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Q9HBI1 (PARVB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 121. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Beta-parvin
Alternative name(s):
Affixin
Gene names
Name:PARVB
ORF Names:CGI-56
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Ref.2 Ref.11 Ref.12 Ref.13 Ref.15

Subunit structure

Interacts with DYSF. Interacts with ILK, ARHGEF6, PXN (via LD motifs), ACTN2 and actin. Ref.2 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.19

Subcellular location

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. Cell projectionlamellipodium. Cytoplasmmyofibrilsarcomere. CytoplasmmyofibrilsarcomereZ line. Note: Constituent of focal adhesions. Detected at the tips of the leading edge of cells. Colocalizes with F-actin at the tips of lamellipodia. Ref.2 Ref.13 Ref.15 Ref.19

Tissue specificity

Expressed predominantly in heart and skeletal muscle. Ref.2 Ref.10

Sequence similarities

Belongs to the parvin family.

Contains 2 CH (calponin-homology) domains.

Sequence caution

The sequence AAD34051.1 differs from that shown. Reason: Frameshift at positions 4, 14, 48, 58, 155, 162, 171, 327, 331 and 344.

The sequence BG743702 differs from that shown. Reason: Frameshift at positions 136, 232 and 237.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Arhgef6Q8K4I33EBI-1047679,EBI-6272809From a different organism.
Arhgef7Q9ES2810EBI-1047679,EBI-642580From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HBI1-1)

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: Q9HBI1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MSSAPRSPTP...TLARKRRARE → MHHVFKDHQR...VETSEYAQGG
Note: Ref.1 (AAL08219) sequence is in conflict in positions: 21:N->K and 37:W->R.
Isoform 3 (identifier: Q9HBI1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MSSAPRSPTPRPRRMKKDESFLGKLGGTLARKRRAREV → M
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 364364Beta-parvin
PRO_0000121583

Regions

Domain87 – 194108CH 1
Domain254 – 361108CH 2

Amino acid modifications

Modified residue541Phosphoserine Ref.16

Natural variations

Alternative sequence1 – 3838MSSAP…RAREV → M in isoform 3.
VSP_045555
Alternative sequence1 – 3737MSSAP…RRARE → MHHVFKDHQRGEKRGFLSPE NKNCRRLELRRGCSCSWGLC SQALMASLAGSLLPGSDRSG VETSEYAQGG in isoform 2.
VSP_041336
Natural variant521P → R.
Corresponds to variant rs34476853 [ dbSNP | Ensembl ].
VAR_034369
Natural variant581V → A. Ref.1 Ref.5 Ref.8 Ref.16
Corresponds to variant rs1983609 [ dbSNP | Ensembl ].
VAR_017242

Experimental info

Mutagenesis2561V → Q: Abolishes interaction with PXN. Ref.19
Mutagenesis2991F → D: Abolishes interaction with ILK. Abolishes location at focal adhesion sites. Ref.19
Sequence conflict271G → V in AAD34051. Ref.4
Sequence conflict591D → M in AAD34051. Ref.4
Sequence conflict3491T → P in AAD34051. Ref.4
Isoform 2:
Sequence conflict41V → G in BG743702. Ref.8

Secondary structure

.................... 364
Helix Strand Turn

Details...

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: 4BA4B50C83083DC7

FASTA36441,714
        10         20         30         40         50         60 
MSSAPRSPTP RPRRMKKDES FLGKLGGTLA RKRRAREVSD LQEEGKNAIN SPMSPALVDV 

        70         80         90        100        110        120 
HPEDTQLEEN EERTMIDPTS KEDPKFKELV KVLLDWINDV LVEERIIVKQ LEEDLYDGQV 

       130        140        150        160        170        180 
LQKLLEKLAG CKLNVAEVTQ SEIGQKQKLQ TVLEAVHDLL RPRGWALRWS VDSIHGKNLV 

       190        200        210        220        230        240 
AILHLLVSLA MHFRAPIRLP EHVTVQVVVV RKREGLLHSS HISEELTTTT EMMMGRFERD 

       250        260        270        280        290        300 
AFDTLFDHAP DKLSVVKKSL ITFVNKHLNK LNLEVTELET QFADGVYLVL LMGLLEDYFV 

       310        320        330        340        350        360 
PLHHFYLTPE SFDQKVHNVS FAFELMLDGG LKKPKARPED VVNLDLKSTL RVLYNLFTKY 


KNVE 

« Hide

Isoform 2 [UniParc].

Checksum: BA4335437824E465
Show »

FASTA39745,183
Isoform 3 [UniParc].

Checksum: BD4A2F8D5ECD7768
Show »

FASTA32737,538

References

« Hide 'large scale' references
[1]"CLINT, Calponin homology domain protein binding to integrin-linked kinase, ILK1."
Carnio L., Hannigan G.E.
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT ALA-58.
Tissue: Skeletal muscle.
[2]"A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction."
Yamaji S., Suzuki A., Sugiyama Y., Koide Y., Yoshida M., Kanamori H., Mohri H., Ohno S., Ishigatsubo Y.
J. Cell Biol. 153:1251-1264(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ILK, SUBCELLULAR LOCATION, PHOSPHORYLATION, TISSUE SPECIFICITY.
[3]"Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily."
Olski T.M., Noegel A.A., Korenbaum E.
J. Cell Sci. 114:525-538(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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] (ISOFORM 1), VARIANT ALA-58.
Tissue: Colon.
[6]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-238 (ISOFORM 2), VARIANT ALA-58.
Tissue: Brain, Leukocyte and Skin.
[9]"Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-364 (ISOFORM 1).
[10]"Genomic organization and expression profile of the parvin family of focal adhesion proteins in mice and humans."
Korenbaum E., Olski T.M., Noegel A.A.
Gene 279:69-79(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"The first CH domain of affixin activates Cdc42 and Rac1 through alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging factor."
Mishima W., Suzuki A., Yamaji S., Yoshimi R., Ueda A., Kaneko T., Tanaka J., Miwa Y., Ohno S., Ishigatsubo Y.
Genes Cells 9:193-204(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARHGEF6.
[12]"Distinct roles of two structurally closely related focal adhesion proteins, alpha-parvins and beta-parvins, in regulation of cell morphology and survival."
Zhang Y., Chen K., Tu Y., Wu C.
J. Biol. Chem. 279:41695-41705(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ILK.
[13]"Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction."
Yamaji S., Suzuki A., Kanamori H., Mishima W., Yoshimi R., Takasaki H., Takabayashi M., Fujimaki K., Fujisawa S., Ohno S., Ishigatsubo Y.
J. Cell Biol. 165:539-551(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ACTN2, SUBCELLULAR LOCATION, FUNCTION.
[14]"Dysferlin interacts with affixin (beta-parvin) at the sarcolemma."
Matsuda C., Kameyama K., Tagawa K., Ogawa M., Suzuki A., Yamaji S., Okamoto H., Nishino I., Hayashi Y.K.
J. Neuropathol. Exp. Neurol. 64:334-340(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYSF.
[15]"Affixin activates Rac1 via betaPIX in C2C12 myoblast."
Matsuda C., Kameyama K., Suzuki A., Mishima W., Yamaji S., Okamoto H., Nishino I., Hayashi Y.K.
FEBS Lett. 582:1189-1196(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARHGEF6 AND ARHGEF7.
[16]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, VARIANT [LARGE SCALE ANALYSIS] ALA-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"Structural basis for paxillin binding and focal adhesion targeting of beta-parvin."
Stiegler A.L., Draheim K.M., Li X., Chayen N.E., Calderwood D.A., Boggon T.J.
J. Biol. Chem. 287:32566-32577(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 235-364 IN COMPLEX WITH PXN, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-256 AND PHE-299, INTERACTION WITH ILK AND PXN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF303887 mRNA. Translation: AAL08219.1.
AB048276 mRNA. Translation: BAB62077.1.
AF237769 mRNA. Translation: AAG27171.1.
AF151814 mRNA. Translation: AAD34051.1. Frameshift.
AK313957 mRNA. Translation: BAG36673.1.
AL031595, AL033543, Z82178 Genomic DNA. Translation: CAI22312.1.
AL033543, AL031595, Z82178 Genomic DNA. Translation: CAI17969.1.
Z82178, AL031595, AL033543 Genomic DNA. Translation: CAI18767.1.
AL033543, AL031595, Z82174 Genomic DNA. Translation: CAQ06491.1.
AL033543, AL031595, AL035398 Genomic DNA. Translation: CAQ06493.1.
AL031595, AL033543, Z82174 Genomic DNA. Translation: CAQ08141.1.
AL031595, AL033543, AL035398 Genomic DNA. Translation: CAQ08144.1.
Z82174, AL031595, AL033543 Genomic DNA. Translation: CAQ08662.1.
AL035398, AL031595, AL033543 Genomic DNA. Translation: CAQ09485.1.
CH471138 Genomic DNA. Translation: EAW73328.1.
BC039811 mRNA. No translation available.
BC046103 mRNA. Translation: AAH46103.2.
BG743702 mRNA. No translation available.
AL159142 mRNA. Translation: CAB76900.1.
RefSeqNP_001003828.1. NM_001003828.2.
NP_001230314.1. NM_001243385.1.
NP_001230315.1. NM_001243386.1.
NP_037459.2. NM_013327.4.
XP_005261650.1. XM_005261593.1.
XP_005261651.1. XM_005261594.1.
XP_005261652.1. XM_005261595.1.
UniGeneHs.475074.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4EDLX-ray2.10A/B/C/D/E/F235-364[»]
4EDMX-ray2.00A/B235-364[»]
4EDNX-ray2.90A/B/C/D/E/F/G/H/I/J235-364[»]
ProteinModelPortalQ9HBI1.
SMRQ9HBI1. Positions 90-196, 235-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118912. 3 interactions.
IntActQ9HBI1. 7 interactions.
MINTMINT-6178745.

PTM databases

PhosphoSiteQ9HBI1.

Polymorphism databases

DMDM20139178.

Proteomic databases

PaxDbQ9HBI1.
PRIDEQ9HBI1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338758; ENSP00000342492; ENSG00000188677. [Q9HBI1-1]
ENST00000404989; ENSP00000384353; ENSG00000188677. [Q9HBI1-3]
ENST00000406477; ENSP00000384515; ENSG00000188677. [Q9HBI1-2]
GeneID29780.
KEGGhsa:29780.
UCSCuc003bem.3. human. [Q9HBI1-2]
uc003ben.3. human. [Q9HBI1-1]
uc003beo.3. human.

Organism-specific databases

CTD29780.
GeneCardsGC22P044395.
HGNCHGNC:14653. PARVB.
MIM608121. gene.
neXtProtNX_Q9HBI1.
PharmGKBPA32951.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303418.
HOVERGENHBG053517.
KOK06275.
OMANLFTNYK.
OrthoDBEOG70KGPW.
PhylomeDBQ9HBI1.
TreeFamTF314025.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpressQ9HBI1.
BgeeQ9HBI1.
CleanExHS_PARVB.
GenevestigatorQ9HBI1.

Family and domain databases

Gene3D1.10.418.10. 2 hits.
InterProIPR001715. CH-domain.
IPR028433. Parvin.
[Graphical view]
PANTHERPTHR12114. PTHR12114. 1 hit.
PfamPF00307. CH. 2 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 2 hits.
PROSITEPS50021. CH. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPARVB.
GenomeRNAi29780.
NextBio52306.
PROQ9HBI1.
SOURCESearch...

Entry information

Entry namePARVB_HUMAN
AccessionPrimary (citable) accession number: Q9HBI1
Secondary accession number(s): B0QYM8 expand/collapse secondary AC list , B0QYN1, B2R9X6, Q5TGJ5, Q86X93, Q96PN1, Q9NSP7, Q9UGT3, Q9Y368, Q9Y3L6, Q9Y3L7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 121 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 22

Human chromosome 22: entries, gene names and cross-references to MIM