wanglab/gogpt-training-data huggingface dataset:
Protein: Fibroblast growth factor 8 (FGF-8) (Androgen-induced growth factor) (AIGF) (Heparin-binding growth factor 8) (HBGF-8) (P37237)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. Required for normal brain, eye, ear and limb development during embryogenesis. Required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Plays a role in neurite outgrowth in hippocampal cells (By similarity). Cooperates with Wnt-1 in mouse mammary tumor virus-induced murine mammary tumorigenesis.
Subcellular location: Secreted.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Fibroblast growth factor receptor 3
- Fibroblast growth factor receptor 4
- Klotho
- Pro-epidermal growth factor
- Vascular endothelial growth factor receptor 2
- Fibroblast growth factor receptor-like 1
- Beta-klotho
- Decorin
Sequence:
MGSPRSALSCLLLHLLVLCLQAQVRSAAQKRGPGAGNPADTLGQGHEDRPFGQRSRAGKNFTNPAPNYPEEGSKEQRDSVLPKVTQRHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQVLANKRINAMAEDGDPFAKLIVETDTFGSRVRVRGAETGLYICMNKKGKLIAKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPRGHHTTEQSLRFEFLNYPPFTRSLRGSQRTWAPEPR
Protein: General amino-acid permease GAP1 (P19145)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: General amino-acid permease involved in the uptake of all the naturally occurring L-amino-acids, related compounds such as ornithine and citrulline, some D-amino acids, toxic amino acid analogs such as azetidine-2-carboxylate, and the polyamines putrescine and spermidine. Senses its transport substrates to set an appropriate level of transporter activity at the cell surface. Required for FLO11 expression and invasive growth.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11352928, ECO:0000269|PubMed:11500494, ECO:0000269|PubMed:12417748, ECO:0000269|PubMed:12499351, ECO:0000269|PubMed:14523026, ECO:0000269|PubMed:15039776, ECO:0000269|PubMed:15707981, ECO:0000269|PubMed:21471002}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15707981}; Multi-pass membrane protein {ECO:0000255}. Note=Depending on nitrogen source, GAP1 is transported to the plasma membrane, where it functions for amino acid uptake, or to the vacuole, where it is degraded (PubMed:11352928, PubMed:11500494, PubMed:12417748, PubMed:12499351, PubMed:14523026, PubMed:15039776, PubMed:21471002). {ECO:0000269|PubMed:11352928, ECO:0000269|PubMed:11500494, ECO:0000269|PubMed:12417748, ECO:0000269|PubMed:12499351, ECO:0000269|PubMed:14523026, ECO:0000269|PubMed:15039776, ECO:0000269|PubMed:21471002}.
Interaction partners:
- Ammonium transporter MEP2
- GABA-specific permease
- Ubiquitin ligase-binding protein BUL1
- Protein LST4
- Ubiquitin ligase-binding protein BUL2
- Plasma membrane ATPase 1
- Vacuolar amino acid transporter 5
- E3 ubiquitin-protein ligase RSP5
- Nitrogen permease reactivator protein
- Uracil permease
Sequence:
MSNTSSYEKNNPDNLKHNGITIDSEFLTQEPITIPSNGSAVSIDETGSGSKWQDFKDSFKRVKPIEVDPNLSEAEKVAIITAQTPLKHHLKNRHLQMIAIGGAIGTGLLVGSGTALRTGGPASLLIGWGSTGTMIYAMVMALGELAVIFPISGGFTTYATRFIDESFGYANNFNYMLQWLVVLPLEIVSASITVNFWGTDPKYRDGFVALFWLAIVIINMFGVKGYGEAEFVFSFIKVITVVGFIILGIILNCGGGPTGGYIGGKYWHDPGAFAGDTPGAKFKGVCSVFVTAAFSFAGSELVGLAASESVEPRKSVPKAAKQVFWRITLFYILSLLMIGLLVPYNDKSLIGASSVDAAASPFVIAIKTHGIKGLPSVVNVVILIAVLSVGNSAIYACSRTMVALAEQRFLPEIFSYVDRKGRPLVGIAVTSAFGLIAFVAASKKEGEVFNWLLALSGLSSLFTWGGICICHIRFRKALAAQGRGLDELSFKSPTGVWGSYWGLFMVIIMFIAQFYVAVFPVGDSPSAEGFFEAYLSFPLVMVMYIGHKIYKRNWKLFIPAEKMDIDTGRREVDLDLLKQEIAEEKAIMATKPRWYRIWNFWC
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 2 (PPP4R2-related protein) (Q9W2U4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4) (By similarity). The probable PP4 complex Pp4-19C-PPP4R2r-flfl (PPP4C-PPP4R2-PPP4R3) is required to prevent caspase induced cell death (in vitro).
Interaction partners:
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 3
- Serine/threonine-protein phosphatase
- LD07294p
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase PP2A
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase 2A activator
- Serine/threonine-protein phosphatase PP2A 65 kDa regulatory subunit
- Serine/threonine-protein phosphatase 2B catalytic subunit 2
Sequence:
MVTMENSDEIMQILERFTDLKQKEIPKELEEYLQYVAKTGDTIFKWSSLKYLFREKLLSVIKHFNEDSPRLEEIPNYPNVDPFNYETMKSSLLERLDLFNAAPFTVQRLCELLIDPRKQYSRIDKFMRALEKNILVVSTIDPGRKRTESENGDSLDSVVNGDLSMEVNIDIEMENNNGNADEGSSPGAGSAGCAQKASCPRSDDNDQPKAKKAKLEIDGEERSEASDETDTEVATRVKNEKDEKNDNDETDSPHEAAEIEEPDEEVDEADQETKTTKQPAYGSQKEGEQEESFPSSADDEAEDPMVSKSIEAEKELVAQEKKREEDKKVAIEPKEEIVKKEEVVESDKPDGKVAQLGDKAVVKKSTPPADGENQEPVKVKAENEKEEKKHAPIKTEKQDDIDSTETDDAPSAEKPAEEKIASSESKPKTKSEDDPEAETKKSQPEKTETEAAEKSVSDEKQAAEPNAESENRNDLTTSKATEAAQESVEKSPVEDASSPAVEDLAAATTPQSPLGAADSAAETPPAETGDDSQASPLVAAVTPPVLALNDQPMEDTPAEEEARVSPSATVEEVVMAESANAGAMATEEAAKDDPAAMEIDDTSQEVMMQ
Protein: Coagulation factor XI (FXI) (EC 3.4.21.27) (Plasma thromboplastin antecedent) (PTA) [Cleaved into: Coagulation factor XIa heavy chain; Coagulation factor XIa light chain] (Q91Y47)
Organism: Mus musculus (Mouse)
Function: Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX.
Subcellular location: Secreted.
Interaction partners:
- Coagulation factor XII
- Antithrombin-III
- Coagulation factor VIII
- Coagulation factor IX
- Tissue factor
- Platelet glycoprotein Ib alpha chain
- Thrombomodulin
- Vitamin K-dependent protein C
- Prothrombin
- Coagulation factor VII
Sequence:
MTSLHQVLYFIFFASVSSECVTKVFKDISFQGGDLSTVFTPSATYCRLVCTHHPRCLLFTFMAESSSDDPTKWFACILKDSVTEILPMVNMTGAISGYSFKQCPQQLSTCSKDVYVNLDMKGMNYNSSVVKNARECQERCTDDAHCQFFTYATGYFPSVDHRKMCLLKYTRTGTPTTITKLNGVVSGFSLKSCGLSNLACIRDIFPNTVLADLNIDSVVAPDAFVCRRICTHHPTCLFFTFFSQAWPKESQRHLCLLKTSESGLPSTRITKSHALSGFSLQHCRHSVPVFCHPSFYNDTDFLGEELDIVDVKGQETCQKTCTNNARCQFFTYYPSHRLCNERNRRGRCYLKLSSNGSPTRILHGRGGISGYSLRLCKMDNVCTTKINPRVVGGAASVHGEWPWQVTLHISQGHLCGGSIIGNQWILTAAHCFSGIETPKKLRVYGGIVNQSEINEGTAFFRVQEMIIHDQYTTAESGYDIALLKLESAMNYTDFQRPICLPSKGDRNAVHTECWVTGWGYTALRGEVQSTLQKAKVPLVSNEECQTRYRRHKITNKMICAGYKEGGKDTCKGDSGGPLSCKYNGVWHLVGITSWGEGCGQKERPGVYTNVAKYVDWILEKTQTV
Protein: Delta(24)-sterol reductase (EC 1.3.1.72) (Cell elongation protein DIMINUTO) (Cell elongation protein Dwarf1) (Protein CABBAGE1) (Protein ENHANCED VERY-LOW-FLUENCE RESPONSE 1) (Q39085)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a critical role in the general process of plant cell elongation. Involved in the synthesis of campesterol, an early precursor of brassinolide. Required for the conversion of 24-methylenecholesterol to campesterol and for the conversion of isofucosterol to sitosterol. Necessary for both the isomerization and reduction of 24-methylenecholesterol. Regulates indirectly phytochrome-mediated light responses through the modulation of brassinosteroid biosynthesis.
Subcellular location: Microsome membrane {ECO:0000269|PubMed:9761794}; Single-pass type II membrane protein {ECO:0000269|PubMed:9761794}; Cytoplasmic side {ECO:0000269|PubMed:9761794}.
Interaction partners:
- Delta
- 7-dehydrocholesterol reductase
- Probable 3-beta-hydroxysteroid-Delta
- Sterol 14-demethylase
- Delta
- Cycloartenol-C-24-methyltransferase
- Lanosterol synthase
- Putative Delta
- Steroid
- Cytochrome P450 710A1
Sequence:
MSDLQTPLVRPKRKKTWVDYFVKFRWIIVIFIVLPFSATFYFLIYLGDMWSESKSFEKRQKEHDENVKKVIKRLKGRDASKDGLVCTARKPWIAVGMRNVDYKRARHFEVDLGEFRNILEINKEKMTARVEPLVNMGQISRATVPMNLSLAVVAELDDLTVGGLINGYGIEGSSHIYGLFADTVEAYEIVLAGGELVRATRDNEYSDLYYAIPWSQGTLGLLVAAEIRLIKVKEYMRLTYIPVKGDLQALAQGYIDSFAPKDGDKSKIPDFVEGMVYNPTEGVMMVGTYASKEEAKKKGNKINNVGWWFKPWFYQHAQTALKKGQFVEYIPTREYYHRHTRCLYWEGKLILPFGDQFWFRYLLGWLMPPKVSLLKATQGEAIRNYYHDMHVIQDMLVPLYKVGDALEWVHREMEVYPIWLCPHKLFKQPIKGQIYPEPGFEYENRQGDTEDAQMYTDVGVYYAPGCVLRGEEFDGSEAVRRMEKWLIENHGFQPQYAVSELDEKSFWRMFNGELYEECRKKYRAIGTFMSVYYKSKKGRKTEKEVREAEQAHLETAYAEAD
Protein: Broad specificity amino-acid racemase YgeA (EC 5.1.1.10) (P03813)
Organism: Escherichia coli (strain K12)
Function: Amino-acid racemase able to utilize a broad range of substrates. Highest activity is observed with L-homoserine and D-homoserine. Has tenfold lower activity against L-methionine, L-leucine, L-valine and L-histidine. Has low activity with L-norvaline, L-asparagine, D-methionine, L-aminobutyric acid, L-isoleucine, L-serine, L-norleucine, L-alanine, L-glutamine, LL-diaminopimelic acid and L-phenylalanine. Has no activity against ten L-amino acids (Thr, Glu, Asp, Arg, Lys, Tyr, Trp, Orn, Cit and Aad). D-amino acids might be used as components of peptidoglycan and/or be involved in peptidoglycan metabolism and remodeling.
Interaction partners:
- Arabinose-proton symporter
Sequence:
MKTIGLLGGMSWESTIPYYRLINEGIKQRLGGLHSAQVLLHSVDFHEIEECQRRGEWDKTGDILAEAALGLQRAGAEGIVLCTNTMHKVADAIESRCTLPFLHIADATGRAITGAGMTRVALLGTRYTMEQDFYRGRLTEQFSINCLIPEADERAKINQIIFEELCLGQFTEASRAYCAQVIARLAEQGAQGVIFGCTEIGLLVPEERSVLPVFDTAAIHAEDAVAFMLS
Protein: Microtubule-associated protein 70-4 (AtMAP70-4) (70 kDa microtubule-associated protein 4) (Q9LQU7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plant-specific protein that interact with microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Associated to microtubules.
Interaction partners:
- Protein SCAR3
- Protein trichome birefringence-like 18
- 187-kDa microtubule-associated protein AIR9
- Kinesin-like protein KIN-12B
- Kinesin-like protein KIN-14C
- Protein trichome birefringence-like 8
- Protein trichome birefringence-like 9
- Protein trichome birefringence-like 16
- At4g28310
- 65-kDa microtubule-associated protein 1
Sequence:
MEERGFMSPSLAISASYREGGSKGMSRRRSMRPSFDADNEFMNLLHGSDPVRIELNRLENEVRDKDRELSEGQAEIKALRLSERQREKAVEELTEELGKMAEKLKLIENLLESKNLEIKKINEEKKASMAAQFAAEASLRRVHAAQKDDDMPPIEAILAPLEAELKLSRQEIAKLQDDNKSLDRLTKSKEAALLDAERTVQSALAKASMVDDLQNKNQELMKQIEICQEENRIIDKMHRQKVAEVEKLMQSVRELEEAVLAGGAAANAVRDYQRKFQEMNEERKILERELARAKVNANRVATVVANEWKDSNDKVMPVRQWLEERRFLQGEMQQLRDKLAIADRAAKSEAQLKEKFLLRLRVLEESLKGPTSSSSRGTSVGRSSSNGPTRRQSLGGAETSPKITSNGSLIKRTPSSQLRSLTASASTVLKHAKGTSRSFDGGTRSLDRSKVLINGPRSNFPLNHKSSEGTSRGESPSSIKGEEESADKATNNDSVPGVLYDLLQKEVITLRKAAHEKDQSLRDKDEAIEMLAKKVETLTKAMDVEAKKMRREVAVMGKEVAAMRVVDKGQQDSKTRRLSVSKGNTAQLLSGRVSGRIGMTRSTQ
Protein: Alanine--glyoxylate aminotransferase 2, mitochondrial (AGT 2) (EC 2.6.1.44) ((R)-3-amino-2-methylpropionate--pyruvate transaminase) (EC 2.6.1.40) (Beta-ALAAT II) (Beta-alanine-pyruvate aminotransferase) (EC 2.6.1.18) (D-3-aminoisobutyrate-pyruvate aminotransferase) (D-AIBAT) (D-beta-aminoisobutyrate-pyruvate aminotransferase) (Q3UEG6)
Organism: Mus musculus (Mouse)
Function: Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BYV1}.
Interaction partners:
- Acidic amino acid decarboxylase GADL1
- Cysteine sulfinic acid decarboxylase
- Alanine--glyoxylate aminotransferase
- Glutamate decarboxylase 2
- Homogentisate 1,2-dioxygenase
- N
- Glutamate decarboxylase 1
- Coagulation factor XIII B chain
- Putative hydrolase DDAH2
- UDP-glucuronosyltransferase 3A2
Sequence:
MSLAWRNLQKPFYLETSLRILQMRPSLSLGASRIAVPKLTLHTKHSMPPCDFSPEKYQSLAYSRVLAIHKQHLSPVDTAYFRKPLLLHQGHMEWLFDSEGNRYLDFFSGIVTVSVGHCHPKVSAVAKKQIDRLWHTSSVFFHSPMHEYAEKLSALLPEPLKVIFLVNSGSEANDLAMVMARAHSNHTDIISFRGAYHGCSPYTLGLTNVGIYKMEVPGGIGCQSTMCPDVFRGPWGGIHCRDSPVQTVRDCSCAPDCCQAKERYIEQFKDTLNTSVATSIAGFFAEPIQGVNGVVQYPKEFLKEAFALVRERGGVCIADEVQTGFGRLGSHFWGFQTHDVLPDIVTMAKGIGNGFPMAAVVTTPEIAKSLAKRLLHFSTFGGNPLACAIGSAVLEVIEEENLQRNSQEVGTYMLLKFAKLRDEFDIVGDVRGKGLMVGIEMVQDKISRQPLPKTEVNQIHEDCKDMGLLVGRGGNFSQTFRIVPPMCVTKMEVDFAYEVFRAALIQHMERRAK
Protein: Ras-related protein Rab-7L1 (Rab-7-like protein 1) (Ras-related protein Rab-29) (Q91YQ1)
Organism: Mus musculus (Mouse)
Function: The small GTPases Rab are key regulators in vesicle trafficking (By similarity). Essential for maintaining the integrity of endosome-trans-Golgi network structure (By similarity). Together with LRRK2, plays a role in the retrograde trafficking pathway for recycling proteins, such as mannose 6 phosphate receptor (M6PR), between lysosomes and the Golgi apparatus in a retromer-dependent manner (By similarity). Recruits LRRK2 to the Golgi apparatus and stimulates LRRK2 kinase activity (By similarity). Regulates also neuronal process morphology in the intact central nervous system (CNS) (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O14966}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O14966}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:O14966}. Golgi apparatus {ECO:0000250|UniProtKB:O14966}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O14966}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:O14966}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O14966}. Note=Colocalizes with GM130 at the Golgi apparatus (By similarity). Colocalizes with LRRK2 at dynamic tubules emerging from and retracting to the Golgi apparatus (By similarity). Colocalizes with TGN46 at the trans-Golgi network (TGN) (By similarity). {ECO:0000250|UniProtKB:O14966, ECO:0000250|UniProtKB:Q63481}.
Interaction partners:
- Cyclin-G-associated kinase
- Nuclear ubiquitous casein and cyclin-dependent kinase substrate 1
- BAG family molecular chaperone regulator 5
- RILP-like protein 1
- Leucine-rich repeat serine/threonine-protein kinase 2
- RILP-like protein 2
- Vacuolar protein sorting-associated protein 35
- Guanine nucleotide exchange factor C9orf72 homolog
- Mth938 domain-containing protein
Sequence:
MGSRDHLFKVLVVGDAAVGKTSLVQRYSQDSFSKHYKSTVGVDFALKVLQWSDSEMVRLQLWDIAGQERFTSMTRLYYRDASACVIMFDVTNATTFSNSQRWKQDLDSKLTLPSGEPVPCLLLANKSDLSPWAVSRDQIDRFSKENGFTGWTETSVKENKNINEAMRVLVEKMMNNSREDVMSLSTQGNYINLQAKPSSGWTCC
Protein: Adhesion defective protein 3 (LisH domain-containing protein adn3) (O74522)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable transcriptional regulator involved in cell adhesion.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10759889}. Nucleus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- DASH complex subunit dam1
Sequence:
MADFMDIEPSSHSAKASQYESSAPASSSLGNSHPNESLDYYIYDYFVKHNFEEAAQAFLRESKIQIPKSSSSTAFSPSNNNAPSPFPPKNSSLASPSKISESISGDRLYNHMSSAPSPNKKEETNVVHANEDISLDKRQSFGSSSLPPSEVSINVPEGFLVEWFNIFWDVFSARVSRVNSTPIQLYDPSTQRQMARPMSNLQASQPVPSSTFSRSAVVPNPSLPLNPSVLQGQVMNNPTIPKGTPSTSIEGAKTSIPPSHAMQNPHNSFPASADRLQKNHPVQSSNFNPYTPAPSITVPPNYIPNTAMMGPSYSSFGDTDPRTYPAGMGPNPTAARNGFYPPTPAQIHQLKAQQQHLQRQSKQMSEPAPINMKSNKDQQLQYVDFRGVGSGADLQKQQWNKSTSAEGLQPNGLVMRNFGDVRHQKLPTSSPPSQHPPVGQIPSQYLPYQAGLKVPGNTPIPVKQVGGMPLQSPLPVSMKPSADDHSRATPTRSVEAPTLPSYAPRHPTQANGSRYMNPSTSRMTPQSPYMQNYYRPHAQMQDQNNMMSYMLSQQKAMEIAKSREMAIQRNTQTLSSGNQPPQQSGPNPNEFSMSMDPANMQQGNHALSDYHMQLMLLEEQNKKRLMMARQEQGTGSLSPQSYMNSRYSVDVGKEHMSMIPNQTAPMIQPNVPVSANSPAQANTPAADSTKSGTIQPTNRNGEGLSYSPHQQFSPSAPQAEKLSRSMSPFVSQQQQLNQPVSNKPDGLTQNKEVTGMPLNKEELTNPAFPQSRTSWMMPQSFDTSSLNAPGAKDSSSFSSLHAQPGKSGIATMGVADNTIRTTERSTFSEIMKDSPSAHASPGAKTSPNASRAPEPTGGTNSISQDTTQSLQMQSNSVNSSSMVDASKSKEKSGGDTSALDSNAKNEPTAAKPISKLEDDALFNDSAGNAFGFSSKTDSNVEMLNDFDFESFLNDAGADSASVYY
Protein: BRD4-interacting chromatin-remodeling complex-associated protein (Glioma tumor suppressor candidate region gene 1 protein) (F8VPZ9)
Organism: Mus musculus (Mouse)
Function: Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. May play a role in BRD4-mediated gene transcription (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9NZM4}.
Interaction partners:
- Bromodomain-containing protein 9
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- SWI/SNF complex subunit SMARCC1
- AT-rich interactive domain-containing protein 1A
- B-cell CLL/lymphoma 7 protein family member C
- B-cell CLL/lymphoma 7 protein family member A
- Protein SSXT
Sequence:
MDDEDGRCLLDVICDPQALNDFLHGSEKLDSDDLLDAPVEAQSAFYEGPGLHVQEAAANHLNPEPSQPAPSVDLDFLEDDILGSPAAGGGGGGGGAPDQPCDILQQSLQEANITEQTLEAEAELDLGPFQLPTLQPADNGAGATGAAGATAVTAGPQALFPGSADLLGLQAPPTVLTHQALVPPQDVVNKALSVQPFLQPVGLGNVTLQPISGLQGLPNGSPGNAAAATLGLTPIQVVGQPVMALNPPTSQLLAKQVPVSGYLASAAGPSEPVTLASAGVSPQGAGLVIQKNLPAAVTTTLNGNSVFAGTGAATAAASGAPSGQPLAVAPGLGTSPLVQAPSVILHRTPTPIQPKPTGVLPSKLYQLTPKPFPPTGATLTIQGEPGTLPQQPKAPQNLTFMATGKAGQNVVLSGFPAPALQANVFKQPPVTTTGTAPPQPPGALSKPMSVHLLNQGSSIVIPAQHMLPGQNQFLLPGTPAVQLPQSLSALPANVGGQILTAAAPHAGGQLIANPILTNQNLAGPLSLGPVLAPHSGAHSAAHILSAAPIQVGQPALFQMPVSLATGSLPTQSQPAPTGPTATTVLQGVTLPPSAVAMLNTPDGLVQPSTPAATTGEATPVLAVQPATQVPPAVTTPLPMGLQQPQAQQPPQVPTPQAATQPQATPPQASPSLASSPEKIVLGQAPPAATTAILTQDSLQMFLPQERSQQPLSTEGPHLSVPASVIVSAPPPAQDPALATPVTKGAGLGAQTPDSRASPAPAPQIPAAAPLKAPGPASSPSLPHQAPLGDSPHMPSPHPARPPSRPPSRPHSRPPSQPQSLTCPPSEPTLHPCPPPQGPPTLPGIFVIQNQLGAPPPASTPASTAPGPPQPPLRPPSQPPEGPLPPASHLPPASTPSAVASSSEPSARLPVPTPPDFQLQFPPSQGPHKSPTPPPALHMVPEPTAPPPPPPRTFQMVTAPFPALPQPKALLERFHQVPSGIILQNKAGGTPTTPQTSTTLGTLTGPTASVLVSGQAPPGTPAASSHVPASTPMATTGLPPLLPAENKAFASNLPTLSVAKATVSGPGKPPAIQYDSKLCSLKKQPLLQPSKEACFLEHLHKHQGSVLHPDYKTAFPSFEDALHRLLPYHVYQGALPSPNDYHKVDEEFETVSTQLLKRTQAMLNKYRLLLLEESRRVSPSAEMVMIDRMFIQEEKTTLALDKQLAKEKPDEYVSSSRSLGFPVPVSSEGHRLPSHGQSSSSSTSGTSAQPPPHLPTKLVIRHGGAGGSPSVTWARASSSLSSTSSSSSSSSAASSLDADEDGPMPTRNRPPIKTYEARSRIGLKLKIKQEAGLSKVVHNTALDPVHQPLPAPTPAKGAEPPPHPAPPPLPPATQAQMNGTLDHPPPAVRKPTVPASCPRLPLRKTYRENMGNPGAAEGAQGRPRGAGSPTPLPTKVDEATSGLIRELAAVEDELYQRVLKGGPPPPETPASATSQGPTEPSWEAPVLPPAKRRKSESPDVDQASFSSDSPQDDTLTEHLQSAIDSILNLQQAPGRTPAGPYPHTGPTPGTPTSPAPLHRPDAFPPSSHNGGLGARTLNR
Protein: Cilium assembly protein DZIP1L (DAZ-interacting zinc finger protein 1-like) (Q8IYY4)
Organism: Homo sapiens (Human)
Function: Involved in primary cilium formation. Probably acts as a transition zone protein required for localization of PKD1/PC1 and PKD2/PC2 to the ciliary membrane.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:19852954, ECO:0000269|PubMed:28530676}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:28530676}. Note=Localizes to centrioles and to the distal ends of basal bodies (PubMed:28530676). {ECO:0000269|PubMed:28530676}.
Interaction partners:
- Protein chibby homolog 1
Sequence:
MQSPAATAEGLSGPLFGAYTFPTFKFQPRHDSMDWRRISTLDVDRVARELDVATLQENIAGITFCNLDREVCSRCGQPVDPALLKVLRLAQLIIEYLLHCQDCLSASVAQLEARLQTSLGQQQRGQQELGRQADELKGVREESRRRRKMISTLQQLLMQTGTHSYHTCHLCDKTFMNATFLRGHIQRRHAGVAEGGKQKKQEQPVEEVLEELRAKLKWTQGELEAQREAERQRQLQEAELIHQREIEAKKEFDKWKEQEWTKLYGEIDKLKKLFWDEFKNVAKQNSTLEEKLRALQSHSVMESKLGSLRDEESEEWLRQARELQALREKTEIQKTEWKRKVKELHEEHMAEKKELQEENQRLQASLSQDQKKAAAQSQCQISTLRAQLQEQARIIASQEEMIQSLSLRKVEGIHKVPKAVDTEEDSPEEEMEDSQDEQHKVLAALRRNPTLLKHFRPILEDTLEEKLESMGIRKDAKGISIQTLRHLESLLRVQREQKARKFSEFLSLRGKLVKEVTSRAKERQENGAVVSQPDGQPSVKSQQSTLVTREAQPKTRTLQVALPSTPAEPPPPTRQSHGSHGSSLTQVSAPAPRPGLHGPSSTPPSSGPGMSTPPFSSEEDSEGDRVQRVSLQPPKVPSRMVPRPKDDWDWSDTETSEENAQPPGQGSGTLVQSMVKNLEKQLEAPAKKPAGGVSLFFMPNAGPQRAATPGRKPQLSEDESDLEISSLEDLPLDLDQREKPKPLSRSKLPEKFGTGPQSSGQPRVPAW
Protein: Rho GDP-dissociation inhibitor 2 (Rho GDI 2) (Ly-GDI) (Rho-GDI beta) (P52566)
Organism: Homo sapiens (Human)
Function: Regulates the GDP/GTP exchange reaction of the Rho proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them. Regulates reorganization of the actin cytoskeleton mediated by Rho family members.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10802295}.
Interaction partners:
- Transforming protein RhoA
- Ras-related C3 botulinum toxin substrate 2
- Tumor necrosis factor receptor superfamily member 16
- Cell division control protein 42 homolog
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- Rho GDP-dissociation inhibitor 1
- Rho GDP-dissociation inhibitor 3
- Ras-related C3 botulinum toxin substrate 1
Sequence:
MTEKAPEPHVEEDDDDELDSKLNYKPPPQKSLKELQEMDKDDESLIKYKKTLLGDGPVVTDPKAPNVVVTRLTLVCESAPGPITMDLTGDLEALKKETIVLKEGSEYRVKIHFKVNRDIVSGLKYVQHTYRTGVKVDKATFMVGSYGPRPEEYEFLTPVEEAPKGMLARGTYHNKSFFTDDDKQDHLSWEWNLSIKKEWTE
Protein: Ovochymase-2 (EC 3.4.21.-) (Oviductin) (Q7RTZ1)
Organism: Homo sapiens (Human)
Function: May be required for sperm ADAM3 processing and consequential sperm fertilizing ability (By similarity). In vitro, has an endopeptidase activity.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P79953}.
Interaction partners:
Sequence:
MLISRNKLILLLGIVFFERGKSATLSLPKAPSCGQSLVKVQPWNYFNIFSRILGGSQVEKGSYPWQVSLKQRQKHICGGSIVSPQWVITAAHCIANRNIVSTLNVTAGEYDLSQTDPGEQTLTIETVIIHPHFSTKKPMDYDIALLKMAGAFQFGHFVGPICLPELREQFEAGFICTTAGWGRLTEGGVLSQVLQEVNLPILTWEECVAALLTLKRPISGKTFLCTGFPDGGRDACQGDSGGSLMCRNKKGAWTLAGVTSWGLGCGRGWRNNVRKSDQGSPGIFTDISKVLPWIHEHIQTGNRRKSSRAWCSEQDVIVSGAEGKLHFPESLHLYYESKQRCVWTLLVPEEMHVLLSFSHLDVESCHHSYLSMYSLEDRPIGKFCGESLPSSILIGSNSLRLKFVSDATDNAARFNLTYKALKPNYIPDSGCSYLTVLFEEGLIQSLNYPENYSDKANCDWIFQASKHHLIKLSFQSLEIEESGDCTSDYVTVHSDVERKKEIARLCGYDVPTPVLSPSSIMLISFHSDENGTCRGFQATVSFIPKAGKKIELPTLWFPVLILVM
Protein: Protein RecA (C1F6L2)
Organism: Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB 13165 / 161)
Interaction partners:
- LexA repressor
- DNA polymerase I
- Protein RecA
- Protein RecA
- ATP-dependent DNA helicase RecQ
- UmuC domain-containing protein
- Regulatory protein RecX
- DNA-directed DNA polymerase
- DNA 3'-5' helicase
- DNA 3'-5' helicase II
Sequence:
MPTAALLRRQIESALAEKIPAALSPQPRMVHPSAATGIEALDKLLHGGLPVGAISEISGPECSGRTAIALSFLARMTQSHFCAWVDAGDAMDPVSAASVGVDLNRLLWVRCGVQTIAPRGSTDYRFELPAKYLQPEPVVAPKGLPTGSFGMHPRSEVKGMHEAVGNLFSPRCAEPQKRMPREKEEIRGTSIPSRRSNAAATSKSRPWPRIEQALRAMDLILQTGGFRAVVLDLGGYAPEFVTRIPLATWFRYRAAAERTQASLVLLTQTSCAKSSAELLLRMHPPRFEQQEATVFIGMRPCAELLRRRFTKDDSAVVPLLKQPQRATTATWTNGAAWVGPR
Protein: 2610042L04Rik protein (RIKEN cDNA 2610042L04 gene) (Q9D073)
Organism: Mus musculus (Mouse)
Interaction partners:
- Disks large homolog 4
Sequence:
MTKQRSKINELEELKLYMRKISNDMEEMCGILNLYIYEDLNYRMNTEFNIIKSQHEKTMLDMNKMIQSIIGSMQYSKELIEDNYSYSIKEDHLLRECTQLNENVRILLNENRRLLVEQAGHKCPVGKKRGSLRRPARTSVSQVPRNNSVK
Protein: Immunoglobulin lambda variable 1-40 (Ig lambda chain V-I region NEWM) (P01703)
Organism: Homo sapiens (Human)
Function: V region of the variable domain of immunoglobulin light chains 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:
MAWSPLLLTLLAHCTGSWAQSVLTQPPSVSGAPGQRVTISCTGSSSNIGAGYDVHWYQQLPGTAPKLLIYGNSNRPSGVPDRFSGSKSGTSASLAITGLQAEDEADYYCQSYDSSLSG