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Q14520

- HABP2_HUMAN

UniProt

Q14520 - HABP2_HUMAN

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Protein
Hyaluronan-binding protein 2
Gene
HABP2, HGFAL, PHBP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 1702Cleavage By similarity
Sitei170 – 1712Cleavage By similarity
Active sitei362 – 3621Charge relay system By similarity
Active sitei411 – 4111Charge relay system By similarity
Sitei480 – 4812Cleavage By similarity
Active sitei509 – 5091Charge relay system By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. cell adhesion Source: ProtInc
Complete GO annotation...

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

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29172.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 Publication
Add
BLAST
Chaini24 – 313290Hyaluronan-binding protein 2 50 kDa heavy chain
PRO_0000027899Add
BLAST
Chaini27 – 313287Hyaluronan-binding protein 2 50 kDa heavy chain alternate form By similarity
PRO_0000027900Add
BLAST
Chaini314 – 560247Hyaluronan-binding protein 2 27 kDa light chain
PRO_0000027901Add
BLAST
Chaini320 – 560241Hyaluronan-binding protein 2 27 kDa light chain alternate form By similarity
PRO_0000027902Add
BLAST

Amino acid modifications

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

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.

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ14520.
SMRiQ14520. Positions 30-556.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 10937EGF-like 1
Add
BLAST
Domaini111 – 14838EGF-like 2
Add
BLAST
Domaini150 – 18839EGF-like 3
Add
BLAST
Domaini193 – 27684Kringle
Add
BLAST
Domaini314 – 555242Peptidase S1
Add
BLAST

Sequence similaritiesi

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

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

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.
VSP_044583Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571N → S in BAH14081. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 135 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

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