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Q14520 (HABP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:HABP2
Synonyms:HGFAL, PHBP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length560 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.9

Subunit structure

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

Subcellular location

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

Tissue specificity

Ubiquitously expressed. Ref.1

Post-translational modification

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.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 3 EGF-like domains.

Contains 1 kringle domain.

Contains 1 peptidase S1 domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14520-1)

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.
Isoform 2 (identifier: Q14520-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.1
Chain24 – 313290Hyaluronan-binding protein 2 50 kDa heavy chain
PRO_0000027899
Chain27 – 313287Hyaluronan-binding protein 2 50 kDa heavy chain alternate form By similarity
PRO_0000027900
Chain314 – 560247Hyaluronan-binding protein 2 27 kDa light chain
PRO_0000027901
Chain320 – 560241Hyaluronan-binding protein 2 27 kDa light chain alternate form By similarity
PRO_0000027902

Regions

Domain73 – 10937EGF-like 1
Domain111 – 14838EGF-like 2
Domain150 – 18839EGF-like 3
Domain193 – 27684Kringle
Domain314 – 555242Peptidase S1

Sites

Active site3621Charge relay system By similarity
Active site4111Charge relay system By similarity
Active site5091Charge relay system By similarity
Site169 – 1702Cleavage By similarity
Site170 – 1712Cleavage By similarity
Site480 – 4812Cleavage By similarity

Amino acid modifications

Glycosylation541N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Disulfide bond77 ↔ 88 By similarity
Disulfide bond82 ↔ 97 By similarity
Disulfide bond99 ↔ 108 By similarity
Disulfide bond115 ↔ 125 By similarity
Disulfide bond120 ↔ 136 By similarity
Disulfide bond138 ↔ 147 By similarity
Disulfide bond154 ↔ 165 By similarity
Disulfide bond159 ↔ 176 By similarity
Disulfide bond178 ↔ 187 By similarity
Disulfide bond194 ↔ 276 By similarity
Disulfide bond215 ↔ 257 By similarity
Disulfide bond246 ↔ 271 By similarity
Disulfide bond301 ↔ 435Interchain (between heavy and light chains) By similarity
Disulfide bond347 ↔ 363 By similarity
Disulfide bond447 ↔ 515 By similarity
Disulfide bond477 ↔ 493 By similarity
Disulfide bond505 ↔ 533 By similarity

Natural variations

Alternative sequence1 – 2626Missing in isoform 2.
VSP_044583
Natural variant901V → I. Ref.3
Corresponds to variant rs11575750 [ dbSNP | Ensembl ].
VAR_023399
Natural variant3931E → Q in Marburg II polymorphism. Ref.3 Ref.10
Corresponds to variant rs11575688 [ dbSNP | Ensembl ].
VAR_023400
Natural variant5341G → E in Marburg I polymorphism; impairs the pro-urokinase activating potency; could be a prominent risk predictor of carotid stenosis. Ref.3 Ref.10
Corresponds to variant rs7080536 [ dbSNP | Ensembl ].
VAR_023401

Experimental info

Sequence conflict1571N → S in BAH14081. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 5C1907230784ACD4

FASTA56062,672
        10         20         30         40         50         60 
MFARMSDLHV LLLMALVGKT ACGFSLMSLL ESLDPDWTPD QYDYSYEDYN QEENTSSTLT 

        70         80         90        100        110        120 
HAENPDWYYT EDQADPCQPN PCEHGGDCLV HGSTFTCSCL APFSGNKCQK VQNTCKDNPC 

       130        140        150        160        170        180 
GRGQCLITQS PPYYRCVCKH PYTGPSCSQV VPVCRPNPCQ NGATCSRHKR RSKFTCACPD 

       190        200        210        220        230        240 
QFKGKFCEIG SDDCYVGDGY SYRGKMNRTV NQHACLYWNS HLLLQENYNM FMEDAETHGI 

       250        260        270        280        290        300 
GEHNFCRNPD ADEKPWCFIK VTNDKVKWEY CDVSACSAQD VAYPEESPTE PSTKLPGFDS 

       310        320        330        340        350        360 
CGKTEIAERK IKRIYGGFKS TAGKHPWQAS LQSSLPLTIS MPQGHFCGGA LIHPCWVLTA 

       370        380        390        400        410        420 
AHCTDIKTRH LKVVLGDQDL KKEEFHEQSF RVEKIFKYSH YNERDEIPHN DIALLKLKPV 

       430        440        450        460        470        480 
DGHCALESKY VKTVCLPDGS FPSGSECHIS GWGVTETGKG SRQLLDAKVK LIANTLCNSR 

       490        500        510        520        530        540 
QLYDHMIDDS MICAGNLQKP GQDTCQGDSG GPLTCEKDGT YYVYGIVSWG LECGKRPGVY 

       550        560 
TQVTKFLNWI KATIKSESGF 

« Hide

Isoform 2 [UniParc].

Checksum: 7C085D18333DC859
Show »

FASTA53459,864

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS53579.1. [Q14520-2]
CCDS7577.1. [Q14520-1]
PIRJC4795.
RefSeqNP_001171131.1. NM_001177660.1. [Q14520-2]
NP_004123.1. NM_004132.3. [Q14520-1]
UniGeneHs.422542.

3D structure databases

ProteinModelPortalQ14520.
SMRQ14520. Positions 30-556.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ14520. 1 interaction.
MINTMINT-8201767.
STRING9606.ENSP00000277903.

Protein family/group databases

MEROPSS01.033.

PTM databases

PhosphoSiteQ14520.

Polymorphism databases

DMDM73919921.

Proteomic databases

MaxQBQ14520.
PaxDbQ14520.
PeptideAtlasQ14520.
PRIDEQ14520.

Protocols and materials databases

DNASU3026.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000351270; ENSP00000277903; ENSG00000148702. [Q14520-1]
ENST00000542051; ENSP00000443283; ENSG00000148702. [Q14520-2]
GeneID3026.
KEGGhsa:3026.
UCSCuc001lai.4. human. [Q14520-1]

Organism-specific databases

CTD3026.
GeneCardsGC10P115302.
HGNCHGNC:4798. HABP2.
HPAHPA019518.
MIM603924. gene.
neXtProtNX_Q14520.
PharmGKBPA29172.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000237314.
HOVERGENHBG106385.
InParanoidQ14520.
KOK08648.
OMAYWNSHLL.
OrthoDBEOG75B84T.
PhylomeDBQ14520.
TreeFamTF329901.

Enzyme and pathway databases

SABIO-RKQ14520.

Gene expression databases

ArrayExpressQ14520.
BgeeQ14520.
CleanExHS_HABP2.
GenevestigatorQ14520.

Family and domain databases

Gene3D2.40.20.10. 1 hit.
InterProIPR000742. 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]
PfamPF00008. EGF. 2 hits.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00181. EGF. 3 hits.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 1 hit.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

GeneWikiHABP2.
GenomeRNAi3026.
NextBio11980.
PROQ14520.
SOURCESearch...

Entry information

Entry nameHABP2_HUMAN
AccessionPrimary (citable) accession number: Q14520
Secondary accession number(s): A8K467 expand/collapse secondary AC list , B7Z8U5, F5H5M6, O00663
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM