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Q02040

- AK17A_HUMAN

UniProt

Q02040 - AK17A_HUMAN

Protein

A-kinase anchor protein 17A

Gene

AKAP17A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (01 May 2007)
      Previous versions | rss
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    Functioni

    Splice factor regulating alternative splice site selection for certain mRNA precursors. Mediates regulation of pre-mRNA splicing in a PKA-dependent manner.2 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. protein kinase A binding Source: UniProtKB

    GO - Biological processi

    1. B cell activation Source: UniProtKB
    2. mRNA processing Source: UniProtKB-KW
    3. regulation of RNA splicing Source: UniProtKB
    4. regulation of transcription, DNA-templated Source: UniProtKB
    5. RNA splicing Source: UniProtKB-KW
    6. signal transduction Source: UniProtKB

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A-kinase anchor protein 17A
    Short name:
    AKAP-17A
    Alternative name(s):
    721P
    B-lymphocyte antigen
    Protein XE7
    Protein kinase A-anchoring protein 17A
    Short name:
    PRKA17A
    Splicing factor, arginine/serine-rich 17A
    Gene namesi
    Name:AKAP17A
    Synonyms:CXYorf3, DXYS155E, SFRS17A, XE7
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:18783. AKAP17A.

    Subcellular locationi

    Nucleus speckle 2 Publications

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi438 – 4392LL → PP: Abolishes binding to PKA-RI; when associated with 445-P-P-446. 1 Publication
    Mutagenesisi445 – 4462KK → PP: Abolishes binding to PKA-RI; when associated with 438-P-P-439. 1 Publication

    Organism-specific databases

    PharmGKBiPA162402969.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 695695A-kinase anchor protein 17APRO_0000022692Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei537 – 5371Phosphoserine2 Publications
    Modified residuei633 – 6331Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ02040.
    PaxDbiQ02040.
    PRIDEiQ02040.

    PTM databases

    PhosphoSiteiQ02040.

    Expressioni

    Tissue specificityi

    Widely expressed. Found in heart, brain, lung, liver, skeletal muscle, kidney and pancreas. Expressed in activated B-cells and placenta. Expressed in all cell lines tested including Jurkat-TAg, U-937 and HEK293 cells.1 Publication

    Gene expression databases

    BgeeiQ02040.
    CleanExiHS_SFRS17A.
    GenevestigatoriQ02040.

    Organism-specific databases

    HPAiHPA043247.

    Interactioni

    Subunit structurei

    Monomer. Component of the spliceosome. Interacts with ZRANB2 and SFRS1/ASF through its Arg/Ser-rich domain. Interacts with RI and RII subunits of PKA.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ZRANB2O952184EBI-1042725,EBI-1051583

    Protein-protein interaction databases

    BioGridi113860. 7 interactions.
    IntActiQ02040. 4 interactions.
    MINTiMINT-1443812.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02040.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini147 – 256110RRMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni83 – 11230PKA-RI and PKA-RII subunit binding domainAdd
    BLAST
    Regioni425 – 45430PKA-RI-alpha subunit binding domainAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi587 – 695109Arg-richAdd
    BLAST

    Domaini

    RI-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.1 Publication

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG271981.
    InParanoidiQ02040.
    KOiK13169.
    OMAiHNHQFST.
    OrthoDBiEOG7353WR.
    PhylomeDBiQ02040.
    TreeFamiTF320443.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q02040-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAAATIVHDT SEAVELCPAY GLYLKPITKM TISVALPQLK QPGKSISNWE    50
    VMERLKGMVQ NHQFSTLRIS KSTMDFIRFE GEVENKSLVK SFLACLDGKT 100
    IKLSGFSDIL KVRAAEFKID FPTRHDWDSF FRDAKDMNET LPGERPDTIH 150
    LEGLPCKWFA LKESGSEKPS EDVLVKVFEK FGEIRNVDIP MLDPYREEMT 200
    GRNFHTFSFG GHLNFEAYVQ YREYMGFIQA MSALRGMKLM YKGEDGKAVA 250
    CNIKVSFDST KHLSDASIKK RQLERQKLQE LEQQREEQKR REKEAEERQR 300
    AEERKQKELE ELERERKREE KLRKREQKQR DRELRRNQKK LEKLQAEEQK 350
    QLQEKIKLEE RKLLLAQRNL QSIRLIAELL SRAKAVKLRE QEQKEEKLRL 400
    QQQEERRRLQ EAELRRVEEE KERALGLQRK ERELRERLLS ILLSKKPDDS 450
    HTHDELGVAH ADLLQPVLDI LQTVSSGCVS ATTLHPLGGQ PPAGAPKESP 500
    AHPEADGAPK SVNGSVAEEA PCKEVQSSCR VVPEDGSPEK RCPGGVLSCI 550
    PDNNQQPKGI PACEQNVSRK DTRSEQDKCN REPSKGRGRA TGDGLADRHK 600
    RERSRARRAS SREDGRPRKE RRPHKKHAYK DDSPRRRSTS PDHTRSRRSH 650
    SKDRHRRERS RERRGSASRK HSRHRRRSER SRSRSPSRHR STWNR 695
    Length:695
    Mass (Da):80,735
    Last modified:May 1, 2007 - v2
    Checksum:i639E88ECA8006CF2
    GO
    Isoform 2 (identifier: Q02040-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         385-385: A → L
         386-695: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:385
    Mass (Da):45,248
    Checksum:i4C1E253616C969A6
    GO
    Isoform 3 (identifier: Q02040-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         385-445: AVKLREQEQK...ERLLSILLSK → VGGSLCSRQP...EGVALVCRSR
         446-695: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:445
    Mass (Da):51,409
    Checksum:i049E8E08BF58DF27
    GO

    Sequence cautioni

    The sequence AAA36187.1 differs from that shown. Reason: Frameshift at position 461.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti443 – 4431L → Q in AAA36187. (PubMed:1438229)Curated
    Sequence conflicti500 – 5001P → A in AAA61303. (PubMed:1302606)Curated
    Sequence conflicti500 – 5001P → A in AAI10497. (PubMed:15489334)Curated
    Sequence conflicti502 – 5021H → P in AAA36187. (PubMed:1438229)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti194 – 1941P → S.1 Publication
    Corresponds to variant rs17852504 [ dbSNP | Ensembl ].
    VAR_055353

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei385 – 44561AVKLR…ILLSK → VGGSLCSRQPRPGCPQCPPL KCGRRHGAVSPPAAAVATKP ALMPRMTAPSREGVALVCRS R in isoform 3. 1 PublicationVSP_024947Add
    BLAST
    Alternative sequencei385 – 3851A → L in isoform 2. CuratedVSP_004490
    Alternative sequencei386 – 695310Missing in isoform 2. CuratedVSP_004491Add
    BLAST
    Alternative sequencei446 – 695250Missing in isoform 3. 1 PublicationVSP_024948Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L03426 mRNA. Translation: AAA61303.1.
    L03426 mRNA. Translation: AAA61304.1.
    M99578 mRNA. Translation: AAA36187.1. Frameshift.
    AL683807 Genomic DNA. Translation: CAI41499.1.
    AL683807 Genomic DNA. Translation: CAI41501.1.
    BC028151 mRNA. Translation: AAH28151.1.
    BC110496 mRNA. Translation: AAI10497.1.
    BC110497 mRNA. Translation: AAI10498.1.
    CCDSiCCDS14116.1. [Q02040-1]
    PIRiA46419.
    I54325.
    RefSeqiNP_005079.2. NM_005088.2. [Q02040-1]
    UniGeneiHs.522572.

    Genome annotation databases

    EnsembliENST00000313871; ENSP00000324827; ENSG00000197976. [Q02040-1]
    ENST00000474361; ENSP00000435479; ENSG00000197976. [Q02040-2]
    GeneIDi8227.
    KEGGihsa:8227.
    UCSCiuc004cqa.3. human. [Q02040-1]
    uc010ncx.1. human. [Q02040-3]

    Polymorphism databases

    DMDMi146291102.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L03426 mRNA. Translation: AAA61303.1 .
    L03426 mRNA. Translation: AAA61304.1 .
    M99578 mRNA. Translation: AAA36187.1 . Frameshift.
    AL683807 Genomic DNA. Translation: CAI41499.1 .
    AL683807 Genomic DNA. Translation: CAI41501.1 .
    BC028151 mRNA. Translation: AAH28151.1 .
    BC110496 mRNA. Translation: AAI10497.1 .
    BC110497 mRNA. Translation: AAI10498.1 .
    CCDSi CCDS14116.1. [Q02040-1 ]
    PIRi A46419.
    I54325.
    RefSeqi NP_005079.2. NM_005088.2. [Q02040-1 ]
    UniGenei Hs.522572.

    3D structure databases

    ProteinModelPortali Q02040.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113860. 7 interactions.
    IntActi Q02040. 4 interactions.
    MINTi MINT-1443812.

    PTM databases

    PhosphoSitei Q02040.

    Polymorphism databases

    DMDMi 146291102.

    Proteomic databases

    MaxQBi Q02040.
    PaxDbi Q02040.
    PRIDEi Q02040.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313871 ; ENSP00000324827 ; ENSG00000197976 . [Q02040-1 ]
    ENST00000474361 ; ENSP00000435479 ; ENSG00000197976 . [Q02040-2 ]
    GeneIDi 8227.
    KEGGi hsa:8227.
    UCSCi uc004cqa.3. human. [Q02040-1 ]
    uc010ncx.1. human. [Q02040-3 ]

    Organism-specific databases

    CTDi 8227.
    GeneCardsi GC0XP001710.
    HGNCi HGNC:18783. AKAP17A.
    HPAi HPA043247.
    MIMi 312095. gene.
    465000. gene.
    neXtProti NX_Q02040.
    PharmGKBi PA162402969.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271981.
    InParanoidi Q02040.
    KOi K13169.
    OMAi HNHQFST.
    OrthoDBi EOG7353WR.
    PhylomeDBi Q02040.
    TreeFami TF320443.

    Miscellaneous databases

    GeneWikii SFRS17A.
    GenomeRNAii 8227.
    NextBioi 30970.
    PROi Q02040.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q02040.
    CleanExi HS_SFRS17A.
    Genevestigatori Q02040.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of the human pseudoautosomal gene XE7."
      Ellison J.W., Ramos C., Yen P.H., Shapiro L.J.
      Hum. Mol. Genet. 1:691-696(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning and sequencing of a trophoblast-endothelial-activated lymphocyte surface protein: cDNA sequence and genomic structure."
      Voland J.R., Wyzykowski R.J., Huang M., Dutton R.W.
      Proc. Natl. Acad. Sci. U.S.A. 89:10425-10429(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT SER-194.
      Tissue: Blood.
    5. "Large-scale proteomic analysis of the human spliceosome."
      Rappsilber J., Ryder U., Lamond A.I., Mann M.
      Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH THE SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
    6. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "XE7: a novel splicing factor that interacts with ASF/SF2 and ZNF265."
      Mangs A.H., Speirs H.J.L., Goy C., Adams D.J., Markus M.A., Morris B.J.
      Nucleic Acids Res. 34:4976-4986(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZRANB2 AND SFRS1.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Splicing factor arginine/serine-rich 17A (SFRS17A) is an A-kinase anchoring protein that targets protein kinase A to splicing factor compartments."
      Jarnaess E., Stokka A.J., Kvissel A.K., Skalhegg B.S., Torgersen K.M., Scott J.D., Carlson C.R., Tasken K.
      J. Biol. Chem. 284:35154-35164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, MUTAGENESIS OF 438-LEU-LEU-439 AND 445-LYS-LYS-446.
    11. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537 AND SER-633, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAK17A_HUMAN
    AccessioniPrimary (citable) accession number: Q02040
    Secondary accession number(s): Q02832
    , Q2TB98, Q5JQ74, Q5JQ76, Q8N6U9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: May 1, 2007
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3