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Q14520

- HABP2_HUMAN

UniProt

Q14520 - HABP2_HUMAN

Protein

Hyaluronan-binding protein 2

Gene

HABP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Cleaves the alpha-chain at multiple sites and the beta-chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro-urokinase) to the active two chain form. Activates coagulation factor VII.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei169 – 1702CleavageBy similarity
    Sitei170 – 1712CleavageBy similarity
    Active sitei362 – 3621Charge relay systemBy similarity
    Active sitei411 – 4111Charge relay systemBy similarity
    Sitei480 – 4812CleavageBy similarity
    Active sitei509 – 5091Charge relay systemBy similarity

    GO - Molecular functioni

    1. glycosaminoglycan binding Source: ProtInc
    2. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. cell adhesion Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    SABIO-RKQ14520.

    Protein family/group databases

    MEROPSiS01.033.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hyaluronan-binding protein 2 (EC:3.4.21.-)
    Alternative name(s):
    Factor VII-activating protease
    Factor seven-activating protease
    Short name:
    FSAP
    Hepatocyte growth factor activator-like protein
    Plasma hyaluronan-binding protein
    Cleaved into the following 4 chains:
    Gene namesi
    Name:HABP2
    Synonyms:HGFAL, PHBP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:4798. HABP2.

    Subcellular locationi

    Secreted 1 Publication
    Note: Secreted as an inactive single-chain precursor and is then activated to a heterodimeric form.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29172.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23231 PublicationAdd
    BLAST
    Chaini24 – 313290Hyaluronan-binding protein 2 50 kDa heavy chainPRO_0000027899Add
    BLAST
    Chaini27 – 313287Hyaluronan-binding protein 2 50 kDa heavy chain alternate formBy similarityPRO_0000027900Add
    BLAST
    Chaini314 – 560247Hyaluronan-binding protein 2 27 kDa light chainPRO_0000027901Add
    BLAST
    Chaini320 – 560241Hyaluronan-binding protein 2 27 kDa light chain alternate formBy similarityPRO_0000027902Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi54 – 541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi77 ↔ 88By similarity
    Disulfide bondi82 ↔ 97By similarity
    Disulfide bondi99 ↔ 108By similarity
    Disulfide bondi115 ↔ 125By similarity
    Disulfide bondi120 ↔ 136By similarity
    Disulfide bondi138 ↔ 147By similarity
    Disulfide bondi154 ↔ 165By similarity
    Disulfide bondi159 ↔ 176By similarity
    Disulfide bondi178 ↔ 187By similarity
    Disulfide bondi194 ↔ 276By similarity
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi215 ↔ 257By similarity
    Disulfide bondi246 ↔ 271By similarity
    Disulfide bondi301 ↔ 435Interchain (between heavy and light chains)PROSITE-ProRule annotation
    Disulfide bondi347 ↔ 363By similarity
    Disulfide bondi447 ↔ 515By similarity
    Disulfide bondi477 ↔ 493By similarity
    Disulfide bondi505 ↔ 533By similarity

    Post-translational modificationi

    Proteolytic cleavage at Gly-23 or Met-27 can give rise to the 50 kDa heavy chain and cleavage at Arg-313 or Lys-319 can give rise to the 27 kDa light chain. The heavy chain can undergo further proteolytic cleavage at Lys-169 or Arg-170 to give rise to 2 inactive 26 kDa fragments and the light chain can undergo further proteolytic cleavage at Arg-480 to give rise to inactive 17 kDa and 8 kDa fragments By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ14520.
    PaxDbiQ14520.
    PeptideAtlasiQ14520.
    PRIDEiQ14520.

    PTM databases

    PhosphoSiteiQ14520.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ14520.
    BgeeiQ14520.
    CleanExiHS_HABP2.
    GenevestigatoriQ14520.

    Organism-specific databases

    HPAiHPA019518.

    Interactioni

    Subunit structurei

    Heterodimer; disulfide-linked. Heterodimer of a 50 kDa heavy and a 27 kDa light chain linked by a disulfide bond By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ14520. 1 interaction.
    MINTiMINT-8201767.
    STRINGi9606.ENSP00000277903.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14520.
    SMRiQ14520. Positions 30-556.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini73 – 10937EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini111 – 14838EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini150 – 18839EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini193 – 27684KringlePROSITE-ProRule annotationAdd
    BLAST
    Domaini314 – 555242Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 3 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 kringle domain.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Kringle, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG5640.
    HOGENOMiHOG000237314.
    HOVERGENiHBG106385.
    InParanoidiQ14520.
    KOiK08648.
    OMAiYWNSHLL.
    OrthoDBiEOG75B84T.
    PhylomeDBiQ14520.
    TreeFamiTF329901.

    Family and domain databases

    Gene3Di2.40.20.10. 1 hit.
    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view]
    PfamiPF00008. EGF. 2 hits.
    PF00051. Kringle. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view]
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00181. EGF. 3 hits.
    SM00130. KR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 1 hit.
    PROSITEiPS00022. EGF_1. 3 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 3 hits.
    PS00021. KRINGLE_1. 1 hit.
    PS50070. KRINGLE_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14520-1) [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

    MFARMSDLHV LLLMALVGKT ACGFSLMSLL ESLDPDWTPD QYDYSYEDYN    50
    QEENTSSTLT HAENPDWYYT EDQADPCQPN PCEHGGDCLV HGSTFTCSCL 100
    APFSGNKCQK VQNTCKDNPC GRGQCLITQS PPYYRCVCKH PYTGPSCSQV 150
    VPVCRPNPCQ NGATCSRHKR RSKFTCACPD QFKGKFCEIG SDDCYVGDGY 200
    SYRGKMNRTV NQHACLYWNS HLLLQENYNM FMEDAETHGI GEHNFCRNPD 250
    ADEKPWCFIK VTNDKVKWEY CDVSACSAQD VAYPEESPTE PSTKLPGFDS 300
    CGKTEIAERK IKRIYGGFKS TAGKHPWQAS LQSSLPLTIS MPQGHFCGGA 350
    LIHPCWVLTA AHCTDIKTRH LKVVLGDQDL KKEEFHEQSF RVEKIFKYSH 400
    YNERDEIPHN DIALLKLKPV DGHCALESKY VKTVCLPDGS FPSGSECHIS 450
    GWGVTETGKG SRQLLDAKVK LIANTLCNSR QLYDHMIDDS MICAGNLQKP 500
    GQDTCQGDSG GPLTCEKDGT YYVYGIVSWG LECGKRPGVY TQVTKFLNWI 550
    KATIKSESGF 560
    Length:560
    Mass (Da):62,672
    Last modified:November 1, 1996 - v1
    Checksum:i5C1907230784ACD4
    GO
    Isoform 2 (identifier: Q14520-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:534
    Mass (Da):59,864
    Checksum:i7C085D18333DC859
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti157 – 1571N → S in BAH14081. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti90 – 901V → I.1 Publication
    Corresponds to variant rs11575750 [ dbSNP | Ensembl ].
    VAR_023399
    Natural varianti393 – 3931E → Q in Marburg II polymorphism. 2 Publications
    Corresponds to variant rs11575688 [ dbSNP | Ensembl ].
    VAR_023400
    Natural varianti534 – 5341G → E in Marburg I polymorphism; impairs the pro-urokinase activating potency; could be a prominent risk predictor of carotid stenosis. 2 Publications
    Corresponds to variant rs7080536 [ dbSNP | Ensembl ].
    VAR_023401

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626Missing in isoform 2. 1 PublicationVSP_044583Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S83182 mRNA. Translation: AAB46909.1.
    D49742 mRNA. Translation: BAA08576.1.
    AY534754 Genomic DNA. Translation: AAS16352.1.
    AK290832 mRNA. Translation: BAF83521.1.
    AK303948 mRNA. Translation: BAH14081.1.
    AL390197 Genomic DNA. Translation: CAH71108.1.
    CH471066 Genomic DNA. Translation: EAW49505.1.
    BC031412 mRNA. Translation: AAH31412.1.
    CCDSiCCDS53579.1. [Q14520-2]
    CCDS7577.1. [Q14520-1]
    PIRiJC4795.
    RefSeqiNP_001171131.1. NM_001177660.1. [Q14520-2]
    NP_004123.1. NM_004132.3. [Q14520-1]
    UniGeneiHs.422542.

    Genome annotation databases

    EnsembliENST00000351270; ENSP00000277903; ENSG00000148702. [Q14520-1]
    ENST00000542051; ENSP00000443283; ENSG00000148702. [Q14520-2]
    GeneIDi3026.
    KEGGihsa:3026.
    UCSCiuc001lai.4. human. [Q14520-1]

    Polymorphism databases

    DMDMi73919921.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S83182 mRNA. Translation: AAB46909.1 .
    D49742 mRNA. Translation: BAA08576.1 .
    AY534754 Genomic DNA. Translation: AAS16352.1 .
    AK290832 mRNA. Translation: BAF83521.1 .
    AK303948 mRNA. Translation: BAH14081.1 .
    AL390197 Genomic DNA. Translation: CAH71108.1 .
    CH471066 Genomic DNA. Translation: EAW49505.1 .
    BC031412 mRNA. Translation: AAH31412.1 .
    CCDSi CCDS53579.1. [Q14520-2 ]
    CCDS7577.1. [Q14520-1 ]
    PIRi JC4795.
    RefSeqi NP_001171131.1. NM_001177660.1. [Q14520-2 ]
    NP_004123.1. NM_004132.3. [Q14520-1 ]
    UniGenei Hs.422542.

    3D structure databases

    ProteinModelPortali Q14520.
    SMRi Q14520. Positions 30-556.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q14520. 1 interaction.
    MINTi MINT-8201767.
    STRINGi 9606.ENSP00000277903.

    Protein family/group databases

    MEROPSi S01.033.

    PTM databases

    PhosphoSitei Q14520.

    Polymorphism databases

    DMDMi 73919921.

    Proteomic databases

    MaxQBi Q14520.
    PaxDbi Q14520.
    PeptideAtlasi Q14520.
    PRIDEi Q14520.

    Protocols and materials databases

    DNASUi 3026.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351270 ; ENSP00000277903 ; ENSG00000148702 . [Q14520-1 ]
    ENST00000542051 ; ENSP00000443283 ; ENSG00000148702 . [Q14520-2 ]
    GeneIDi 3026.
    KEGGi hsa:3026.
    UCSCi uc001lai.4. human. [Q14520-1 ]

    Organism-specific databases

    CTDi 3026.
    GeneCardsi GC10P115302.
    HGNCi HGNC:4798. HABP2.
    HPAi HPA019518.
    MIMi 603924. gene.
    neXtProti NX_Q14520.
    PharmGKBi PA29172.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOGENOMi HOG000237314.
    HOVERGENi HBG106385.
    InParanoidi Q14520.
    KOi K08648.
    OMAi YWNSHLL.
    OrthoDBi EOG75B84T.
    PhylomeDBi Q14520.
    TreeFami TF329901.

    Enzyme and pathway databases

    SABIO-RK Q14520.

    Miscellaneous databases

    GeneWikii HABP2.
    GenomeRNAii 3026.
    NextBioi 11980.
    PROi Q14520.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14520.
    Bgeei Q14520.
    CleanExi HS_HABP2.
    Genevestigatori Q14520.

    Family and domain databases

    Gene3Di 2.40.20.10. 1 hit.
    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR000001. Kringle.
    IPR013806. Kringle-like.
    IPR018056. Kringle_CS.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR009003. Trypsin-like_Pept_dom.
    [Graphical view ]
    Pfami PF00008. EGF. 2 hits.
    PF00051. Kringle. 1 hit.
    PF00089. Trypsin. 1 hit.
    [Graphical view ]
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00181. EGF. 3 hits.
    SM00130. KR. 1 hit.
    SM00020. Tryp_SPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF57440. SSF57440. 1 hit.
    PROSITEi PS00022. EGF_1. 3 hits.
    PS01186. EGF_2. 2 hits.
    PS50026. EGF_3. 3 hits.
    PS00021. KRINGLE_1. 1 hit.
    PS50070. KRINGLE_2. 1 hit.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Purification and characterization of a novel hyaluronan-binding protein (PHBP) from human plasma: it has three EGF, a kringle and a serine protease domain, similar to hepatocyte growth factor activator."
      Choi-Miura N.-H., Tobe T., Sumiya J., Nakano Y., Sano Y., Mazda T., Tomita M.
      J. Biochem. 119:1157-1165(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 24-42; 140-169; 174-183; 206-235; 255-260; 314-334; 417-429; 433-459; 500-517 AND 546-551, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Plasma.
    2. Kitamura N.
      Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. SeattleSNPs variation discovery resource
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-90; GLN-393 AND GLU-534.
    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] (ISOFORMS 1 AND 2).
      Tissue: Liver and Trachea.
    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] (ISOFORM 1).
      Tissue: Colon.
    8. "The FVII activating protease cleaves single-chain plasminogen activators."
      Roemisch J., Vermoehlen S., Feussner A., Stoehr H.-A.
      Haemostasis 29:292-299(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Identification of the substrates for plasma hyaluronan binding protein."
      Choi-Miura N.H., Yoda M., Saito K., Takahashi K., Tomita M.
      Biol. Pharm. Bull. 24:140-143(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Marburg I polymorphism of factor VII-activating protease: a prominent risk predictor of carotid stenosis."
      Willeit J., Kiechl S., Weimer T., Mair A., Santer P., Wiedermann C.J., Roemisch J.
      Circulation 107:667-670(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GLN-393 AND GLU-534.

    Entry informationi

    Entry nameiHABP2_HUMAN
    AccessioniPrimary (citable) accession number: Q14520
    Secondary accession number(s): A8K467
    , B7Z8U5, F5H5M6, O00663
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 136 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, Direct protein sequencing, 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3