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Protein

Beta-parvin

Gene

PARVB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. cell adhesion Source: UniProtKB-KW
  3. cell junction assembly Source: Reactome
  4. cell projection assembly Source: UniProtKB
  5. establishment or maintenance of cell polarity regulating cell shape Source: UniProtKB
  6. lamellipodium assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_20649. Cell-extracellular matrix interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-parvin
Alternative name(s):
Affixin
Gene namesi
Name:PARVB
ORF Names:CGI-56
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:14653. PARVB.

Subcellular locationi

  1. Cell junctionfocal adhesion
  2. Cell membrane; Peripheral membrane protein; Cytoplasmic side
  3. Cytoplasmcytoskeleton
  4. Cell projectionlamellipodium
  5. Cytoplasmmyofibrilsarcomere
  6. CytoplasmmyofibrilsarcomereZ line

  7. Note: Constituent of focal adhesions. Detected at the tips of the leading edge of cells. Colocalizes with F-actin at the tips of lamellipodia.

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-SubCell
  2. cytosol Source: Reactome
  3. focal adhesion Source: UniProtKB
  4. lamellipodium Source: UniProtKB
  5. plasma membrane Source: UniProtKB-SubCell
  6. Z disc Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi256 – 2561V → Q: Abolishes interaction with PXN. 1 Publication
Mutagenesisi299 – 2991F → D: Abolishes interaction with ILK. Abolishes location at focal adhesion sites. 1 Publication

Organism-specific databases

PharmGKBiPA32951.

Polymorphism and mutation databases

BioMutaiPARVB.
DMDMi20139178.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 364364Beta-parvinPRO_0000121583Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei54 – 541Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9HBI1.
PaxDbiQ9HBI1.
PRIDEiQ9HBI1.

PTM databases

PhosphoSiteiQ9HBI1.

Expressioni

Tissue specificityi

Expressed predominantly in heart and skeletal muscle.2 Publications

Gene expression databases

BgeeiQ9HBI1.
CleanExiHS_PARVB.
ExpressionAtlasiQ9HBI1. baseline and differential.
GenevestigatoriQ9HBI1.

Interactioni

Subunit structurei

Interacts with DYSF. Interacts with ILK, ARHGEF6, PXN (via LD motifs), ACTN2 and actin.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Arhgef6Q8K4I33EBI-1047679,EBI-6272809From a different organism.
Arhgef7Q9ES2810EBI-1047679,EBI-642580From a different organism.

Protein-protein interaction databases

BioGridi118912. 6 interactions.
IntActiQ9HBI1. 8 interactions.
MINTiMINT-6178745.

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi243 – 2464Combined sources
Helixi250 – 2523Combined sources
Helixi254 – 26815Combined sources
Helixi269 – 2713Combined sources
Turni278 – 2847Combined sources
Helixi286 – 29510Combined sources
Helixi302 – 3043Combined sources
Helixi312 – 32817Combined sources
Helixi338 – 3425Combined sources
Helixi346 – 36015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9HBI1.
SMRiQ9HBI1. Positions 235-364.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 194108CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini254 – 361108CH 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the parvin family.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG303418.
GeneTreeiENSGT00390000009673.
HOGENOMiHOG000247027.
HOVERGENiHBG053517.
InParanoidiQ9HBI1.
KOiK06275.
OMAiLAMHFQA.
OrthoDBiEOG70KGPW.
PhylomeDBiQ9HBI1.
TreeFamiTF314025.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiIPR001715. CH-domain.
IPR028433. Parvin.
[Graphical view]
PANTHERiPTHR12114. PTHR12114. 1 hit.
PfamiPF00307. CH. 2 hits.
[Graphical view]
PIRSFiPIRSF039131. Parvin. 1 hit.
SMARTiSM00033. CH. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 2 hits.
PROSITEiPS50021. CH. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9HBI1-1) [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

        10         20         30         40         50
MSSAPRSPTP RPRRMKKDES FLGKLGGTLA RKRRAREVSD LQEEGKNAIN
60 70 80 90 100
SPMSPALVDV HPEDTQLEEN EERTMIDPTS KEDPKFKELV KVLLDWINDV
110 120 130 140 150
LVEERIIVKQ LEEDLYDGQV LQKLLEKLAG CKLNVAEVTQ SEIGQKQKLQ
160 170 180 190 200
TVLEAVHDLL RPRGWALRWS VDSIHGKNLV AILHLLVSLA MHFRAPIRLP
210 220 230 240 250
EHVTVQVVVV RKREGLLHSS HISEELTTTT EMMMGRFERD AFDTLFDHAP
260 270 280 290 300
DKLSVVKKSL ITFVNKHLNK LNLEVTELET QFADGVYLVL LMGLLEDYFV
310 320 330 340 350
PLHHFYLTPE SFDQKVHNVS FAFELMLDGG LKKPKARPED VVNLDLKSTL
360
RVLYNLFTKY KNVE
Length:364
Mass (Da):41,714
Last modified:March 1, 2001 - v1
Checksum:i4BA4B50C83083DC7
GO
Isoform 2 (identifier: Q9HBI1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-37: MSSAPRSPTP...TLARKRRARE → MHHVFKDHQR...VETSEYAQGG

Show »
Length:397
Mass (Da):45,183
Checksum:iBA4335437824E465
GO
Isoform 3 (identifier: Q9HBI1-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MSSAPRSPTPRPRRMKKDESFLGKLGGTLARKRRAREV → M

Note: No experimental confirmation available.

Show »
Length:327
Mass (Da):37,538
Checksum:iBD4A2F8D5ECD7768
GO

Sequence cautioni

The sequence AAD34051.1 differs from that shown. Reason: Frameshift at positions 4, 14, 48, 58, 155, 162, 171, 327, 331 and 344. Curated
The sequence BG743702 differs from that shown. Reason: Frameshift at positions 136, 232 and 237. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271G → V in AAD34051 (PubMed:10810093).Curated
Sequence conflicti59 – 591D → M in AAD34051 (PubMed:10810093).Curated
Sequence conflicti349 – 3491T → P in AAD34051 (PubMed:10810093).Curated
Isoform 2 (identifier: Q9HBI1-2)
Sequence conflicti4 – 41V → G in BG743702 (PubMed:15489334).Curated
Sequence conflicti21 – 211N → K in AAL08219 (Ref. 1) Curated
Sequence conflicti37 – 371W → R in AAL08219 (Ref. 1) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521P → R.
Corresponds to variant rs34476853 [ dbSNP | Ensembl ].
VAR_034369
Natural varianti58 – 581V → A.4 Publications
Corresponds to variant rs1983609 [ dbSNP | Ensembl ].
VAR_017242

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838MSSAP…RAREV → M in isoform 3. 1 PublicationVSP_045555Add
BLAST
Alternative sequencei1 – 3737MSSAP…RRARE → MHHVFKDHQRGEKRGFLSPE NKNCRRLELRRGCSCSWGLC SQALMASLAGSLLPGSDRSG VETSEYAQGG in isoform 2. 2 PublicationsVSP_041336Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14056.1. [Q9HBI1-1]
CCDS46724.1. [Q9HBI1-2]
CCDS58808.1. [Q9HBI1-3]
RefSeqiNP_001003828.1. NM_001003828.2. [Q9HBI1-2]
NP_001230314.1. NM_001243385.1. [Q9HBI1-3]
NP_001230315.1. NM_001243386.1.
NP_037459.2. NM_013327.4. [Q9HBI1-1]
UniGeneiHs.475074.

Genome annotation databases

EnsembliENST00000338758; ENSP00000342492; ENSG00000188677. [Q9HBI1-1]
ENST00000404989; ENSP00000384353; ENSG00000188677. [Q9HBI1-3]
ENST00000406477; ENSP00000384515; ENSG00000188677. [Q9HBI1-2]
GeneIDi29780.
KEGGihsa:29780.
UCSCiuc003bem.3. human. [Q9HBI1-2]
uc003ben.3. human. [Q9HBI1-1]
uc003beo.3. human.

Polymorphism and mutation databases

BioMutaiPARVB.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS14056.1. [Q9HBI1-1]
CCDS46724.1. [Q9HBI1-2]
CCDS58808.1. [Q9HBI1-3]
RefSeqiNP_001003828.1. NM_001003828.2. [Q9HBI1-2]
NP_001230314.1. NM_001243385.1. [Q9HBI1-3]
NP_001230315.1. NM_001243386.1.
NP_037459.2. NM_013327.4. [Q9HBI1-1]
UniGeneiHs.475074.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ9HBI1.
SMRiQ9HBI1. Positions 235-364.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118912. 6 interactions.
IntActiQ9HBI1. 8 interactions.
MINTiMINT-6178745.

PTM databases

PhosphoSiteiQ9HBI1.

Polymorphism and mutation databases

BioMutaiPARVB.
DMDMi20139178.

Proteomic databases

MaxQBiQ9HBI1.
PaxDbiQ9HBI1.
PRIDEiQ9HBI1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338758; ENSP00000342492; ENSG00000188677. [Q9HBI1-1]
ENST00000404989; ENSP00000384353; ENSG00000188677. [Q9HBI1-3]
ENST00000406477; ENSP00000384515; ENSG00000188677. [Q9HBI1-2]
GeneIDi29780.
KEGGihsa:29780.
UCSCiuc003bem.3. human. [Q9HBI1-2]
uc003ben.3. human. [Q9HBI1-1]
uc003beo.3. human.

Organism-specific databases

CTDi29780.
GeneCardsiGC22P044395.
HGNCiHGNC:14653. PARVB.
MIMi608121. gene.
neXtProtiNX_Q9HBI1.
PharmGKBiPA32951.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG303418.
GeneTreeiENSGT00390000009673.
HOGENOMiHOG000247027.
HOVERGENiHBG053517.
InParanoidiQ9HBI1.
KOiK06275.
OMAiLAMHFQA.
OrthoDBiEOG70KGPW.
PhylomeDBiQ9HBI1.
TreeFamiTF314025.

Enzyme and pathway databases

ReactomeiREACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_20649. Cell-extracellular matrix interactions.

Miscellaneous databases

GeneWikiiPARVB.
GenomeRNAii29780.
NextBioi52306.
PROiQ9HBI1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9HBI1.
CleanExiHS_PARVB.
ExpressionAtlasiQ9HBI1. baseline and differential.
GenevestigatoriQ9HBI1.

Family and domain databases

Gene3Di1.10.418.10. 2 hits.
InterProiIPR001715. CH-domain.
IPR028433. Parvin.
[Graphical view]
PANTHERiPTHR12114. PTHR12114. 1 hit.
PfamiPF00307. CH. 2 hits.
[Graphical view]
PIRSFiPIRSF039131. Parvin. 1 hit.
SMARTiSM00033. CH. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 2 hits.
PROSITEiPS50021. CH. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. 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.

Entry informationi

Entry nameiPARVB_HUMAN
AccessioniPrimary (citable) accession number: Q9HBI1
Secondary accession number(s): B0QYM8
, B0QYN1, B2R9X6, Q5TGJ5, Q86X93, Q96PN1, Q9NSP7, Q9UGT3, Q9Y368, Q9Y3L6, Q9Y3L7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 131 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.