wanglab/gogpt-training-data huggingface dataset:
Protein: Proteasome subunit beta type-2 (Macropain subunit C7-I) (Multicatalytic endopeptidase complex subunit C7-I) (Proteasome component C7-I) (Proteasome subunit beta-4) (beta-4) (P40307)
Organism: Rattus norvegicus (Rat)
Function: Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P49721}. Nucleus {ECO:0000250|UniProtKB:P49721}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000250|UniProtKB:P49721}.
Interaction partners:
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-2
- Proteasome subunit beta type-5
- 26S proteasome non-ATPase regulatory subunit 14
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-7
- Proteasome subunit alpha type-1
- Proteasome subunit alpha type-3
- 26S proteasome regulatory subunit 6B
Sequence:
MEYLIGIQGPDYVLVASDRVAASNIVQMKDDHDKMFKMSEKILLLCVGEAGDTVQFAEYIQKNVQLYKMRNGYELSPTAAANFTRRNLADCLRSRTPYHVNLLLAGYDEHEGPALYYMDYLAALAKAPFAAHGYGAFLTLSILDRYYTPTISRERAVELLRKCLEELQKRFILNLPTFSVRVIDKDGIHNLENITFTKRSS
Protein: Dermcidin (EC 3.4.-.-) (Preproteolysin) [Cleaved into: Survival-promoting peptide; DCD-1] (P81605)
Organism: Homo sapiens (Human)
Function: Found in sweat, has an antimicrobial activity during early bacterial colonization. The secreted peptide assembles into homohexameric complexes that can associate with and also insert into pathogen membranes. Once inserted in bacteria membranes forms anion channels probably altering the transmembrane potential essential for bacterial survival. Highly effective against E.coli, E.faecalis, S.aureus and C.albicans. Optimal pH and salt concentration resemble the conditions in sweat. Also exhibits proteolytic activity, cleaving on the C-terminal side of Arg and, to a lesser extent, Lys residues.
Subcellular location: Secreted {ECO:0000269|PubMed:11694882, ECO:0000269|PubMed:15340161, ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:25946035, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717, ECO:0000269|PubMed:9736629}.; SUBCELLULAR LOCATION: [Survival-promoting peptide]: Secreted {ECO:0000269|PubMed:9736629}.; SUBCELLULAR LOCATION: [DCD-1]: Secreted {ECO:0000305|PubMed:23426625}. Membrane {ECO:0000269|PubMed:23426625}; Peripheral membrane protein {ECO:0000269|PubMed:23426625}. Membrane {ECO:0000269|PubMed:23426625}; Single-pass membrane protein {ECO:0000269|PubMed:23426625}. Note=The secreted peptide assembles into homohexameric complexes that can probably associate with pathogen membranes and also insert into these membranes where they behave as channels. {ECO:0000269|PubMed:23426625}.
Interaction partners:
Sequence:
MRFMTLLFLTALAGALVCAYDPEAASAPGSGNPCHEASAAQKENAGEDPGLARQAPKPRKQRSSLLEKGLDGAKKAVGGLGKLGKDAVEDLESVGKGAVHDVKDVLDSVL
Protein: RNA exonuclease 4 (Q9ZU79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Large ribosomal subunit protein uL30z
- Mannose-P-dolichol utilization defect 1 protein homolog 2
- Histidine-tRNA ligase
- Uncharacterized protein At2g34460
- Transcription regulator
- Reticulon-like protein B8
- Protein BASIC PENTACYSTEINE4
- Cold shock domain-containing protein 4
- Protein kinase superfamily protein
- Proliferating cellular nuclear antigen 1
Sequence:
MDSQLNPSKRRKISVRHRCVACYKMFNRREHLVEHMKISYHSLHQPRCGVCLKHCKSFESVREHLNVPDHLSKGNCKAIFTKRGCTLCLQIFEEAFALAEHKNKCHLSPPRPLGTSTQRNPSSSLAGSRLKAMALDCEMVGGGADGTIDQCASVCLVDDDENVIFSTHVQPLLPVTDYRHEITGLTKEDLKDGMPLEHVRERVFSFLCGGQNDGAGRLLLVGHDLRHDMSCLKLEYPSHLLRDTAKYVPLMKTNLVSQSLKYLTKSYLGYKIQCGKHEVYEDCVSAMRLYKRMRDQEHVCSGKAEGNGLNSRKQSDLEKMNAEELYQKSTSEYRCWCLDRLSNP
Protein: DNA cross-link repair 1 protein (Q86KS1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May be required for DNA interstrand cross-link repair.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- X-ray repair cross-complementing protein 5
- ATP-dependent DNA helicase ku70
- Poly
- Symplekin
- BRCT domain-containing protein
- PBZ-type domain-containing protein
- DNA-dependent protein kinase catalytic subunit
- CPSF domain-containing protein
- Poly [ADP-ribose] polymerase
- DNA ligase 3
Sequence:
MSDDEDDINLYITRSKNNENKKTNKNRLIDNNIQKTKTTTAVLTTRTTTTTTTTTASTQLKWDYGDEDDDDYSAPKDIDEEQSSKQFNYQNNQIVVKQDHDDYSAPKDMDEEQSSRQFNYQNDQTLVKQDDDHDDYNEPKDIDSQSLIDEDCDFEFDNSDFFFDDGTTNNNDNNNKNNKNNNNNNNNNNNNNNYNNNNNKNYKRKYYQSYNNSNNINNNNNNNNDKFEKRLSDLKKTGKEEAKKRGYQVRKTPTKEKKIPPSFKVIDGTNFLVDGFQYKSEDFTHYFLTHFHSDHYVGITKTWSFGNIYCTEETGKLVSHKLGVDQRYIVKCEWNKLIEIQGVKVAFLDSNHCPGSALILFIIPLRNKDGEIIGEESILHTGDFRYNQSMNNYPLLKGRTISKLYLDNTYCDPQYVFPPQPEIIKQVASIVRKENDGETLFLFGTYVIGKERILLEIAKQEGKPVHVSNEKYAILCCLSTCLDINKFTTNELITPFRAVTMSMLSYHNMLSLLDSSNNKYKRVIGFRPTGWTQAKKSITYLNRGPTTFYSVAYSEHSSFNELRDCIDHFRPTQIIPTVDCDSPIKVKNILAHFSDLYEKKKQLTIASFFSAQPVTNFFQSFFKSKSEPIIDEDNKKLIPITTTTTTNINTLTATDTTTTKIKTSNTLIKDEFTDDLIWDCSDDLISDRKLLTQSDNSSALCKIEKEENFNDLSENNNNSNNNNNNNNNNNNNNNNNNNNNNNNNKLIIENDIKEEIIDFDDPVFISQQKWIEKQIYNNNNNSNNNNFTTPTKTNGNLSNNAKLNLTPTQTQTQTPTQNNKKQKTTNVSPTSYNSNNSSQQSGLKRSKSDPNVKKNQLQTSQPPSQSLITSFFQKCASPTSLFSATPPTPSITTTSNQSTKNKNSTTTTSTSTSNNKPFKN
Protein: Uncharacterized protein C16A10.01 (P87293)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cell tip {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MGVQLKLDPNSKNWLRQPDQQPIQDSICTLPGPGSLLKKKIRKTEFRIDNGLLGNTSPIINVESKIPFHRRANSTPEESRKRVSFSLTSNDGAKSDRSSQKSSNSRKSIRSQSRSRSSSVGSDSQASIQSGTNSEVVSDDEEDGNFASIPELHEDNEYHSNLATSSNPFSDGSSSKSASLTASSAAASPTVSFSPASTSENLTPTSSKSLASNTSLVQSFNSASRSSSISGNQYTYNLLGKSTDESPKITISAGTSMSHFPSASSKLIQMRRHAHMNSEKCDPELLSHNEYFPMMKRGFISRFLCLFVSRDANVYIGPLESSHAKPYRPFGSFVSRFTNRVASDLESQIPDALEAVLTQNNDYDFNSFLHNMGYSRCYVDENYHITIHVSSYERRVEFMLAVCEAMMLYGSPSHKIQQSLRIASRILQLPATFLYLPDCMFVYFKKLEQYSPDVFVVRVTSQTDLNRMVLVNEIFRRVMRDKLSAEDGTEVLRNITSFRPLYRDWLVAFMHGVASASILPVVYGGGWRDMLIGFVLGLLLGIFRVYINPRFFLFDSLFEVIISIILSFLGRAFGSISRYDKPVFCFAALVEGAITLILPGYVVFCGVLELQSKNIVAGGVRMLYAVIFSLFLSFGITIGSALYGWMDKDATDADTCMSIIAVSPYWYILLIPIFTLSLLIVTQSHPRQWPIQMFVACCGYVVYYFSSLHFGASQISSAIGSFAVGCLGNMYSHFIKSSSFAVVLPAIFVLVPSGFAAQGGVSAGLDTASQITSKNTTTNTTTVTTENSQNSSLEFGFTMVEIAIGIAIGFLASSLTVYPFFGYRRKNMML
Protein: Golgi associated, gamma adaptin ear containing, ARF binding protein 3 (J3KSS7)
Organism: Homo sapiens (Human)
Subcellular location: Early endosome membrane {ECO:0000256|ARBA:ARBA00004220}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004220}. Golgi apparatus, trans-Golgi network membrane {ECO:0000256|ARBA:ARBA00004150}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004150}.
Interaction partners:
Sequence:
MKNCGRRFHNEVGKFRFLNELIKVVSPKYLGDRVSEKVKTKVIELLYSWTMALPEEAKIKDAYHMLKRQGIVQSDPPIPVDRTLIPSPPPRPKNPVFDDEEKSKLLAKLLKSKNPDDLQEANKLIKSMVKEDEARIQKVTKRLHTLEEVNNNVRLLSEMLLHYSQEDSSDGDRELMKELFDQCENKRRTLFKLASETEDNDNSLGDILQASDNLSRVINSYKTIIEGQVINGEVATLTLPDSEGNSQCSNQGTLIDLAELDTTNSLSSVLAPAPTPPSSGIPILPPPPQASGPPRSRSSSQAEATLGPSSTSNALSWLDEELLCLGLADPAPNVPPKESAGNSQWHLLQREQSDLDFFSPRPGTAACGASDAPLLQPSAPSSSSSQAPLPPPFPAPVVPASVPAPSAGSSLFSTGVAPALAPKVEPAVPGHHGLALGNSALHHLDALDQLLEEAKVTSGLVKPTTSPLIPTTTPARPLLPFSTGPGSPLFQPLSFQSQGSPPKGPELSLASIHVPLESIKPSSALPVTAYDKNGFRILFHFAKECPPGRPDVLVVVVSMLNTAPLPVKSIVLQAAVPKSMKVKLQPPSGTELSPFSPIQPPAAITQVMLLANPLKWQAVSYGHLGRTWNLAS
Protein: Uncharacterized protein (O53245)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
Sequence:
MDVIWSATIATTVATGMRKPRMHGMPPITSGSMVTRVTRMSIRLAGDSTLGRFSTSRLGLSSAKSKPEGDFGTACGAVSGGDAGVVALAEGVDDGQSKPGAAGGARGVGGFRESRADCGEQFGVASWTPQGEFEFGGQEAKGVRSSWPASLTN
Protein: Putative uncharacterized membrane protein C622.02 (O94592)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MAANISKLEAIIDNTPNSSPDPEVSHKLWVSSLNKFQYTLPLLISNFAGLGIAFIYCLIAFIREMSHPSSRKDTMEHGLPIILCSTLMLVGNILYYFLSKHPLKVTVPEDLVQIPMQQMSSPAQEAP
Protein: Cyclin dependent kinase 16 (E5RJM2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDRMKKIKRQLSMTLRGGRGIDKTNGAPEQIGLDESGGGGGSDPGEAPTRAAPGELRSARGPLSSAPEIVHEDLKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDN
Protein: Phospholipid-transporting ATPase IK (EC 7.6.2.1) (ATPase, class I, type 8B, member 3) (Sperm aminophospholipid transporter) (SAPLT) (Q6UQ17)
Organism: Mus musculus (Mouse)
Function: P4-ATPase flippase which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids from the outer to the inner leaflet of various membranes and ensures the maintenance of asymmetric distribution of phospholipids. Phospholipid translocation seems also to be implicated in vesicle formation and in uptake of lipid signaling molecules. May be responsible for the maintenance of asymmetric distribution of phosphatidylserine (PS) in spermatozoa membranes. Involved in acrosome reactions and binding of spermatozoa to zona pellucida.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, acrosome membrane {ECO:0000269|PubMed:14975727, ECO:0000269|PubMed:19017724}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O60423}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cell cycle control protein 50C
- Cell cycle control protein 50A
- Cell cycle control protein 50B
Sequence:
MDGVHLGENLEDKDTEFTWEVKANDRTYHKQFKKKGFLCWRQKKYKSNAIHTAKYNIFSFLPLNLYEQFHRMSNLYFLFIIILQGIPEISTLPWFTLFAPLVCLFVIRATRDLVDDIGRHRSDKIINNRPCQILRGKSFLWKKWKNLCVGDVVCLSKDSIVPADLLLLASTEPSSLCYVETADIDGETNLKFRQALTVTHHELTSPKKMASFQGTVTCEEPNSRMHHFVGSLEWNSRKYPLDIGNLLLRGCKIRNTDTCYGLVIYAGLDTKIMKNCGKIHLKRTKLDLMMNKLVALIFLSLVIASLLLTVGFTFMVKQFKAKHYYMSPTHGRSDAMESFFIFWGFLILLSVMVPMAMFIIAEFIYLGNSIFINWDLNMYYEPLDMPAKARSTSLNDQLGQVQYIFSDKTGTLTQNIMTFKKCCINGCIYDSDDEHGTLRKRNPYAWNPFADGKLQFYNKELESLVQGRQDRAVQEFWRLLAICHTVMVQEKDNQLLYQAASPDEEALVTAARNFGYVFLSRTQDTITLVELGEERVYQVLAMMDFNSVRKRMSVLVRNPEGSICLYTKGADTVILERLRSKGVMEATTEEVLAAFAEQTLRTLCLAYKDVEEDAYKEWEPEHQEAALLLQNRAQALHQVYNKMEQNLQLLGATAIEDKLQDGVPETIKCLKKGNIKIWVLTGDKPETAVNIGFACQLLSENMIILEDKDINQVLERYWEDNVHQKAFKMMTHHNMALVINGEFLDQLLLSLRKEPRALVQNAVVDEVAQEPVVSALDFLQKRRISQMWRNAGPSLGTSHSADSKIRESPEVQRERAFVDLASKCQAVICCRVTPKQKALVVALVKKYQQVVTLAIGDGANDVNMIKTADIGVGLAGQEGMQAVQNSDYVLAQFCYLQRLLLVHGRWSYMRVCKFLRYFFYKTVASMMAQIWFSLVNGFSAQPLYEGWFLALFNLLYSTLPVLYIGLFEQDVTAEKSLKMPELYMAGQKGELFNYSIFMQAITHGTITSMINFFVTVMVSSDMSKAGSSHDYQSLGVLVAISSLLSVTLEVMLVVKYWTLLFVGAVVLSLSSYVLMTSLTQSLWMYRISPKTFPFLFADYNVLFEPCSLLLIVLNVALNVLPMLALRTIHRTVLKQRPKGEEEAPSEEVAVEPAMRHLRRGIPARRSSYAFSHREGYANLITQGTILRRQTHVDDSDGGTVCESLNPPEEDIPLQNKDSVFNPRKISILAKKRRHFFGKGSQEEVHPNTSSQTMEKQPTIHRDSETQKLPTTTSATSGKLLPSASEDEAFYSVASQYTLASQPKHTDVHSSFWKSPLWRDSASSSPSQLEVPRKQS
Protein: Transcription factor HES-7.1-A (HES-related protein 1-A) (XHR1-A) (HES-related protein 1-A') (XHR1-A') (Hairy and enhancer of split 7.1-A) (Q8UW74)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional repressor. Represses transcription from both N box- and E box-containing promoters (By similarity). Demarcates the prospective midbrain-hindbrain boundary (MHB) region in the neuroectoderm in early gastrulae embryos by repressing transcription of a number of target genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8BKT2, ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MKGTSEVKPMETHRKLLKPLVEKRRRERINNSLEKLRIFLFQTLKSEKLKNPKVEKAEILECTVQFLQSRKLLPLDREAVDKEYQSGFQHCLETTLHFMNSKPDMNGVTKELLSHQMSSCKSPSDAWSPNCAPLTKHVPSLSYQDSAPHLVSNSISISPTKTLVDSHFTYQSFKTWRPWV
Protein: Ceramide kinase-like isoform 3 (G0XYF1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFRGRRRSRVGALEEAPPENPKAAAEPERVLLRGIFEIRRESCDVALGERALRWRRIQPELPAGGTRHDLLSKEESLELEDIFSVKLKRRCWAKHPGRDTLLGITLFICLKEQRNKLKDSTLDLINFSEDHCDIWFRQFKKILDGSTNALAHSLFGTPHVVTATMHIILGHIRSVDVCTFSSAGKLLCFGFSAMFGFGGRTLALAEKYRWMSPSQRRDFAIIKALAKLKPEDCKISFLLAGCSQNKQERKSQRSAESDCGGHWQTIQGQFLNISIMAMPCPCSMAPRGFTPDTRLHNGSMALRVVRNTTRSEFVKHLKRHSSVKNQFNFPFVETYIIEEVKIHPKSNSNGYSPQEEGGNHTTASEHGFPWNVDGDLMEAASEVHIRLHPRLIRLYGGSLEEMNDCKVACDCI
Protein: AMP deaminase (AMPD1) (EC 3.5.4.6) (Q54DD0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the conversion of adenosine monophosphate (AMP) to inosine monophosphate (IMP) and ammonia (NH4(+)). Participates in the regulation of the adenylated nucleotide pool and the interconversion to guanylated nucleotides during early morphodifferentiation.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:1916064}.
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- Hypoxanthine-guanine phosphoribosyltransferase
- Adenosine kinase
- Adenylosuccinate synthetase
- Probable adenine phosphoribosyltransferase
- Adenylosuccinate lyase
- Inosine triphosphate pyrophosphatase
- Bifunctional purine biosynthesis protein purH
- Cytosolic purine 5'-nucleotidase
- Adenylate kinase
Sequence:
MSTPLRGSSPQVSFYESELDQEGGSDASHFTYRNYMEDDKINSFTFNMARKDQTQLFQRIILTNESESEIEEYAEVAEQLLDAINLREKYVFHPKIWKADAPVGEKPPYSPFESDESTNCATEHMFKEVNGVYFVYSNETDMKSNKALFSVPHTLASYYKDINNLMMLSSYGPAKTFTFKRLQLLESKFNMHTLLNDSLELFQQKTAPHRDFYNVRKVDTHVHHSSSMNQKHLLKFIKRKLKENPNEIVIFRDDKYLTLAEVFKSLNLDVDELSVDTLDVHADNNTFHRFDKFNLKYNPCGQSRLREIFLKTDNLIKGKYLAEISKEVFTDLESSKYQCAEYRLSIYGRKMSEWDTLASWIVDNDLFSTKVRWLIQVPRLYDVYRETSTTTFQDFLNNVFHPLFEVTKDPSSHPKLHLFLQQVVGIDCVDDESKFEKKFTEKFPVPGEWSSEHNPPYTYYLYYLYANLYTLNQFREEKGLNILTLRPHSGEAGEVDHMGAAFYLAHGINHGINLRKTPVLQYLYYLTQIGIAMSPLSNNSLFLTYNRNPFPAFFARGLNVSISTDDPLQFHYTKEPLMEEYSIATQVWRLSVCDICEIARNSVLQSGFEHNVKSHWLGPDYANSGGNDIKKTNISDIRVCFRNETLIEELHLILKSLQTLPNFKNLNINFLLDKLPSEITTGNDYKLKKAQLKLNGANKLRNSSVGSTPNNGTPSSSGTPSLSSPGAIVHLMKTKPYIPPPLSLNIKQENNNNNNNNNNNNNNNNNNNTNTNTNSNSTTTNQDDNSKSDK
Protein: Myosuppressin receptor 2, isoform C (M9PDT9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- RYamide receptor
Sequence:
MVTNMSQPHYCGTGIDDFHTNYKYFHGYFSLIVCILGTIANTLNIIVLTRREMRSPTNAILTGLAVADLAVMLEYIPYTVHDYILSVRLPREEQLSYSWACFIKFHSVFPQVLHTISIWLTVTLAVWRYIAVSYPQRNRIWCGMRTTLITIATAYVVCVLVVSPWLYLVTAIAKFLETLDANGKTIASVPLSQYILDYNRQDEVTMQVMSSTTPDVSWAIPSDSANGTAVSLLSLTTVIPLTTLSTGVTTSSSLGERNVTVYKLYHSALALRDRQFRNATFLIYSVLIKLIPCFALTILSVRLIGALLEAKRRRKILACHAANDMQPIVNGKVVIPTQPKSCKLLEKEKQTDRTTRMLLAVLLLFLVTEFPQGIMGLLNVLLGDAFFLQCYLKLSDLMDILALINSSINFILYCSMSRQFRSTFALLFRPRWLDKWLPLSQHDGEGRVGGSGGLGGYGGYGRQRLLHTDAVSKSMAIDLGLTTQVTNVXQESSGRAAMSAAAGGAAASVALALAATDVDGCPPATDAAVSTNDISLVEKLHLQPSPRGTAISSGQHRRRRSGSGTKCIWPTTDWLRKLRNQKARETEQSSEQDIELGKSSINRRSSVLLMVLLSSSDEVKAKAVLVSEQPPSPADEDVEDAIDALWL
Protein: PCNA-interacting partner (PARP-1 binding protein) (PARP1-binding protein) (B4DZ31)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAVFNQKSVSDMIKEFRKNWRALCNSERTTLCGADSMLLALQLSMAENNKQHSGEFTVSLSDVLLTWKYLLHEKLNLPVENMDVTDHYEDVRKIYDDFLKNSNMLDLIDVYQKCRALTSNCENYNTVSPGSTIQPPSERGSLLLSRPDLLAPGEDPPVSASLTLERQKGESLLAWSWSLNFRLPGIPITVQKKRRDLKKLAAVMRQSQLLDFLSGKQYAVGDETDLSIPTSPTSKYNRDNEKVQLLARKIIFSYLNLLVNSKNDLAVAYILNIPDRGLGREAFTDLKHAAREKQMSIFLVATSFIRTIELGGKGYAPPPSDPLRTHVKGLSNFINFIDKLDEILGEIPNPSIAGGQILSVIKMQLIKGQNSRDPFCKAIEEVAQDLDLRIKNIINSQEGVVALSTTDISPARPKSHAINHGTAYCGRDTVKALLVLLDEEAANAPTKNKAELLYDEENTIHHHGTSILTLFRSPTQVNNSIKPLRERICVSMQEKKIKMKQTLIRSQFACTYKDDYMISKDNWNNVNLASKPLCVLYMENDLSEGVNPSVGRSTIGTSFGNVHLDRSKNEKVSRKSTSQTGNKSSKRKQVDLDGENILCDNRNEPPQHKNAKIPKKSNDSQNRLYGKLAKVAKSNKCTAKDKLISGQAKLTQFFRL
Protein: Lymphocyte antigen 6C2 (Ly-6C2) (P0CW03)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Integrin alpha-M
- Receptor-type tyrosine-protein phosphatase C
- Adhesion G protein-coupled receptor E1
- Integrin alpha-X
- Low affinity immunoglobulin gamma Fc region receptor III
- C-C chemokine receptor type 2
- T-cell surface glycoprotein CD4
- Killer cell lectin-like receptor subfamily B member 1C
- B-lymphocyte antigen CD19
- Sialic acid-binding Ig-like lectin 5
Sequence:
MDSTHATKSCLLILLVALLCAGRAQGLQCYECYGVPIETSCPAVTCRASDGFCIAQNIELIEDSQRRKLKTRQCLSFCPAGVPIKDPNIRERTSCCSEDLCNAAVPTAGSTWTMAGVLLFSLSSVILQTLL
Protein: 2-hydroxyhexa-2,4-dienoate hydratase (EC 4.2.1.132) (Q83VZ5)
Organism: Comamonas testosteroni (Pseudomonas testosteroni)
Function: Involved in the catatabolism of testosterone. Catalyzes the hydration of 2-hydroxyhexa-2,4-dienoic acid to 4-hydroxy-2-oxohexanoic acid.
Interaction partners:
Sequence:
MSDKQFIETQGQRLYEALRSARTLAPLTDNHPEMTVEDAYHISLHMLRLREASGERVIGKKIGVTSKPVQDMLNVHQPDFGFLTDSMEYEDGAAVSLKAAGLIQPRAEGEIAFMLKKDLQGPGVTREDVLAATEWVAPCFEIVDSRINDWKIKIQDTVADNASCGVFVIGKQHTDPASLDLAAAAMQMSKNGQPAGSGLGSAVQGHPAEAVAWLANTLGAFGIPFKAGEVILSGSLAPLVPAAAGDRFDMVIEGMGTCSIQFTE
Protein: Immunoglobulin kappa variable 4-1 (Ig kappa chain V-IV region B17) (Ig kappa chain V-IV region JI) (Ig kappa chain V-IV region Len) (Ig kappa chain V-IV region STH) (P06312)
Organism: Homo sapiens (Human)
Function: V segment of the variable domain of immunoglobulins light chain that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular location: Secreted {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}. Cell membrane {ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
Interaction partners:
Sequence:
MVLQTQVFISLLLWISGAYGDIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNNKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLTISSLQAEDVAVYYCQQYYSTP
Protein: Nicotinic acetylcholine receptor Dalpha6 subunit variant type I (Nicotinic acetylcholine receptor alpha6, isoform A) (Q9VL79)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034104}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00034104}.
Interaction partners:
Sequence:
MDSPLPASLSLFVLLIFLAIIKESCQGPHEKRLLNHLLSTYNTLERPVANESEPLEVKFGLTLQQIIDVDEKNQILTTNAWLNLEWNDYNLRWNETEYGGVKDLRITPNKLWKPDVLMYNSADEGFDGTYHTNIVVKHNGSCLYVPPGIFKSTCKIDITWFPFDDQHCEMKFGSWTYDGNQLDLVLNSEDGGDLSDFITNGEWYLLAMPGKKNTIVYACCPEPYVDITFTIQIRRRTLYYFFNLIVPCVLISSMALLGFTLPPDSGEKLTLGVTILLSLTVFLNLVAETLPQVSDAIPLLGTYFNCIMFMVASSVVLTVVVLNYHHRTADIHEMPPWIKSVFLQWLPWILRMGRPGRKITRKTILLSNRMKELELKERSSKSLLANVLDIDDDFRHTISGSQTAIGSSASFGRPTTVEEHHTAIGCNHKDLHLILKELQFITARMRKADDEAELIGDWKFAAMVVDRFCLIVFTLFTIIATVTVLLSAPHIIVQ
Protein: ProSAAS (IA-4) (Proprotein convertase subtilisin/kexin type 1 inhibitor) (Proprotein convertase 1 inhibitor) (pro-SAAS) [Cleaved into: KEP; Big SAAS (b-SAAS); Little SAAS (l-SAAS); Big PEN-LEN (b-PEN-LEN) (SAAS CT(1-49)); PEN; PEN-20; PEN-19; Little LEN (l-LEN); Big LEN (b-LEN) (BigLEN) (SAAS CT(25-40))] (Q9QXV0)
Organism: Mus musculus (Mouse)
Function: May function in the control of the neuroendocrine secretory pathway. Proposed be a specific endogenous inhibitor of PCSK1. ProSAAS and Big PEN-LEN, both containing the C-terminal inhibitory domain, but not the processed peptides reduce PCSK1 activity in the endoplasmic reticulum and Golgi. It reduces the activity of the 87 kDa form but not the autocatalytically derived 66 kDa form of PCSK1. Subsequent processing of proSAAS may eliminate the inhibition. Slows down convertase-mediated processing of proopiomelanocortin and proenkephalin. May control the intracellular timing of PCSK1 rather than its total level of activity.
Subcellular location: Secreted {ECO:0000269|PubMed:10632593, ECO:0000269|PubMed:11742530}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:11742530}.
Interaction partners:
- G-protein coupled receptor 171
- Neuroendocrine convertase 2
- G-protein coupled receptor 83
- Secretogranin-2
- Neuroendocrine convertase 1
- Carboxypeptidase E
- Secretogranin-1
- Neuroendocrine protein 7B2
Sequence:
MAGSPLLCGPRAGGVGILVLLLLGLLRLPPTLSARPVKEPRSLSAASAPLVETSTPLRLRRAVPRGEAAGAVQELARALAHLLEAERQERARAEAQEAEDQQARVLAQLLRAWGSPRASDPPLAPDDDPDAPAAQLARALLRARLDPAALAAQLVPAPAAAPRPRPPVYDDGPTGPDVEDAGDETPDVDPELLRYLLGRILTGSSEPEAAPAPRRLRRSVDQDLGPEVPPENVLGALLRVKRLENPSPQAPARRLLPP
Protein: ATP synthase subunit g, mitochondrial (ATPase subunit g) (Q09774)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Putative ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit d
- ATP synthase subunit 4
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit a
- ATP synthase subunit alpha
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit 9, mitochondrial
Sequence:
MFSTSRIISRINYNFLRKSHYSTKTVAEQAKGRFTPLIQKLSAVQQPIMYWANVSKELVQQVYHSQKIAPPSNTHSPFLFWKSQSSEAWGRNFFIAVEIVGIFCAGQMVGRRKITPYH