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Q96JB6

- LOXL4_HUMAN

UniProt

Q96JB6 - LOXL4_HUMAN

Protein

Lysyl oxidase homolog 4

Gene

LOXL4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    May modulate the formation of a collagenous extracellular matrix.

    Cofactori

    Copper.By similarity
    Contains 1 lysine tyrosylquinone.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi611 – 6111CopperSequence Analysis
    Metal bindingi613 – 6131CopperSequence Analysis
    Metal bindingi615 – 6151CopperSequence Analysis

    GO - Molecular functioni

    1. copper ion binding Source: InterPro
    2. protein binding Source: IntAct
    3. protein-lysine 6-oxidase activity Source: Ensembl
    4. scavenger receptor activity Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Copper, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_150206. Crosslinking of collagen fibrils.
    REACT_150366. Elastic fibre formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysyl oxidase homolog 4 (EC:1.4.3.-)
    Alternative name(s):
    Lysyl oxidase-like protein 4
    Lysyl oxidase-related protein C
    Gene namesi
    Name:LOXL4
    Synonyms:LOXC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:17171. LOXL4.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: InterPro
    4. receptor complex Source: MGI

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30431.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 756732Lysyl oxidase homolog 4PRO_0000018535Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi58 ↔ 122PROSITE-ProRule annotation
    Disulfide bondi71 ↔ 132PROSITE-ProRule annotation
    Disulfide bondi102 ↔ 112PROSITE-ProRule annotation
    Disulfide bondi191 ↔ 276PROSITE-ProRule annotation
    Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi204 ↔ 286PROSITE-ProRule annotation
    Disulfide bondi251 ↔ 261PROSITE-ProRule annotation
    Disulfide bondi336 ↔ 400PROSITE-ProRule annotation
    Disulfide bondi349 ↔ 410PROSITE-ProRule annotation
    Disulfide bondi380 ↔ 390PROSITE-ProRule annotation
    Disulfide bondi450 ↔ 515PROSITE-ProRule annotation
    Disulfide bondi463 ↔ 528PROSITE-ProRule annotation
    Disulfide bondi497 ↔ 507PROSITE-ProRule annotation
    Disulfide bondi558 ↔ 564PROSITE-ProRule annotation
    Disulfide bondi610 ↔ 658PROSITE-ProRule annotation
    Glycosylationi629 – 6291N-linked (GlcNAc...)Sequence Analysis
    Cross-linki638 ↔ 674Lysine tyrosylquinone (Lys-Tyr)By similarity
    Disulfide bondi642 ↔ 648PROSITE-ProRule annotation
    Disulfide bondi670 ↔ 680PROSITE-ProRule annotation
    Modified residuei674 – 67412',4',5'-topaquinoneBy similarity
    Disulfide bondi717 ↔ 731PROSITE-ProRule annotation

    Post-translational modificationi

    The lysine tyrosylquinone cross-link (LTQ) is generated by condensation of the epsilon-amino group of a lysine with a topaquinone produced by oxidation of tyrosine.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, LTQ, TPQ

    Proteomic databases

    MaxQBiQ96JB6.
    PaxDbiQ96JB6.
    PRIDEiQ96JB6.

    PTM databases

    PhosphoSiteiQ96JB6.

    Expressioni

    Tissue specificityi

    Expressed in many tissues, the highest levels among the tissues studied being in the skeletal muscle, testis and pancreas. Expressed in cartilage.

    Gene expression databases

    BgeeiQ96JB6.
    CleanExiHS_LOXL4.
    GenevestigatoriQ96JB6.

    Organism-specific databases

    HPAiCAB033876.
    HPA037609.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    KDM1AO603412EBI-749562,EBI-710124
    PRMT6Q96LA82EBI-749562,EBI-912440
    TRIP13Q156453EBI-749562,EBI-358993

    Protein-protein interaction databases

    BioGridi123925. 14 interactions.
    IntActiQ96JB6. 11 interactions.
    MINTiMINT-1448374.
    STRINGi9606.ENSP00000260702.

    Structurei

    3D structure databases

    ProteinModelPortaliQ96JB6.
    SMRiQ96JB6. Positions 311-410.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini32 – 133102SRCR 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini159 – 287129SRCR 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini311 – 411101SRCR 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini421 – 529109SRCR 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni533 – 736204Lysyl-oxidase likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the lysyl oxidase family.Curated
    Contains 4 SRCR domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG40770.
    HOGENOMiHOG000220841.
    HOVERGENiHBG052336.
    InParanoidiQ96JB6.
    KOiK00280.
    OMAiNCLSKSA.
    OrthoDBiEOG7SN8C6.
    PhylomeDBiQ96JB6.
    TreeFamiTF326061.

    Family and domain databases

    Gene3Di3.10.250.10. 4 hits.
    InterProiIPR001695. Lysyl_oxidase.
    IPR019828. Lysyl_oxidase_CS.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view]
    PfamiPF01186. Lysyl_oxidase. 1 hit.
    PF00530. SRCR. 4 hits.
    [Graphical view]
    PRINTSiPR00074. LYSYLOXIDASE.
    PR00258. SPERACTRCPTR.
    SMARTiSM00202. SR. 4 hits.
    [Graphical view]
    SUPFAMiSSF56487. SSF56487. 4 hits.
    PROSITEiPS00926. LYSYL_OXIDASE. 1 hit.
    PS00420. SRCR_1. 1 hit.
    PS50287. SRCR_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q96JB6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAWSPPATLF LFLLLLGQPP PSRPQSLGTT KLRLVGPESK PEEGRLEVLH    50
    QGQWGTVCDD NFAIQEATVA CRQLGFEAAL TWAHSAKYGQ GEGPIWLDNV 100
    RCVGTESSLD QCGSNGWGVS DCSHSEDVGV ICHPRRHRGY LSETVSNALG 150
    PQGRRLEEVR LKPILASAKQ HSPVTEGAVE VKYEGHWRQV CDQGWTMNNS 200
    RVVCGMLGFP SEVPVDSHYY RKVWDLKMRD PKSRLKSLTN KNSFWIHQVT 250
    CLGTEPHMAN CQVQVAPARG KLRPACPGGM HAVVSCVAGP HFRPPKTKPQ 300
    RKGSWAEEPR VRLRSGAQVG EGRVEVLMNR QWGTVCDHRW NLISASVVCR 350
    QLGFGSAREA LFGARLGQGL GPIHLSEVRC RGYERTLSDC PALEGSQNGC 400
    QHENDAAVRC NVPNMGFQNQ VRLAGGRIPE EGLLEVQVEV NGVPRWGSVC 450
    SENWGLTEAM VACRQLGLGF AIHAYKETWF WSGTPRAQEV VMSGVRCSGT 500
    ELALQQCQRH GPVHCSHGGG RFLAGVSCMD SAPDLVMNAQ LVQETAYLED 550
    RPLSQLYCAH EENCLSKSAD HMDWPYGYRR LLRFSTQIYN LGRTDFRPKT 600
    GRDSWVWHQC HRHYHSIEVF THYDLLTLNG SKVAEGHKAS FCLEDTNCPT 650
    GLQRRYACAN FGEQGVTVGC WDTYRHDIDC QWVDITDVGP GNYIFQVIVN 700
    PHYEVAESDF SNNMLQCRCK YDGHRVWLHN CHTGNSYPAN AELSLEQEQR 750
    LRNNLI 756
    Length:756
    Mass (Da):84,483
    Last modified:December 1, 2001 - v1
    Checksum:i13051ACADB922BBC
    GO

    Sequence cautioni

    The sequence AAH07522.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31W → R in AAH13153. (PubMed:15489334)Curated
    Sequence conflicti101 – 1011R → Q in AAH13153. (PubMed:15489334)Curated
    Sequence conflicti493 – 4931S → G in AAL27543. (PubMed:11691588)Curated
    Sequence conflicti539 – 5391A → T in AAL27543. (PubMed:11691588)Curated
    Sequence conflicti542 – 5421V → A in AAL27543. (PubMed:11691588)Curated
    Sequence conflicti703 – 7031Y → H in AAL27543. (PubMed:11691588)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti154 – 1541R → Q.
    Corresponds to variant rs33995374 [ dbSNP | Ensembl ].
    VAR_050012
    Natural varianti372 – 3721P → T.
    Corresponds to variant rs11189525 [ dbSNP | Ensembl ].
    VAR_059431
    Natural varianti405 – 4051D → A.1 Publication
    Corresponds to variant rs1983864 [ dbSNP | Ensembl ].
    VAR_050013

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF338441 mRNA. Translation: AAK71934.1.
    AY036093 mRNA. Translation: AAK64186.1.
    AF395336 mRNA. Translation: AAL27543.1.
    AK025542 mRNA. Translation: BAB15167.1.
    AK172781 mRNA. Translation: BAD18762.1.
    AL139241 Genomic DNA. Translation: CAH72819.1.
    CH471066 Genomic DNA. Translation: EAW49886.1.
    BC007522 mRNA. Translation: AAH07522.1. Different initiation.
    BC013153 mRNA. Translation: AAH13153.1.
    CCDSiCCDS7473.1.
    RefSeqiNP_115587.6. NM_032211.6.
    UniGeneiHs.306814.
    Hs.671890.

    Genome annotation databases

    EnsembliENST00000260702; ENSP00000260702; ENSG00000138131.
    GeneIDi84171.
    KEGGihsa:84171.
    UCSCiuc001kpa.1. human.

    Polymorphism databases

    DMDMi20177960.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF338441 mRNA. Translation: AAK71934.1 .
    AY036093 mRNA. Translation: AAK64186.1 .
    AF395336 mRNA. Translation: AAL27543.1 .
    AK025542 mRNA. Translation: BAB15167.1 .
    AK172781 mRNA. Translation: BAD18762.1 .
    AL139241 Genomic DNA. Translation: CAH72819.1 .
    CH471066 Genomic DNA. Translation: EAW49886.1 .
    BC007522 mRNA. Translation: AAH07522.1 . Different initiation.
    BC013153 mRNA. Translation: AAH13153.1 .
    CCDSi CCDS7473.1.
    RefSeqi NP_115587.6. NM_032211.6.
    UniGenei Hs.306814.
    Hs.671890.

    3D structure databases

    ProteinModelPortali Q96JB6.
    SMRi Q96JB6. Positions 311-410.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123925. 14 interactions.
    IntActi Q96JB6. 11 interactions.
    MINTi MINT-1448374.
    STRINGi 9606.ENSP00000260702.

    PTM databases

    PhosphoSitei Q96JB6.

    Polymorphism databases

    DMDMi 20177960.

    Proteomic databases

    MaxQBi Q96JB6.
    PaxDbi Q96JB6.
    PRIDEi Q96JB6.

    Protocols and materials databases

    DNASUi 84171.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260702 ; ENSP00000260702 ; ENSG00000138131 .
    GeneIDi 84171.
    KEGGi hsa:84171.
    UCSCi uc001kpa.1. human.

    Organism-specific databases

    CTDi 84171.
    GeneCardsi GC10M099997.
    HGNCi HGNC:17171. LOXL4.
    HPAi CAB033876.
    HPA037609.
    MIMi 607318. gene.
    neXtProti NX_Q96JB6.
    PharmGKBi PA30431.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40770.
    HOGENOMi HOG000220841.
    HOVERGENi HBG052336.
    InParanoidi Q96JB6.
    KOi K00280.
    OMAi NCLSKSA.
    OrthoDBi EOG7SN8C6.
    PhylomeDBi Q96JB6.
    TreeFami TF326061.

    Enzyme and pathway databases

    Reactomei REACT_150206. Crosslinking of collagen fibrils.
    REACT_150366. Elastic fibre formation.

    Miscellaneous databases

    ChiTaRSi LOXL4. human.
    GeneWikii LOXL4.
    GenomeRNAii 84171.
    NextBioi 73532.
    PROi Q96JB6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q96JB6.
    CleanExi HS_LOXL4.
    Genevestigatori Q96JB6.

    Family and domain databases

    Gene3Di 3.10.250.10. 4 hits.
    InterProi IPR001695. Lysyl_oxidase.
    IPR019828. Lysyl_oxidase_CS.
    IPR001190. SRCR.
    IPR017448. SRCR-like_dom.
    [Graphical view ]
    Pfami PF01186. Lysyl_oxidase. 1 hit.
    PF00530. SRCR. 4 hits.
    [Graphical view ]
    PRINTSi PR00074. LYSYLOXIDASE.
    PR00258. SPERACTRCPTR.
    SMARTi SM00202. SR. 4 hits.
    [Graphical view ]
    SUPFAMi SSF56487. SSF56487. 4 hits.
    PROSITEi PS00926. LYSYL_OXIDASE. 1 hit.
    PS00420. SRCR_1. 1 hit.
    PS50287. SRCR_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and biological activity of a novel lysyl oxidase-related gene expressed in cartilage."
      Ito H., Akiyama H., Iguchi H., Iyama K., Miyamoto M., Ohsawa K., Nakamura T.
      J. Biol. Chem. 276:24023-24029(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Testis.
    2. "Cloning and characterization of a fifth human lysyl oxidase isoenzyme: the third member of the lysyl oxidase-related subfamily with four scavenger receptor cysteine-rich domains."
      Maeki J.M., Tikkanen H., Kivirikko K.I.
      Matrix Biol. 20:493-496(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "A novel human lysyl oxidase-like gene (LOXL4) on chromosome 10q24 has an altered scavenger receptor cysteine rich domain."
      Asuncion L., Fogelgren B., Fong K.S.K., Fong S.F.T., Kim Y., Csiszar K.
      Matrix Biol. 20:487-491(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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], VARIANT ALA-405.
      Tissue: Eye.

    Entry informationi

    Entry nameiLOXL4_HUMAN
    AccessioniPrimary (citable) accession number: Q96JB6
    Secondary accession number(s): Q5W0B3
    , Q96DY1, Q96PC0, Q9H6T5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 16, 2002
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: 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