-) (Magnetochrome MamP) (Magnetosome-associated protein MamP) (Q2W8Q1)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Involved in redox-control of magnetite formation; oxidizes Fe(2+) to Fe(3+) or to mixed-valent Fe(2+)-Fe(3+) oxide minerals. May control magnetite crystal size and number (Probable). Overproduction of MamP leads to more crystals than normal during exponential growth of normal size; in stationary phase crystal numbers become wild-type.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:25048532}; Single-pass membrane protein {ECO:0000305|PubMed:25048532}. Note=Not seen in magnetosome membranes. {ECO:0000269|PubMed:25048532}.
Interaction partners:
- Probable membrane transporter protein MamO
- Magnetosome protein MamB
- Magnetosome protein MamR
- Magnetosome protein MamT
- Magnetosome protein MamS
- Magnetosome protein MamQ 1
- Magnetosome protein MamM
- Magnetosome protein MamN
- Magnetosome protein MamA
- Magnetosome formation protease MamE
Sequence:
MNSKVALLVVGLAVVLALVIGRQGPVAPQATNTQSQAVAAGPVAAPVAFPQPLYPQAANVAMPVEPDPAAGGGTAPATESPLPNFVPRKLKVFEGHWQGMDGRLMTEELARKLNYPRGLQGVLLGEVTLNAAFSGLLAGDLIVRIDDTPVTDMESFKAASRTVANRSDARISVLRKDNRPGAPVVRKLTVVLREAEGGLGFAQLEGAPMILAGDPRPHGYRGACTDCHPIGQGFELTPDPDLISLPPPTITRDMVARSVNPHEVRGPCEACHVIK
Protein: Uncharacterized protein (Q585A6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 3-beta hydroxysteroid dehydrogenase/isomerase domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- NADH-ubiquinone oxidoreductase complex I subunit
- NADH-ubiquinone oxidoreductase, mitochondrial, putative
- Uncharacterized protein
- NADH dehydrogenase 1 beta subcomplex subunit 8
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Complex 1 LYR protein domain-containing protein
- FAD-binding domain-containing protein
Sequence:
MRCVRSAAVLVKFGRSFDSTTRFGKELGFSHKMRDIPVLTGNPRPVAREEEWSCRYKLTDRMEDVVMDILKKEGWCEAEVQREMSEIFERKTQGCRSSLNTWTTVEEFQRTPWYRRYKPTDTCVAKYISYEVVKLLEEALIPPSLRGDPYAHLRKRHMEDNWMNDRFSEEAAKYIQREDLNKHTKGLPQYGQITRRKFLEFDRQFKESYGGKQHVNEAYSAWLQSIGKG
Protein: Extracellular tyrosine-protein kinase PKDCC (EC 2.7.10.2) (Protein kinase domain-containing protein, cytoplasmic) (Protein kinase-like protein SgK493) (Sugen kinase 493) (Vertebrate lonesome kinase) (Q5RJI4)
Organism: Mus musculus (Mouse)
Function: Secreted tyrosine-protein kinase that mediates phosphorylation of extracellular proteins and endogenous proteins in the secretory pathway, which is essential for patterning at organogenesis stages. Mediates phosphorylation of MMP1, MMP13, MMP14, MMP19 and ERP29. May also have serine/threonine protein kinase activity. Required for longitudinal bone growth through regulation of chondrocyte differentiation. May be indirectly involved in protein transport from the Golgi apparatus to the plasma membrane. Probably plays a role in platelets: rapidly and quantitatively secreted from platelets in response to stimulation of platelet degranulation.
Subcellular location: Secreted {ECO:0000269|PubMed:25171405}. Golgi apparatus {ECO:0000269|PubMed:19465597}. Note=Both secreted and present in the Golgi apparatus. {ECO:0000269|PubMed:19465597, ECO:0000269|PubMed:25171405}.
Interaction partners:
Sequence:
MRRRRAAVAAGFCASFLLGSVLNVLFAPGSEPPRPGQSPGSSAAPGPGRRGGRGELARQIRERYEEVQRYSRGGPGPGAGRPERRRLMDLAPGGPGLQRPRPPRVRSPPDGAPGWPPAPGPGSPGPGPRLGCAALRNVSGAQYVGSGYTKAVYRVRLPGGAAVALKAVDFSGHDLGSCVREFGARRGCYRLAAHKLLKEMVLLERLRHPNVLQLYGYCYQDSEGIPDTLTTITELGAPVEMIQLLQTSWEDRFRICLSLGRLLHHLAHSPLGSVTLLDFRPRQFVLVNGELKVTDLDDARVEETPCTSSADCTLEFPARNFSLPCSAQGWCEGMNEKRNLYNAYRFFFTYLLPHSAPPSLRPLLDSIVNATGELAWGVDETLAQLETALHLFRSGQYLQNSTSSRAEYQRIPDSAITQEDYRCWPSYHHGGCLLSVFNLAEAIDVCESHAQCRAFVVTNQTTWTGRKLVFFKTGWNQVVPDAGKTTYVKAPG
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform B (EC 3.4.23.-)) (Q9VQ13)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cathepsin B, isoform A)
- cathepsin L
- Cathepsin L1
- Mucin related 11Da
- FI04419p
- Uncharacterized protein, isoform B
- Cathepsin F
- MIP16848p
- IP19042p
- Femcoat
Sequence:
MRVRWNHFKLLLFWLTVLAVLAFEAEARKRVRIGLHKNPEPIEENIKNELKTLSIKHNLNVDDTKAKTKTDTKVPGSKVATLENLYNTEYYTTLGFGNPPQDLKVLIDTGSANLWVLSSKCPDSVAPCANRIKYNSSASTTYRAINTAFNIAYGSNSEEGPIALSGFQSQDTVNFAGYSIKNQIFAEITNAPETAFLKSQLDGILGLGFASIAINSITPPFYNLMAQGLVNRSVFSIYLNRNGTNAINGGELILGGSDSGLYSGCLTYVPVSSAGYWQFTMTSANLNGFQFCENCEAILDVGTSLIVVPEQVLDTINQILGVLNPTASNGVFLVDCSSIGDLPDIVFTVARRKFPLKSSDYVLRYGNTCVSGFTSMNGNSLLILGEIFLGAYYTTYDIVYKLIGLAPAIH
Protein: Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3 (Membrane-associated guanylate kinase inverted 3) (MAGI-3) (Scaffolding-like protein) (Q9JK71)
Organism: Rattus norvegicus (Rat)
Function: Acts as a scaffolding protein at cell-cell junctions, thereby regulating various cellular and signaling processes. Cooperates with PTEN to modulate the kinase activity of AKT1. Its interaction with PTPRB and tyrosine phosphorylated proteins suggests that it may link receptor tyrosine phosphatase with its substrates at the plasma membrane. In polarized epithelial cells, involved in efficient trafficking of TGFA to the cell surface. Regulates the ability of LPAR2 to activate ERK and RhoA pathways. Regulates the JNK signaling cascade via its interaction with FZD4 and VANGL2.
Subcellular location: Cell membrane; Peripheral membrane protein. Cell junction, tight junction. Nucleus. Note=Concentrates in specific sites at the plasma membrane and in the nucleus. In epithelial cells, it localizes at tight junctions.
Interaction partners:
- Catenin beta-1
- Rap guanine nucleotide exchange factor 2
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1
- Rap guanine nucleotide exchange factor 6
- Lysophosphatidic acid receptor 2
- Frizzled-4
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- SH3 domain-binding protein 4
- Vang-like protein 2
Sequence:
MSKTLKKKKHWLSKVQECAVSWAGPPGDLGAEIRGGAERGEFPYLGRLRDEPGGGGGTCCVVSGKAPSPGDVLLEVNGTPVSGLTNRDTLAVIRHFREPIRLKTVKPGKVINKDLRHYLSLQFQKGSIDHKLQQVIRDNLYLITIPCTTRAPRDGEVPGVDYNFISVEQFKALEESGALLESGTYDGNFYGTPKPPAEPSPFQPDPVDQVLFDNEFDTESQRKRTTSVSKMERMDSSLPEEEEDEDKEAVNGSGSMETREMHSESSDCWMKTVPSYNQTNRSMDFRNYMMRDENLEPLPKNWEMAYTDTGTIYFIDHNTKTTTWLDPRLCKKAKAPEDCEDGELPYGWEKIEDPQYGTYYVDHLNQKTQFENPVEEAKRKKQIGQAETHSAKTDVERAHFTRDPSQLKGVLVRASLKKSTMGFGFTIIGGDRPDEFLQVKNVLKDGPAAQDGKMAPGDVIVDINGNCVLGHTHADVVQMFQLVPVNQYVNLTLCRGYALPDDSEDPVVDIVAATPVINGQSLAKGEACMSTQDFKLGAMVLDQNGKSGKLLSSDRLNGPSDSNEQRASLASSGSSQPELVTIPLVKGPKGFGFAIADSPTGQKVKMILDSQWCQGLQKGDIIKEIYHQNVQNLTHLQVVEVLKQFPVGADVPLLILRGGPCSPTKTAKMKTDTKETSGSLETINEPTPQPMPFPPSIIRSGSPKLDPSEVYLKSKTLYEDKPPNTKDLDVFLRKQESGFGFRVLGGDGPDQSIYIGAIIPLGAAEKDGRLRAADELMCIDGIPVKGKSHKQVLDLMTTAARNGHVLLTVRRKIFYGEKQPEDESPQAFSQSGSPRLNRTELPTRSAPQESYDVILQRKENEGFGFVILTSKSKPPPGVIPHKIGRVIDGSPADRCGRLKVGDHISAVNGQSIVDLSHDNIVQLIKDAGVTVTLTVVAEEEHHGPPSGTNSARQSPALQHRPMGQAQATHIPGDRTALEGEVGKDVCSSYRHSWSDHKHLAQPDTAVISVVGSRHSQSLGCYPVELERGPRGFGFSLRGGKEYNMGLFILRLAEDGPAIKDGRIHVGDQIVEINGEPTQGITHTRAIELIQAGGNKVLLLLRPGTGLIPDHGDWDIYSPSSSNVIYDEQPPPLPSSHSAATFEESHVPVTEDSLIRVQTCEKAEELKDTVQEKKSTLNGSQPEMKYQSIQKNVSKKDPSRSHGHGDKNLLKGENGVTRRGRSASPKKSVNRHSEEHLEKIPRPLRSDPKGKSRDRSLSPRKGENKGQVTIKAGSGQDPCRKDRGRSSSPRKQQKIGGNSLSNTEGKLSEAGSRRAAGLSSDSPEQLPEGKEKSGVSRKDLKLSQLGKNRTRSPEKRSSKVDEASLPSKKTSDTASRVVSEKEKGRKPGTGERSRDKTGESVQTSAKPLTQEAGEKMALSKASEVTDRGKERAGGAPESSSPVKKAPITPGPWRVPRANKVTGTAGMADKQL