wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-crystallin B chain (Alpha(B)-crystallin) (Q9PUR2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Alpha-crystallin A chain
- BCL2-associated athanogene 3.
- Beta-crystallin B2
- Actin alpha 1, skeletal muscle b.
- Beta A1-crystallin
- Beta-crystallin B3
- Myotilin
- Crystallin, beta B1
- Heat shock protein beta-2
- Beta-crystallin A4
Sequence:
MEISIQHPWYRRPLFPGFFPYRIFDQYFGEHLSDSDPFSPFYTMFYYRPYLWRFPSWWDSGMSEMRQDRDRFVINLDVKHFSPDELTVKVNEDFIEIHGKHDERQDDHGIVAREFFRKYKIPAGVDPGAITSSLSSDGVLTINTLRHQLDILERSIPIICGEKPPAQK
Protein: Presequence translocated-associated motor subunit pam17, mitochondrial (O94539)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner.
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- DnaJ protein homolog xdj1
- Mitochondrial import inner membrane translocase subunit tim23
- Mitochondrial import inner membrane translocase subunit tim16
- Mitochondrial import inner membrane translocase subunit tim44
- Mitochondrial import inner membrane translocase subunit tim17
- Mitochondrial import inner membrane translocase subunit tim14
- Polyphosphoinositide phosphatase
- Protein mgr2
- Protein VAC14 homolog
- Pre-mRNA-splicing factor cwf23
Sequence:
MIPIIRPGLVVKRLQSPKIFLTLWKTCYNVKTYSTESIKQKKPQDLNWPTFLKLRKSRRIFETLTSIPTALTGLGLGSAYFLTRTVDPTMTIMGLDLFTLYVIGTIASGGLGWLLGPSIGRKIWTLLHKSQARQIAAREQEFYRHLVKNRVTPQMESYSNPIPDYYGEKIYSLSDYRRWLRDQKAYIQRAFWRTSNR
Protein: Serum paraoxonase/arylesterase 1 (PON 1) (EC 3.1.1.2) (EC 3.1.1.81) (EC 3.1.8.1) (Aromatic esterase 1) (A-esterase 1) (Serum aryldialkylphosphatase 1) (P55159)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification.
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Apolipoprotein A-II
- Phosphatidylcholine-sterol acyltransferase
- Clusterin
- Apolipoprotein A-I
- Apolipoprotein C-I
- Apolipoprotein B-100
- Apolipoprotein E
- Apolipoprotein M
- Apolipoprotein C-III
- Phospholipid transfer protein
Sequence:
MAKLLGLTLVGLVLALYKNHRSSYQTRLNAFREVTPVDLPNCTLVKGIEAGAEDLEILPNGLTFFSTGLKYPGIKSFDPSKPGKILLMDLNEKEPAVSELAIMGNTLDMSSFNPHGISTFIDEDNTVYLLVVSHPDSSSTVEVFKFQEEERSLLHLKTITHELLPSINDIAAVGPESFYATNDHYFADPYLRSWEMYLGLSWSNVVYYSPDKVRVVADGFDFANGIGISLDGKYVYIAELLAHKIHVYEKHANWTLTPLKVLSFDTLVDNISVDPVTGDLWVGCHPNGMRIFFYDSENPPGSEVLRIQSILSEDPKVTVVYAENGTVLQGTTVAAVYKGKLLIGTVFHRALCCDL
Protein: Prefoldin subunit (Q382P3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Prefoldin subunit, putative
- Prefoldin subunit 2, putative
- Prefoldin subunit
Sequence:
MSGVSRGESDPSHAPADAAMGSMLRLEHFLDAVLRQSLARVLAQRDEVYNMASNCCQLRSLFDEMQSLSSTHSFIRRDEGSSTALTVSAAVAAGEGKQSVGNATVVRGAGSTSGDVSVQQRNHIMVDLGNHFFVQCTVTDASRMWVNLGCGVVLPMFRDEALVFLQRRERLLRERAARLSKEALRIKYRMRLVMEAITRLYDRTTGRKATWKG
Protein: D-serine dehydratase (EC 4.3.1.18) (D-serine deaminase) (DSD) (Q9US35)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Converts specifically D-serine to pyruvate and ammonia. May play a role in D-serine detoxification (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Serine racemase
- Threonine dehydratase, mitochondrial
- Lactoylglutathione lyase
- Glutathione-independent glyoxalase hsp3102
- Putative glutathione-independent glyoxalase hsp3105
- Probable glutathione-independent glyoxalase hsp3103
- Probable glutathione-independent glyoxalase hsp3104
- Glutathione-independent glyoxalase hsp3101
- Enhancer of rudimentary homolog 1
Sequence:
MASNVDKFSSRFYLNVNKEELKKEYVGKTIQQVPTPGFVIDEAIFEKNCNRMLDRASDIGVTFRAHVKTHKTIEGTLLQLGDGRTKAVVVSTLMEGFSLIPLILEGKIDDLLYGLPVAKSRLPELYELSKIVPHLRLMIDNPKQLDILREFTSTLPDDAKPWSIFVKIDMGTHRAGVTNDSQVVKDLISTILSDKSLFDLFGFYCHAGHSYASRSIDAASEFLCAEIDAANTAAKFATSIDPSLKLTLSVGATPTAHSVSPKVKELLPTLSGKLEVHAGNYPMNDVQQMITKCISQADVADYVFAEVISNYPGRNGEPGEVLVNAGVIAMSRETSPEGDFGIVITPGFESFYVDRLSQEHGILKSKDPKATLPDASQVLCIIPNHSCITAAAFPWYYITKGSDVITDIWVPWKGW
Protein: Photosystem II reaction center protein L (PSII-L) (Q2LIN0)
Organism: Oryza barthii
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid, chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01317}; Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01317}.
Interaction partners:
Sequence:
MTQSNPNEQNVELNRTSLYWGLLLIFVLAVLFSNYFFN
Protein: Decapping and exoribonuclease protein 1 (KlDxo1) (EC 3.6.1.-) (5'-3' exoribonuclease Dxo1) (EC 3.1.13.-) (NAD-capped RNA hydrolase Dxo1) (DeNADding enzyme Dxo1) (EC 3.6.1.-) (Q6CPU0)
Organism: Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Function: Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA. The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (By similarity). In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (By similarity). Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation. Has decapping and 5'-3' exonuclease activities. Has decapping activity toward incomplete 5'-end cap mRNAs such as unmethylated 5'-end-capped RNA to release GpppN and 5'-end monophosphate RNA. The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q06349}.
Interaction partners:
- 5'-3' exoribonuclease 2
- Decapping nuclease RAI1
- KLLA0C10758p
- Phosphodiesterase
- Ribosomal RNA-processing protein 42
Sequence:
MTTVSCDKDENKVDQLGESLSQLRISTRKNNKPSQKKGSLVLSCKKFPHVSVNYVVDKTPKLLTDCKEVHNCSYIINDATLLWNEASRKPRLRPEVCTYIKDSKWENKAVKDSFIGIDLTKGYDDYVPLDRNVLNSLVILKEAYQRYEKTLNPEKTTFVSLRHHIIDIIMCPFLDEPLSLLMTVQPDKNILISVDKSKDKPNGIHETRNSFNKKICYTGFALEDLLIESPTEGHILEHELYYSIVHGSLNDEIDLLIQAEMDSINTLTDTYTEIKSSVHFKLGNTYHRRKLLRMWIQTNLLPKSDLLIGFRNSYSNELEQLKAYKIQDIYHKINNSSIVGKPGKFYKFNPNVANDWFQHIFQVLKQNLLLLSQESTSTTFKVQIDTNLTLSISPASQFVTALG
Protein: Regulatory protein, putative (Q887S8)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Interaction partners:
- RNA polymerase sigma-70 family protein
- Regulatory protein, putative
- RNA polymerase sigma-70 family protein
- RNA polymerase sigma-70 family protein
- TonB-dependent siderophore receptor, putative
- TonB-dependent siderophore receptor
- RNA polymerase sigma-70 family protein
- RNA polymerase sigma-70 family protein
- TonB-dependent siderophore receptor, putative
- TonB-dependent siderophore receptor
Sequence:
MNLSNDSLNKSDISPAVAQQAVGWLLEMQEGALDARRQHAWQSWLNGNSEHQRAWAHMQRVNQRLSGLSSPLAHAALGAPKSAGRRHALKLLLLLGAGSMAGWSLREQIALQPLLADYNSGVGEQRKVALSDGSRVQLNTASAVDVRFDAQQRLIKLLQGELLMSASADARPLNLLSAQGTVRASTGSSRFNLRQLDGRTQLAVFAGAIEVAPANKSGPGLMLRASQQVTFGRDAWDSVRTVDANSGAWADGMLVASRMKLSDFLAELGRYRRGRLNCDANVADLLISGSYPLADSERILDMLQLALPVRVQRFTRYWVNVQARV
Protein: Putative preprotein translocase, SecE subunit (A0A0H2URR7)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MRFIGDIFRLLKDTTWPTRKESWRDFRSIMEYTAFFVVIIYIFDQLIVSGLIRFINIF
Protein: DNA replication inhibitor plutonium (P42570)
Organism: Drosophila melanogaster (Fruit fly)
Function: Inhibits DNA replication early in developments. May bind and block the action of a replication or initiation factor.
Interaction partners:
- CG5272 protein
- non-specific serine/threonine protein kinase
- Mitosis initiation protein fs
Sequence:
MGEINALSCVGQDDVVSLRIVCTMARDGKQHNLEDVDMYGNTALLKACYLGRFECARTLLEFGANIFAMNYFGQNALTLATYAGHLTLVKELLRRRSYKDFNLSSMIPALCVATLQKHSALVAYFTQLDSRGVQETQTVHGLGVAELRGMIKAAGRLDKRNVRSPPTFISNRLR
Protein: Integrin alpha-11 (P61622)
Organism: Mus musculus (Mouse)
Function: Integrin alpha-11/beta-1 is a receptor for collagen.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Integrin beta-1
- Integrin beta-5
- Integrin beta-3
- Collagen alpha-2
- Integrin beta-8
- Integrin beta-7
- Collagen alpha-1
- Collagen alpha-2
- Integrin beta-6
- Fibronectin
Sequence:
MDFPRGLLVAWTLSLWPGFTDTFNMDTRNPRVIAGPSAAFFGYTVQQHDISGKKWLVVGAPMETNGHQKTGDVYKCPVTQGNCTKLNLGRVTLSNVSERKDNMRLGLSLATNPKDNSFLACSPLWSHECGSSYYTTGMCSRANSNFRFSKTVAPALQRCQTYMDIVIVLDGSNSIYPWVEVQHFLINILKKFYIGPGQIQVGIVQYGEDAVHEFHLNDYRSVKDVVEAASHIEQRGGTETRTAFGIEFARSEAFQKGGRKGAKKVMIVITDGESHDSPDLEKVIRQSEKDNVTRYAVAVLGYYNRRGINPETFLNEIKYIASDPDDKHFFNVTDEAALKDIVDALGDRIFSLEGTNKNETSFGLEMSQTGFSSHVVEDGILLGAVGAYDWNGAVLKETSAGKVIPHRESYLKEFPEELKNHAAYLGYTVTSVVSSRQGRVYVAGAPRFNHTGKVILFSMHNNRSLTIHQALRGEQIGSYFGSEITSVDVNDDRVTDVLLVGAPMYFSEGRERGKVYVYNLRQNRFVYNGTLKDSHSYQNARFGSCIASVQDLNQDSYNDVVVGAPLEDSHRGAIYIFHGFQTNILKKPMQRITASELAPGLQHFGCSIHGQLDLNEDGLVDLAVGALGNAVVLWARPVVQINASLHFEPSKINIFHKDCKRNGRDATCLAAFLCFIPIFLAPHFQTATVGIRYNATMDERRYMPRAHLDEGGDQFTNRAVLLSSGQEHCQRINFHVLDTADYVKPVAFSVEYSLEDPDNGPMLDNGWPTTLRVSVPFWNGCNEDEHCVPDLVLDARSDLPTAMEYCQRVLGRPAQDCSSYTLSFDTTVFIIESTRRRVAVEATLENRGENAYSAVLNISQSENLQFASLIQKDDSDNSIECVNEERRLHKKVCNVSYPFFRAKAKVAFRLDFEFSKSVFLHHLQIHLGAGSDSHEQDSTADDNTALLRFHLKYEADVLFTRSSSLSHFEVKANSSLESYDGIGPPFNCVFKVQNLGFFPIHGVMMKITVPIATRGGNRLLMLRDFFTDQGNTSCNIWGNSTEYRSTPTEEDLSHAPQRNHSNSDVVSIICNLRLAPSQETSFYLVGNLWLTSLKALKYRSLKITVNAALQRQFHSPFIFREEDPSRQVTFEISKQEDWQVPIWIIVGSTLGGLLLLALLVLALWKLGFFKSAKRKREPGLGPIPKELK
Protein: Toxin Tma3 (C0HLM1)
Organism: Tityus macrochirus (Scorpion)
Function: Inhibits voltage-gated sodium channels (Nav). This toxin shows insect lethality against crickets.
Subcellular location: Secreted {ECO:0000269|PubMed:31402191}.
Interaction partners:
Sequence:
KKDDYPVDTAKRNCKFPCNVIDKEGYCDNLCKGRKAEKGYCYRLNASCYCYGLPDDSPTKKSGRCNPNL
Protein: Echinoderm microtubule-associated protein-like 1 (EMAP-1) (Q05BC3)
Organism: Mus musculus (Mouse)
Function: Modulates the assembly and organization of the microtubule cytoskeleton, and probably plays a role in regulating the orientation of the mitotic spindle and the orientation of the plane of cell division. Required for normal proliferation of neuronal progenitor cells in the developing brain and for normal brain development. Does not affect neuron migration per se.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24859200}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:24859200}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24859200}. Note=Detected in cytoplasmic punctae. Co-localizes with microtubules. Enriched in perinuclear regions during interphase and in the region of spindle microtubules during metaphase. Enriched at the midzone during telophase and cytokinesis. Detected at growth cones in neurons. {ECO:0000269|PubMed:24859200}.
Interaction partners:
Sequence:
MEDGFSSYSSLYDTSSLLQFCNDDSASAASSMEVSDRIASLEQRVQMQEDDIQLLKSALADVVRRLNITEEQQAVLNRKGPTKARPLGQTLPLRTTVNNGTVLPKKPSASLPAPSGARKEVVVPVTKSINRTSSSERVSPGGRRESSGDSKGSRNRTGSTSSSSSGKKNSESKPKEPAFSPEEGYVKMFLRGRPVTMYMPKDQVDSYSLEAKAELPTKRLKLEWVYGYRGRDCRNNLYLLPTGETVYFIASVVVLYNVEEQLQRHYAGHNDDVKCLAVHPDRITIATGQVAGTSKDGKQLPPHVRIWDSVTLNTLHVIGIGFFDRAVTCIAFSKSNGGGHLCAVDDSNDHVLSVWDWQKEERLADVKCSNEAVFAADFHPTDTNIIVTCGKSHLYFWTLEGNSLNKKQGLFEKQEKPKFVLCVTFSENGDTITGDSSGNILVWGKGTNRISYAVQGAHEGGIFALCMLRDGTLVSGGGKDRRLISWNGNYQKLHKAEIPEQFGPIRTVAEGKGNVILIGTTRNFVLQGTLSGDFTPITQGHTDELWGLAIHASKPQFLTCGHDKHATLWDAVGHRPVWDKIIEDPAQSSGFHPSGSVVAVGTLTGRWFVFDTETKDLVTVHTDGNEQLSVMRYSPDGNFLAIGSHDNCIYIYGVTDNGRKYTRVGKCSGHSSFITHLDWSVNSQFLVSNSGDYEILYWVPSACKQVVSVETTRDIEWATYTCTLGFHVFGVWPEGSDGTDINAVCRAHERKLLCTGDDFGKVHLFSYPCSQFRAPSHIYSGHSSHVTNVDFLCEDSHLISTGGKDTSIMQWRVI
Protein: Small ribosomal subunit protein bS1m (28S ribosomal protein S28, mitochondrial) (MRP-S28) (S28mt) (P82928)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10751423, ECO:0000269|PubMed:10938081, ECO:0000269|PubMed:24799711}.
Interaction partners:
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein mS40
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein bS21m
- Small ribosomal subunit protein mS26
Sequence:
MAALCRTRAVTAESHFLRVFLFSRSCRGAGTESGSGSESSNSTEPRPRPGGFASALERHSELQRKAELARTRGSPKNVESFASMLRHSPLTQMGPAKDKIVIGRIFHIVENDLYIDFGGKFHCVCKRPEVDGEKYQKGTRVRLRLLDLELTSRFLGATTDTTILEAEAVLLGLQESKDSKSKEERRENK
Protein: Tropomyosin alpha-3 chain (Gamma-tropomyosin) (Tropomyosin-3) (P21107)
Organism: Mus musculus (Mouse)
Function: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments.
Subcellular location: [Isoform 2]: Cytoplasm, cytoskeleton.
Interaction partners:
- High affinity nerve growth factor receptor
- Troponin I, cardiac muscle
- Actin, alpha cardiac muscle 1
- Troponin I, slow skeletal muscle
- Troponin T, slow skeletal muscle
- Troponin T, fast skeletal muscle
- Nucleoprotein TPR
- Tropomyosin alpha-1 chain
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin light chain 3
Sequence:
MMEAIKKKMQMLKLDKENVLDRAEQAEAEQKQAEERSKQLEDELATMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISDELDHALNDMTSI
Protein: Amidinotransferase (Q581V1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- DUF4201 domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MSTALFVQATFFNTDNKSTDNKLMTTAAVSHNQSSQDNIMVVNLQKELQKRLEEDAGVKTLYITMGGEPRFNRALFENKSMALFVGDSMSIHHFTDDYGRITRRLLILYPMTFSRREEIPKQQILKKVEKAANQPEDNCGIEVVDLVELQKKHVYLEGQAAACYSYNGEFVYMALSGRSSEQVLSIICAPENLNIPNEKRFVFTAVLPHRSKENGRVIGEDVIPYTSLVGWCGKGICAWGLEFLRFPSEKDQEAFYEHLENNYSKVINLDESELRAFCGNAREVAIAHGNGERRVLCISHQALNALRPFKRQMLEDWYGLGNILPFYADVLERRAGRSVGSLVSVPVIHGEVLPLPGELGVIEAAKVDIKDGGC
Protein: Uncharacterized protein (Q382I0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSEGRLESLAKLSKILQEKGEVPSGLWAEAGLKVGSRQKDVEAAIKAEKKSKSAAIKRTEEELERAAQAEEARKLGVKVEELQDKMSAMEKEFDINNKKAREEERRAGRSKKEKQREADYGEYDMDTEHV
Protein: p-hydroxybenzoic acid efflux pump subunit AaeA (pHBA efflux pump protein A) (P46482)
Organism: Escherichia coli (strain K12)
Function: Forms an efflux pump with AaeB.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01544}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01544}.
Interaction partners:
- p-hydroxybenzoic acid efflux pump subunit AaeB
- Protein AaeX
- HTH-type transcriptional activator AaeR
- Macrolide export ATP-binding/permease protein MacB
Sequence:
MKTLIRKFSRTAITVVLVILAFIAIFNAWVYYTESPWTRDARFSADVVAIAPDVSGLITQVNVHDNQLVKKGQILFTIDQPRYQKALEEAQADVAYYQVLAQEKRQEAGRRNRLGVQAMSREEIDQANNVLQTVLHQLAKAQATRDLAKLDLERTVIRAPADGWVTNLNVYTGEFITRGSTAVALVKQNSFYVLAYMEETKLEGVRPGYRAEITPLGSNKVLKGTVDSVAAGVTNASSTRDDKGMATIDSNLEWVRLAQRVPVRIRLDNQQENIWPAGTTATVVVTGKQDRDESQDSFFRKMAHRLREFG
Protein: DNA repair protein RAD51 homolog 2 (R51H2) (RAD51 homolog B) (RAD51-like protein 1) (O35719)
Organism: Mus musculus (Mouse)
Function: Involved in the homologous recombination repair (HRR) pathway of double-stranded DNA breaks arising during DNA replication or induced by DNA-damaging agents. May promote the assembly of presynaptic RAD51 nucleoprotein filaments. Binds single-stranded DNA and double-stranded DNA and has DNA-dependent ATPase activity. Part of the RAD51 paralog protein complex BCDX2 which acts in the BRCA1-BRCA2-dependent HR pathway. Upon DNA damage, BCDX2 acts downstream of BRCA2 recruitment and upstream of RAD51 recruitment. BCDX2 binds predominantly to the intersection of the four duplex arms of the Holliday junction and to junction of replication forks. The BCDX2 complex was originally reported to bind single-stranded DNA, single-stranded gaps in duplex DNA and specifically to nicks in duplex DNA. The BCDX2 subcomplex RAD51B:RAD51C exhibits single-stranded DNA-dependent ATPase activity suggesting an involvement in early stages of the HR pathway.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O15315}.
Interaction partners:
- DNA repair protein RAD51 homolog 3
- DNA repair protein XRCC2
- DNA repair protein RAD51 homolog 4
- Breast cancer type 2 susceptibility protein homolog
- DNA repair protein XRCC3
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- Fanconi anemia group M protein homolog
- DNA repair protein RAD52 homolog
- Structure-specific endonuclease subunit MUS81
- Double-strand break repair protein MRE11
Sequence:
MSSKKLRRVGLSPELCDRLSRYQIVNCQHFLSLSPLELMKVTGLSYRGVHELLHTVSKACAPQMQTAYELKTRRSAHLSPAFLSTTLCALDEALHGGVPCGSLTEITGPPGCGKTQFCIMMSVLATLPTSLGGLEGAVVYIDTESAFTAERLVEIAESRFPQYFNTEEKLLLTSSRVHLCRELTCEGLLQRLESLEEEIISKGVKLVIVDSIASVVRKEFDPKLQGNIKERNKFLGKGASLLKYLAGEFSIPVILTNQITTHLSGALPSQADLVSPADDLSLSEGTSGSSCLVAALGNTWGHCVNTRLILQYLDSERRQILIAKSPLAAFTSFVYTIKGEGLVLQGHERP
Protein: Inclusion membrane protein E (B0B9M4)
Organism: Chlamydia trachomatis serovar L2 (strain ATCC VR-902B / DSM 19102 / 434/Bu)
Function: Inclusion membrane protein probably involved in early modification events of the chlamydial inclusion.
Subcellular location: Secreted {ECO:0000305|PubMed:10447885}. Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole membrane {ECO:0000269|PubMed:10447885, ECO:0000269|PubMed:26416906}; Multi-pass membrane protein {ECO:0000255}. Note=Secreted, probably by a type III secretion system (Probable). Localized in the inclusion membrane (PubMed:10447885, PubMed:26416906). Inclusion membrane staining is punctate (PubMed:10447885). {ECO:0000269|PubMed:10447885, ECO:0000269|PubMed:26416906, ECO:0000305|PubMed:10447885}.
Interaction partners:
Sequence:
MECVKQLCRNHLRLDNLTDPVRSVLTKGTTAEKVQLAACCLGVVCSIICLALGIAAAAVGVSCGGFALGLGIIAILLGIVLFATSALDVLENHGLVGCPFKLPCKSSPANEPAVQFFKGKNGSADQVILVTQ
Protein: Transmembrane glycoprotein NMB (Hematopoietic growth factor inducible neurokinin-1 type) (Q14956)
Organism: Homo sapiens (Human)
Function: Could be a melanogenic enzyme.
Subcellular location: Cell membrane; Single-pass type I membrane protein {ECO:0000269|PubMed:16489096, ECO:0000269|PubMed:16609006}. Melanosome membrane {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}; Single-pass type I membrane protein {ECO:0000305}. Early endosome membrane {ECO:0000269|PubMed:29336782}; Single-pass type I membrane protein {ECO:0000305}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:17081065}.
Interaction partners:
- Epidermal growth factor receptor
- Protein-tyrosine kinase 6
- Thymosin beta-10
- 5,6-dihydroxyindole-2-carboxylic acid oxidase
- Leucine-rich repeat serine/threonine-protein kinase 2
- Annexin A5
- CD44 antigen
- Syndecan-4
- Proheparin-binding EGF-like growth factor
Sequence:
MECLYYFLGFLLLAARLPLDAAKRFHDVLGNERPSAYMREHNQLNGWSSDENDWNEKLYPVWKRGDMRWKNSWKGGRVQAVLTSDSPALVGSNITFAVNLIFPRCQKEDANGNIVYEKNCRNEAGLSADPYVYNWTAWSEDSDGENGTGQSHHNVFPDGKPFPHHPGWRRWNFIYVFHTLGQYFQKLGRCSVRVSVNTANVTLGPQLMEVTVYRRHGRAYVPIAQVKDVYVVTDQIPVFVTMFQKNDRNSSDETFLKDLPIMFDVLIHDPSHFLNYSTINYKWSFGDNTGLFVSTNHTVNHTYVLNGTFSLNLTVKAAAPGPCPPPPPPPRPSKPTPSLATTLKSYDSNTPGPAGDNPLELSRIPDENCQINRYGHFQATITIVEGILEVNIIQMTDVLMPVPWPESSLIDFVVTCQGSIPTEVCTIISDPTCEITQNTVCSPVDVDEMCLLTVRRTFNGSGTYCVNLTLGDDTSLALTSTLISVPDRDPASPLRMANSALISVGCLAIFVTVISLLVYKKHKEYNPIENSPGNVVRSKGLSVFLNRAKAVFFPGNQEKDPLLKNQEFKGVS
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform E (EC 1.-.-.-)) (Q86BQ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MAFIWQLISAAIYLVGLLTIGVFLYDNLKSLVSIIKAVLEPYFQPHLPRTLVDKFGQWAVVTGATDGIGKEYARELARQGINLVLISRTKEKLIAVTNEIESQYKVKTKWIAADFAKGREVYDQIEKELAGIDVGILVNNVGMMYEHPESLDLVSEDLLWNLLTVNMGSVTMLTRKILPQMIGRRKGAIVNLGSSSELQPLPNMTVYAASKKFVTYFSKALELEVAEHNIHVQLVMPNFVVTKMNAYTDRVMQGGLFFPNAYTFARSAVFTLGKTSETNGFWTHGIQYAIMKLAPLPIRTYLGHQLFKRLRIEALEQKQKKLKLT
Protein: Magnetosome protein MmsF (Q2W8R4)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Plays a major role in synthesis of cubooctahedral magnetite crystals by controlling crystal growth and morphology after nucleation. Has a partially redundant function with MamF (By similarity). When overexpressed in E.coli the soluble protein self assembles into shells of about 36 nm. This protein mediates the formation of magnetite nanoparticles from a solution of Fe(2+) and Fe(3+) sulfate; the crystals are larger and lack alternative iron oxide/oxyhydroxide species seen in the protein's absence.
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:22716969, ECO:0000269|PubMed:26884433, ECO:0000269|PubMed:27481925}; Multi-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:22716969}. Note=Tagged protein forms straight lines with a punctate pattern extending along most of the cell associated with its inner curvature, in the correct position to be associated with magnetosomes (PubMed:22716969, PubMed:26884433, PubMed:27481925). During magnetosome formation protein is first dispersed in cell inner membrane, the gradually forms foci which align and form lines as the magnetic response increases (PubMed:26884433). {ECO:0000269|PubMed:22716969, ECO:0000269|PubMed:26884433, ECO:0000269|PubMed:27481925}.
Interaction partners:
- Succinate dehydrogenase hydrophobic membrane anchor subunit
- NAD-dependent aldehyde dehydrogenase
- Fumarate hydratase class II
- Succinate dehydrogenase iron-sulfur subunit
- Fumarate hydratase class I
- Succinate dehydrogenase cytochrome b556 subunit
- Succinate dehydrogenase flavoprotein subunit
- Acetyl-CoA hydrolase
- Succinate--CoA ligase subunit alpha
- NAD-dependent aldehyde dehydrogenase
Sequence:
MTEAILRSTLGARTTVMAALSYLSVLCFVPLLVDRDDEFVYFHAKQGLVIWMWGVLALFALHVPVLGKWIFGFSSMGVLVFSLLGLVSVVFQRAWKLPLISWVAHRI
Protein: Transcription factor MYB26 (Myb-related protein 26) (AtMYB26) (Protein MALE STERILE 35) (Q9SPG3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor that regulates lignified secondary cell wall thickening of the anther endocethium, which is necessary for anther dehiscence. May play a role in specifying early endothecial cell development by regulating a number of genes linked to secondary thickening such as NST1 and NST2. Acts upstream of the lignin biosynthesis pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:17329564}.
Interaction partners:
- NAC domain-containing protein 66
- NAC domain-containing protein 43
- NAC domain-containing protein 12
- NAC domain-containing protein 30
- At5g52380
Sequence:
MGHHSCCNKQKVKRGLWSPEEDEKLINYINSYGHGCWSSVPKHAGTYTHIHGFCLQRCGKSCRLRWINYLRPDLKRGSFSPQEAALIIELHSILGNRWAQIAKHLPGRTDNEVKNFWNSSIKKKLMSHHHHGHHHHHLSSMASLLTNLPYHNGFNPTTVDDESSRFMSNIITNTNPNFITPSHLSLPSPHVMTPLMFPTSREGDFKFLTTNNPNQSHHHDNNHYNNLDILSPTPTINNHHQPSLSSCPHDNNLQWPALPDFPASTISGFQETLQDYDDANKLNVFVTPFNDNAKKLLCGEVLEGKVLSSSSPISQDHGLFLPTTYNFQMTSTSDHQHHHRVDSYINHMIIPSSSSSSPISCGQYVIT