wanglab/gogpt-training-data huggingface dataset:
Protein: NCK-interacting protein with SH3 domain (54 kDa VacA-interacting protein) (VIP54) (90 kDa N-WASP-interacting protein) (90 kDa SH3 protein interacting with Nck) (SH3 adapter protein SPIN90) (WASP-interacting SH3-domain protein) (WISH) (Wiskott-Aldrich syndrome protein-binding protein) (N-WASP-binding protein) (Q9ESJ4)
Organism: Mus musculus (Mouse)
Function: Has an important role in stress fiber formation induced by active diaphanous protein homolog 1 (DRF1) (By similarity). Induces microspike formation, in vivo. In vitro, stimulates N-WASP-induced ARP2/3 complex activation in the absence of CDC42. May play an important role in the maintenance of sarcomere and/or in the assembly of myofibrils into sarcomeres. Implicated in regulation of actin polymerization and cell adhesion.
Subcellular location: Nucleus {ECO:0000250}. Note=Colocalizes with DRF1 at membrane ruffles, and with Nck at Z-disks in mature cardiac myocytes. {ECO:0000250}.
Interaction partners:
- SH2/SH3 adapter protein Nck1
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 5
- Actin-related protein 2/3 complex subunit 2
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 1A
- Actin-related protein 2/3 complex subunit 1B
- Growth factor receptor-bound protein 2
Sequence:
MYRALYAFRSAEPNAMAFAAGETFLVLERSSTHWWLAARARSGETGYVPPAYLHRLQGMEQDVLQAIDRAIEAVHNTAMRDGGKYSLEQRGVLQKLIHHRKETLSRRGTSASSATVMTPSTSDHHLDAAVSRQPNGVCRTGFERQHSLPSSEHLGTDGALYQVPPQPRRAAPTTPPPPVKRRDREALVISGSGGRTAIPSGGSSVSSGSSASSTSMDTLYTGSSPSELGPSCSPTPPPVPRRGAHTTVSQPQPSPSKAPSPEPPTEEVAAETNSTPDDLEAQDALSPETTEEKAAAETVVPRTIGAELMELVRRNTGLSHELCRVAIGVVVGHIQATVPASSPIMEQVLLSLVEGKDLSTALPSGQVCHDQQRLEVIFADLARRKDDAQQRSWALYEDEDVIRCYLEELLHILTDADPEVCKKMCKRSDFESVLALVAYYQMEHRASLRLLLLKCFGAMCSLDAAIISTLVSSVLPVELARDMQTDTQDHQKLCYSALVLAMVFSMGEAVPYAHYEHLGTPFAQFLLSIVEDGLPMDTTEQLPDLCMNLLLALNLHLTAPEQNVIMAALSRHTNVKIFSEKLLLLLNRGDDPVRIFRHEPQPPHSVLKFLQDVFSSSATAAIFYHTDMMALIDITVRQIADLSPGDKLRMEYLSLMHAVVRSTPYLQHRHRLSDLQATLRRILTEEEASPQCQMDRMIVQEMYKEFPDLGEVPS
Protein: Nucleoredoxin-like protein 2 (Rod-derived cone viability factor 2) (RdCVF2) (Q9D531)
Organism: Mus musculus (Mouse)
Function: May be involved in the maintenance of both the function and the viability of sensory neurons, including photoreceptors and olfactory neurons. In the retina, isoform 1 may be required for rod function and isoform 2 for cone viability and function.
Interaction partners:
- Segment polarity protein dishevelled homolog DVL-1
Sequence:
MVDVLGGRRLVTREGTVVEAEVALQNKVVALYFAAGRCSPSRDFTPLLCDFYTELVSEARRPAPFEVVFVSADGSAEEMLDFMRELHGSWLALPFHDPYRHELKKRYEITAIPKLVVIKQNGAVITNKGRKQIRERGLACFQNWVEAADVFQNFSG
Protein: Superoxide dismutase (EC 1.15.1.1) (A0A1D8PQH5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Superoxide dismutase
- Mitochondrial 37S ribosomal protein RSM26
- Superoxide dismutase
- Mitochondrial 37S ribosomal protein MRP1
- Thiosulfate sulfurtransferase
- Peroxisomal catalase
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL29m
- Mitochondrial 37S ribosomal protein MRPS17
- Large ribosomal subunit protein uL13m
Sequence:
MITENEKISLPKIDWALDALEPYISKEINDLHINKHHVAYVNGYNAAIDALEKAVGKRDLKSVVEIQQNIKFHGGGHTNHSLFWKNLAPVSKGGGKHPDTSSALGKQIVAQYGSVSNLIDITNSKLAGIQGSGWAFIVKNKQNGGALDVVTTANQDTISAPHLVPIIAIDAWEHAYYLQYQNVKLDYFKAIWNVINWAEAESRYSA
Protein: Beta carbonic anhydrase 2, chloroplastic (AtbCA2) (AtbetaCA2) (EC 4.2.1.1) (Beta carbonate dehydratase 2) (P42737)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Reversible hydration of carbon dioxide. This isoform ensures the supply of bicarbonate for pep carboxylase.
Subcellular location: [Isoform 1]: Plastid, chloroplast {ECO:0000269|PubMed:12766230}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:0000269|PubMed:17407539}.
Interaction partners:
- Cyanate hydratase
- Tubulin-folding cofactor D
Sequence:
MVPFWTTVSRNGSSDSETTLQSASKATKQYKYPSLRPSHRLSLLFLFPFHLSANGACFRCTCFSHFKLELRRMGNESYEDAIEALKKLLIEKDDLKDVAAAKVKKITAELQAASSSDSKSFDPVERIKEGFVTFKKEKYETNPALYGELAKGQSPKYMVFACSDSRVCPSHVLDFHPGDAFVVRNIANMVPPFDKVKYAGVGAAIEYAVLHLKVENIVVIGHSACGGIKGLMSFPLDGNNSTDFIEDWVKICLPAKSKVLAESESSAFEDQCGRCEREAVNVSLANLLTYPFVREGVVKGTLALKGGYYDFVNGSFELWELQFGISPVHSI
Protein: Ornithine decarboxylase antizyme (ODC-Az) (Protein gutfeeling) (P54361)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ornithine decarboxylase (ODC) antizyme protein that negatively regulates ODC activity and intracellular polyamine biosynthesis and uptake in response to increased intracellular polyamine levels. Binds to ODC monomers, inhibiting the assembly of the functional ODC homodimer, and targets the monomers for ubiquitin-independent proteolytic destruction by the 26S proteasome (By similarity). Required for cellular differentiation in neuronal and myogenic lineages during embryonic development.
Interaction partners:
- Ornithine decarboxylase 2
- Ornithine decarboxylase 1
- Eukaryotic translation initiation factor 5A
Sequence:
MPSNMNNKLDPVFSSGFVRREFNDSGIADGKLRTISTSSCATTMSSESYRISLGVGPLWWSDVPVHHRTDHDRASLLTGYSRKSSVDSAGGSLYEASSRASSLSSSQSDCSDLESQPDIHSLCSDDDCQEVLRQILQHDQPVQITIKLHVTEDQYTNWNTILNPVNNLLYVALPKDLPPAGSKQTFISLLEFAEEKLEVDGIVMVMPKDQPDRARLIEAFLFMGFEPLSRKAPQAPPAAINDNENYYFLYSIEE
Protein: tRNA (guanine(9)-N(1))-methyltransferase (EC 2.1.1.221) (Q9FGI9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- tRNA
- tRNA
- Putative tRNA
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- NOL1/NOP2/sun family protein / antitermination NusB domain-containing protein
- tRNA wybutosine-synthesizing protein 2/3/4
- Ribosomal RNA small subunit methyltransferase, mitochondrial-N
- tRNA
- tRNA-specific adenosine deaminase TAD1
- Putative rRNA 2'-O-methyltransferase fibrillarin 3
Sequence:
MAAATGNDDNGCFDKPESEPAPVNVSPPLSKNAQKKQLKQQRYEAKKAEKKAQEKEHKRKEGERKLKEWEETLANATEEERLKLIESRKSLRKERMEKRSEEKEKKIERLNQAKEIGQKIVVDVDFAHLMSESEISSLVQQIMYCYAVNGRSTSPCHLWLTGVQGKMSTELDKLPGFEKWFIEKESRCYIEAMADQKDNLVYLTADSETVLDDLDPKHIYIIGGLVDRNRFKGITMTKAQEQGIKTAKLPIGEYMKMSSSQVLTVNQVLEILVKFLETRDWKTAFFTVIPQRKRTGLDPVDCSKLEHISEEHQEKDTEANESADKHDLLERKKVCVEVPLESSS
Protein: SKN-1 Dependent Zygotic transcript (Q22385)
Organism: Caenorhabditis elegans
Interaction partners:
- SKN-1 Dependent Zygotic transcript
- G_PROTEIN_RECEP_F1_2 domain-containing protein
- Apyrase apy-1
- Very Early Transcript
- BTB domain-containing protein
- Putative T-box protein 11
Sequence:
MSSITVFSVILILTIFPLVFTSGHLRLEFTSSENKFLRLITDYSNETLQLTMGEKKTSSFHPTNEQDTIRIGLSTLNRDPVFYKFKLENTGQHLRNIFDQDDVVVFIQSVFECDEGFFGSKCLLKKAPSTSTIASKMTSTTTMTTTTTTITTSTESEKQASSKGAGLSMGLEHYNSIIIVVLVIIIITLLILIAVFAVLLFSSRSQNQHIIIAGRKSASKCKKLDFEGFEGKSFERSNDFQYEEPRYTAAPFGSFFSKQSEY
Protein: Pleckstrin homology domain containing, family A member 5 (A0A0N4SWC0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAADLNLEWICSLPRSWTYGITRGGRVFFINEEAKSTTWLHPVTGEAVVTGHRRQSTDLPTGWEEAYTFEGARYYINHNERKVTCKHPVTGQPSQDNCIFVVNDQTVATMTSEDKKERPISMINEASNYNMASDYAVHPMSPVGRTSRASKKVHNFGKRSNSIKRNPNAPVVRRGWLYKQMRRRRVFWEVSCCLVFR
Protein: Lysin (Q9MCC8)
Organism: Lactobacillus phage A2
Interaction partners:
Sequence:
MSYTINKEFALGANEGSSQVANRLYIILHDVGAESGARANAAYFKNNISAEIAYTAFVVGDGGQVYQVGEPGYVQWGAGTVANANSPVQIELGHTSDPETFKKDYAVYIELARDMAARYGIPTSLDAGGAGTPGIKSHLWVTQHIWGDHTDPYGYLARWGITKEKLAADLANGTTTVDASTSAPATQSTRPQATVSGNVNATYGLHLLGGSWLDEVTNFGSGDNGFAGMPNHQHDLLYIRVDHGSVKYRVHTVQSGWLDWVTKGDRNDTVNGCAGIAGEAIDGVQIIFLTPAGEPYQQAYYRSQTTQRAGWLGVVCDDGTSLPQYTGTYAGLFGEPLDRLQIGISSINPF
Protein: Cathepsin K (EC 3.4.22.38) (Ctsk protein) (Q568D6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGRFGGFPLLVLLWCGLAHSLDNLSLDEAWESWKITHKREYNGLNEESIRRTIWEKNMLFIEAHNKEYELGIHTYDLGMNHFGDMTLEEVAEKVMGLQMPMYRDPANTFVPDDRVGKLPKSIDYRKLGYVTSVKNQGSCGSCWAFSSVGALEGQLMKTKGQLVDLSPQNLVDCVTENDGCGGGYMTNAFRYVSNNQGIDSEESYPYVGTDQQCAYNTSGVAASCRGYKEIPQGNERALTAAVANVGPVSVGIDAMQSTFLYYKSGVYYDPNCNKEDVNHAVLAVGYGATPRGKKYWIVKNSWGEEWGKKGYVLMARNRNNACGIANLASFPVM
Protein: Submandibular glandular kallikrein-9 (rGK-9) (EC 3.4.21.35) (KLK-S3) (S3 kallikrein) (Submandibular enzymatic vasoconstrictor) (SEV) (Tissue kallikrein) [Cleaved into: Submandibular glandular kallikrein-9 light chain; Submandibular glandular kallikrein-9 heavy chain] (P07647)
Organism: Rattus norvegicus (Rat)
Function: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. This enzyme has a vasoconstrictor activity. KLK-9 has both a chymotrypsin-like and a trypsin-like properties.
Interaction partners:
- Serine protease inhibitor A3K
- Kininogen-1
- CD9 antigen
Sequence:
MWFLILFLALSLGQIDAAPPGQSRVVGGYNCETNSQPWQVAVIGTTFCGGVLIDPSWVITAAHCYSKNYRVLLGRNNLVKDEPFAQRRLVSQSFQHPDYIPVFMRNHTRQRAYDHNNDLMLLHLSKPADITGGVKVIDLPTEEPKVGSICLASGWGMTNPSEMKLSHDLQCVNIHLLSNEKCIETYKNIETDVTLCAGEMDGGKDTCTGDSGGPLICDGVLQGLTSGGATPCAKPKTPAIYAKLIKFTSWIKKVMKENP
Protein: Exosome complex component rrp45 (Ribosomal RNA-processing protein 45) (O74918)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. ski6 is part of the hexameric ring of RNase PH domain-containing subunits proposed to form a central channel which threads RNA substrates for degradation (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Exosome complex exonuclease dis3
- Exosome complex component rrp4
- Exosome complex component rrp42
- Exosome complex protein C1739.07
- Exosome complex component rrp43
- Exosome complex component rrp40
- Exosome complex component mtr3
- Exosome complex component ski6
- Exosome complex component csl4
- Exosome complex component rrp46
Sequence:
MSRHLETSLNNKEFVLNSLEKGLRLDGRQLSDFRSLEIQFGKEYGQVDVSFGHTRVMARITTEITKPYTDRPFDGIFSITTELTPLAYSAFEAGRVSDQEIVISRLIEKAVRRSNALDTESLCIISGQKCWHVRASVHFINHDGNLVDAACIAVIAALCHFRRPELTVVGEEVTVHPVEERVPVPLSILHMPICVTFSFFNNGELAIVDATLEEEDLCNGSMTITLNKNREVCQIYKAGGIIIDPSKIISCAKTAFDIAVSVCSVIQQALDEDLRKKETQYLGGSAENERS
Protein: Alpha-mannosidase (EC 3.2.1.24) (Alpha-D-mannoside mannohydrolase) (P22855)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Degrades free oligosaccharides in the vacuole.
Subcellular location: Vacuole {ECO:0000269|PubMed:11264288, ECO:0000269|PubMed:2266133}. Note=Localizes to the inner surface of the vacuolar membrane. Under nutrient-rich conditions, the protein is delivered to the vacuole by the cytoplasm to vacuole targeting (Cvt) pathway. Under starvation conditions, the protein is localized through autophagy.
Interaction partners:
- Vacuolar aminopeptidase 1
- Autophagy-related protein 19
- Autophagy-related protein 34
- Aspartyl aminopeptidase 4
- ER degradation-enhancing alpha-mannosidase-like protein 1
- Autophagy-related protein 8
- Autophagy-related protein 11
- Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase
- cAMP-dependent protein kinase type 1
- Cerevisin
Sequence:
MSSEDIIYDPQFKPVQGIYENRLRQFIDTGGDYHDLNLPKFYDKKRISLDHDHVKVWWYQVSFERGSSPVSPDKRPSWKSIIERDKKGELEFREANINQPFGPSWSTTWFKVKISLPEDWVKSNEQLLFQWDCSNEGIVIDPKTLIPVTAFSGGERTEYVLPKTSDGKHFFYIEAGNNGMFGCGAGSTINPPDDNRFFHLRKADIVWPDLDARALYIDFWMLGDAARELPGDSWQKHQARQLGNAVMNLFDPNDRSSVRKCRELLQREYFDSFLESSKVYEQGESQVLTNVYGIGNCHIDTAWLWPFAETRRKIVRSWSSQCTLMDRFPEYKFVASQAQQFKWLLEDHPEFFNKVLIPKIQQSQFFAVGGTWVENDTNIPSGESLARQFFFGQRFFLKHFGLKSKIFWLPDTFGYSSQMPQLCRLSGIDKFLTQKLSWNNINSFPHSTFNWAGIDGSQLLTHMPPGNTYTADSHFGDVLRTAKQNKTPEYYGSGLMLYGKGDGGGGPTEEMLQKMRRIRSMNNRNGNVIPKLQVGITVDEFYDDILKRTNQGHDLPTWSGELYFEFHRGTYTSQAQTKKLMRLSEIKLHDLEWIAAKTSVLYPDSYKYPSKQINELWENVLLCQFHDVLPGSCIEMVYKYEAVPMLHNVVKECTSLIDKTVQFLQSQSKADLVEMRTLTWSKPEKVSEECSLNGSYTSSVTGYDDYIVLANGKLKVIICKKTGVITSITDETLGVEYLDTEHGRNKLGANQFVIYDDKPLGWQAWDTELYSVNQYKYVTKPKKVQVSCNTKEKCAVEVIFQISEKCKIKSVISLNATAVTDAKLSKVDISTTVENWDARNKFLKVEFPVNIRNDFASYETQFGITKRPTHYNTSWDVAKFEVCHHKFADYSEYSKGVSILNDCKYGFSTHGNLMRLSLLRSPKAPDAHADMGTHEIKYAIYPHRGALSSDTVKLAHEFNYCFKYKLPKDIGMNFDDIISISGDENVILSNIKRGEDDSAVKSNYSLNPRDEQSIVVRVYESLGGESFASLNTTLNLKRIEKVDNLEMKVYKSLTATRDESNHAINRIPIKLRPFEIASFRLYF
Protein: DNA/RNA-binding protein Kin17 WH-like domain-containing protein (Q9XWF2)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Proline-rich protein PRCC
- RRM domain-containing protein
- Rap-GAP domain-containing protein
- Splicing factor 3B subunit 1 domain-containing protein
- Splicing factor 3B subunit 3
- Peptidyl-prolyl cis-trans isomerase
- Matrin-type domain-containing protein
- Splicing factor 3A subunit 2
- BZIP domain-containing protein.
- BUD13 homolog
Sequence:
MGKHEKGSSKDLANRTKSKGLQKLKFFCQMCQKQCRDANGFKCHLTSEAHQRQLLLFAENSNSYLRQFSNDFEKNFMQLLRTSYGTKRVRANEVYNAFIKDKGHVHMNSTVWHSLTGFVQYLGSSGKCKIDEGDKGWYIAYIDQEALIRKEEDQRKQQQEKDDEERHMQIMDGMVQRGKELAGDDEHEYEATELIRDTPDQKIQLDLNLGILDRKLDVKSGVASAKISIFDMPKVKKEDPDEPGPSQPSRKSGKKRSRSRSPAAKKFSKKSALDEIKEMEERKKERKNRKDYWMREGIVVKVITKSLGSEYYKAKGVVRKVVDDYTAQVKLDDGTVVKLDQEHVETVIPSLGRQMMIVNGAYRGQEATLESIDEKRFSLRLKIASGPTRGRQIDVPYEDASKLA
Protein: Putative nucleotide-sugar transporter (I1VCA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKIAANGRFFTIGLVASWYSSNIGVLLLNKYLLSNYGFKYPIFLTMCHMTACSLLSYVAIAWMKMVPMQTIRSRVQFLKIAALSLVFCVSVVFGNISLRFLPVSFNQAIGATTPFFTAVFAYLITFKREAWLTYFTLVPVVTGVVIASGSEPSFHLFGFIMCIAATAARALKSVLQGILLSSEGEKLNSMNLLLYMAPIAVVFLLPATLIMEKNVVGITIALARDDFRIVWYLLFNSALAYFVNLTNFLVTKHTSALTLQVLGNAKGAVAVVVSILIFRNPVSVTGMLGYSLTVCGVILYSEAKKRSK
Protein: Amelogenin, X isoform (Leucine-rich amelogenin peptide) (LRAP) (P63277)
Organism: Mus musculus (Mouse)
Function: Plays a role in the biomineralization of teeth. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q99217}.
Interaction partners:
- Ameloblastin
- Enamelin
- Tuftelin
- Matrix metalloproteinase-20
- Kallikrein-4
- Amelotin
- BPI fold-containing family A member 2
- Somatoliberin
- Peripherin-2
- Neuropeptide Y receptor type 2
Sequence:
MGTWILFACLLGAAFAMPLPPHPGSPGYINLSYEKSHSQAINTDRTALVLTPLKWYQSMIRQPYPSYGYEPMGGWLHHQIIPVLSQQHPPSHTLQPHHHLPVVPAQQPVAPQQPMMPVPGHHSMTPTQHHQPNIPPSAQQPFQQPFQPQAIPPQSHQPMQPQSPLHPMQPLAPQPPLPPLFSMQPLSPILPELPLEAWPATDKTKREEVD
Protein: Mitochondrial tRNA methylthiotransferase CDK5RAP1 (EC 2.8.4.3) (CDK5 activator-binding protein C42) (CDK5 regulatory subunit-associated protein 1) (mt-tRNA-2-methylthio-N6-dimethylallyladenosine synthase) (mt-tRNA-N6-(dimethylallyl)adenosine(37) methylthiotransferase) (Q96SZ6)
Organism: Homo sapiens (Human)
Function: Methylthiotransferase that catalyzes the conversion of N6-(dimethylallyl)adenosine (i(6)A) to 2-methylthio-N6-(dimethylallyl)adenosine (ms(2)i(6)A) at position 37 (adjacent to the 3'-end of the anticodon) of four mitochondrial DNA-encoded tRNAs (Ser(UCN), Phe, Tyr and Trp). Essential for efficient and highly accurate protein translation by the ribosome. Specifically inhibits CDK5 activation by CDK5R1. Essential for efficient mitochondrial protein synthesis and respiratory chain; shows pathological consequences in mitochondrial disease.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:22422838}.
Interaction partners:
- Exosome complex component RRP40
- Exosome complex component RRP46
- Cyclin-dependent kinase 5
- tRNA dimethylallyltransferase
- Cyclin-dependent kinase 5 activator 1
- Pre-mRNA-processing factor 40 homolog B
Sequence:
MHPLQCVLQVQRSLGWGPLASVSWLSLRMCRAHSSLSSTMCPSPERQEDGARKDFSSRLAAGPTFQHFLKSASAPQEKLSSEVEDPPPYLMMDELLGRQRKVYLETYGCQMNVNDTEIAWSILQKSGYLRTSNLQEADVILLVTCSIREKAEQTIWNRLHQLKALKTRRPRSRVPLRIGILGCMAERLKEEILNREKMVDILAGPDAYRDLPRLLAVAESGQQAANVLLSLDETYADVMPVQTSASATSAFVSIMRGCDNMCSYCIVPFTRGRERSRPIASILEEVKKLSEQVFLPPRPPKVLGLQGLKEVTLLGQNVNSFRDNSEVQFNSAVPTNLSRGFTTNYKTKQGGLRFAHLLDQVSRVDPEMRIRFTSPHPKDFPDEVLQLIHERDNICKQIHLPAQSGSSRVLEAMRRGYSREAYVELVHHIRESIPGVSLSSDFIAGFCGETEEDHVQTVSLLREVQYNMGFLFAYSMRQKTRAYHRLKDDVPEEVKLRRLEELITIFREEATKANQTSVGCTQLVLVEGLSKRSATDLCGRNDGNLKVIFPDAEMEDVNNPGLRVRAQPGDYVLVKITSASSQTLRGHVLCRTTLRDSSAYC
Protein: Probasin (PB) (O08976)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Prostatic spermine-binding protein
- Homeobox protein Nkx-3.1
- Beta-microseminoprotein
- Androgen receptor
Sequence:
MMRVIILLLTLHVLGVSSVMSLKKKIDGPWQTIYLAASTMEKINEGSPLRTYFRHILCGRRCNQVYLYFFIKKGTKCQLYKVIGRKKQEVYYAQYEGSIAFMLKMVNEKILLFHYFNKNRRNDVTRVAGVLAKGKQLNKEEMTEFMNLVEEMGIEEENVQRIMDTDNCPSKIKP
Protein: Double-strand break repair protein mre-11 (Q23255)
Organism: Caenorhabditis elegans
Function: Involved in DNA double-strand break repair (DSBR). Possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. Also involved in meiotic DSB processing. In response to ionizing radiation, probably required for the association between the brc-1-brd-1 heterodimer and rad-51 and let-70 in order to activate E3-ubiquitin ligase activity of the heterodimer and induce ubiquitination at DNA damage sites.
Subcellular location: Nucleus {ECO:0000269|PubMed:11238374}. Chromosome {ECO:0000250|UniProtKB:P49959}. Note=Localizes to DNA double-strand breaks (DSBs). {ECO:0000250|UniProtKB:P49959}.
Interaction partners:
- DNA repair protein rad-50
- Exonuclease 1
- Serine/threonine-protein kinase ATM
- Flap endonuclease 1
- Ku domain-containing protein
- ATP-dependent DNA helicase II subunit 2
- DNA endonuclease activator Ctp1 C-terminal domain-containing protein
- Serine/threonine-protein kinase ATR
- RecQ-like DNA helicase blm-1
- Breast cancer type 1 susceptibility protein homolog
Sequence:
MCGSDDSFDDFVPDSQEPASSRTRNQDHLDDDEVPCSQRPDAANDTMVEDLDEGDEPAHDESEDIIKILVATDIHCGYGENKANIHMDAVNTFEEVLQIATEQKVDMILLGGDLFHENNPSREVQHRVTQLLRQYCLNGNPIALEFLSDASVNFNQSVFGHVNYYDQNLNVGLPIFTIHGNHDDLSGKGLTALDLLHESGLVNLFGKHSNIQEFIVSPILLRKGETRLALYGIGSQRDDRLVRAFKNNSISFLRPNAGAEDWFNLFVLHQNRPRRAMHRSTGNFLPESLIPQFFDLLIWGHEHECKPDPQYVASSEAVGDGFYILQPGSTVATSLTPEEALQKNAFLIKIKGRKFASKPIPLQTVRPMVCDELLLDKIPPGSRPILKTDRPKHTDGRYIDEIAIEAKINEMITTAKAKRRPRQPELPLIRLKVIYDGDWLNITPANAKRIGLRYENVVANAVDMVFIKKNNKPKEGKLQTENEKNITEMADEMGQVSATNLQTIINDYFINQPLVDQMTVLKPIGIGRALEQYSAIEEGGLATSANRNFDSCLMHQIDVVRKTLKKMPLPPINDPSDLDKFRDLITKDLYDMKKADSERFKNPVADVEMEEDEDDPQYYMPPQSTSRTNYASGSEDEVANSDEEMGSSISRHSKQPTTRGRGRGARGAGASRETTRGRSNKVVSTRQIDSDGFEIINDSPSPPPASRSTRGKARGKSAPSKKRDLSFF
Protein: Serine peptidase inhibitor, Kunitz type, 2 (Q6P796)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAQLCEPRRGRALLALLASLLLSGAQAASRDLDVHENTIDGLARSSDGASALSVPRKQDSADLAGEIFNYEEYCVPKAVTGPCRAAFPRWYYDVEKNSCSSFIYGGCRGNKNSYLSQEACMQHCSGKQMYPFLTPGTKAVILVGLFIMVLILLLGSSMVFLIRMVRRKQERALRTVWSTADDKEQLVKNTCVL
Protein: Zinc finger protein 473 (A0A8I6A164)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MERKEEELKRSHWNQAAMAEEFVTLKDVAMDFTLEDWEDLESELGQRDLFWDATLNNYQDLFSFTHPPQPSLIFQPDVREELEATSDGEWEEGPCTLHWTSN
Protein: Receptor for retinol uptake STRA6 (Retinol-binding protein receptor STRA6) (Stimulated by retinoic acid gene 6 protein homolog) (Q9BX79)
Organism: Homo sapiens (Human)
Function: Functions as retinol transporter. Accepts all-trans retinol from the extracellular retinol-binding protein RBP4, facilitates retinol transport across the cell membrane, and then transfers retinol to the cytoplasmic retinol-binding protein RBP1. Retinol uptake is enhanced by LRAT, an enzyme that converts retinol to all-trans retinyl esters, the storage forms of vitamin A. Contributes to the activation of a signaling cascade that depends on retinol transport and LRAT-dependent generation of retinol metabolites that then trigger activation of JAK2 and its target STAT5, and ultimately increase the expression of SOCS3 and inhibit cellular responses to insulin. Important for the homeostasis of vitamin A and its derivatives, such as retinoic acid. STRA6-mediated transport is particularly important in the eye, and under conditions of dietary vitamin A deficiency (Probable). Does not transport retinoic acid.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18316031, ECO:0000269|PubMed:21901792, ECO:0000269|PubMed:9452451}; Multi-pass membrane protein {ECO:0000305}. Note=In the retinal pigment epithelium localizes to the basolateral membrane. {ECO:0000250|UniProtKB:Q0V8E7}.
Interaction partners:
- Retinol-binding protein 4
- Retinol-binding protein 1
- Lecithin retinol acyltransferase
- Transthyretin
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Retinoic acid receptor alpha
- Calmodulin-like protein 6
- Calmodulin-like protein 4
- Cytochrome P450 26A1
Sequence:
MSSQPAGNQTSPGATEDYSYGSWYIDEPQGGEELQPEGEVPSCHTSIPPGLYHACLASLSILVLLLLAMLVRRRQLWPDCVRGRPGLPSPVDFLAGDRPRAVPAAVFMVLLSSLCLLLPDEDALPFLTLASAPSQDGKTEAPRGAWKILGLFYYAALYYPLAACATAGHTAAHLLGSTLSWAHLGVQVWQRAECPQVPKIYKYYSLLASLPLLLGLGFLSLWYPVQLVRSFSRRTGAGSKGLQSSYSEEYLRNLLCRKKLGSSYHTSKHGFLSWARVCLRHCIYTPQPGFHLPLKLVLSATLTGTAIYQVALLLLVGVVPTIQKVRAGVTTDVSYLLAGFGIVLSEDKQEVVELVKHHLWALEVCYISALVLSCLLTFLVLMRSLVTHRTNLRALHRGAALDLSPLHRSPHPSRQAIFCWMSFSAYQTAFICLGLLVQQIIFFLGTTALAFLVLMPVLHGRNLLLFRSLESSWPFWLTLALAVILQNMAAHWVFLETHDGHPQLTNRRVLYAATFLLFPLNVLVGAMVATWRVLLSALYNAIHLGQMDLSLLPPRAATLDPGYYTYRNFLKIEVSQSHPAMTAFCSLLLQAQSLLPRTMAAPQDSLRPGEEDEGMQLLQTKDSMAKGARPGASRGRARWGLAYTLLHNPTLQVFRKTALLGANGAQP
Protein: Alpha-1-antitrypsin 1-3 (Alpha-1 protease inhibitor 3) (Alpha-1 protease inhibitor 6) (Alpha-1-antitrypsin 1-6) (Serine protease inhibitor 1-3) (Serine protease inhibitor 1-6) (Serine protease inhibitor A1c) (Serpin A1c) (Q00896)
Organism: Mus musculus (Mouse)
Function: Inhibitor of serine proteases. Can inhibit trypsin and chymotrypsin; relatively ineffective against elastase.
Subcellular location: Secreted {ECO:0000269|PubMed:11961105, ECO:0000269|PubMed:8619829}.
Interaction partners:
- Albumin
- Neutrophil elastase
- Alpha-1-antitrypsin 1-2
- Vitamin K-dependent protein C
- Alpha-1-antitrypsin 1-1
- Alpha-1-antitrypsin 1-4
- Alpha-2-HS-glycoprotein
- Haptoglobin
- Apolipoprotein A-I
- RAC-alpha serine/threonine-protein kinase
Sequence:
MTPSISWGLLLLAGLCCLVPSFLAEDVQETDTSQKDQSPASHEIATNLGDFAISLYRELVHQSNTSNIFFSPVSIATAFAMLSLGSKGDTHTQILEGLQFNLTQTSEADIHKSFQHLLQTLNRPDSELQLSTGNGLFVNNDLKLVEKFLEEAKNHYQAEVFSVNFAESEEAKKVINDFVEKGTQGKIVEAVKKLDQDTVFALANYILFKGKWKKPFDPENTEEAEFHVDESTTVKVPMMTLSGMLDVHHCSTLSSWVLLMDYAGNATAVFLLPDDGKMQHLEQTLSKELISKFLLNRRRRLAQIHFPRLSISGEYNLKTLMSPLGITRIFNNGADLSGITEENAPLKLSQAVHKAVLTIDETGTEAAAVTVLLAVPYSMPPILRFDHPFLFIIFEEHTQSPLFVGKVVDPTH
Protein: Glucanase (EC 3.2.1.-) (Q8VV73)
Organism: Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum)
Interaction partners:
Sequence:
MRKNLFAKRAVAFLLGIVITAAGIVSFNTVSTSAAGEYNYAKALQYSMFFYDANMCGTGVDENSLLSWRGDCHVYDARLPLDSQNTNMSDGFISSNRSVLDPDGDGKVDVSGGFHDAGDHVKFGLPEAYAASTVGWGYYEFKDQFRATGQAVHAEVILRYFNDYFMRCTFRDASGNVVAFCHQVGDGDIDHAFWGAPENDTMFRRGWFITKEKPGTDIISATAASLAINYMNFKDTDPQYAAKSLDYAKALFDFAEKNPKGVVQGEDGPKGYYGSSKWQDDYCWAAAWLYLATQNEHYLDEAFKYYDYYAPPGWIHCWNDVWSGTACILAEINDLYDKDSQNFEDRYKRASNKNQWEQIDFWKPIQDLLDKWSGGGITVTPGGYVFLNQWGSARYNTAAQLIALVYDKHHGDTPSKYANWARSQMDYLLGKNPLNRCYVVGYSSNSVKYPHHRAASGLKDANDSSPHKYVLYGALVGGPDASDQHVDRTNDYIYNEVAIDYNAAFVGACAGLYRFFGDSSMQIDPSMPSHNVPVPPTPTPPDTQIVYGDLNGDQKVTSTDYTMLKRYLMKSIDRFNTSEQAADLNRDGKINSTDLTILKRYLLYSIPSLPI