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Q9HBI0 (PARVG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gamma-parvin
Gene names
Name:PARVG
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length331 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Probably plays a role in the regulation of cell adhesion and cytoskeleton organization By similarity.

Subunit structure

Interacts with integrin-linked protein kinase and actin By similarity.

Subcellular location

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasmcytoskeleton By similarity. Note: Constituent of focal adhesions By similarity.

Tissue specificity

Expressed predominantly in lymphoid organs, including spleen, thymus, lymph node, bone marrow and peripheral blood leukocytes and moderately in the digestive tract, including stomach, duodenum, jejunum, ileum, ileocecum and appendix, as well as in lung and liver. Also expressed in tumors, but at a lower level than in the corresponding normal tissues. Ref.6

Sequence similarities

Belongs to the parvin family.

Contains 2 CH (calponin-homology) domains.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandActin-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcell-matrix adhesion

Traceable author statement Ref.1. Source: UniProtKB

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

cytoskeleton

Traceable author statement Ref.1. Source: UniProtKB

focal adhesion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionactin binding

Traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HBI0-1)

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: Q9HBI0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     272-273: LH → IS
     274-331: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9HBI0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     187-187: S → R
     188-331: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 331331Gamma-parvin
PRO_0000121585

Regions

Domain44 – 151108CH 1
Domain210 – 317108CH 2

Natural variations

Alternative sequence1871S → R in isoform 3.
VSP_012953
Alternative sequence188 – 331144Missing in isoform 3.
VSP_012954
Alternative sequence272 – 2732LH → IS in isoform 2.
VSP_004540
Alternative sequence274 – 33158Missing in isoform 2.
VSP_004541

Sequences

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

Last modified March 1, 2001. Version 1.
Checksum: 392BFCDD0B7D86A4

FASTA33137,485
        10         20         30         40         50         60 
MEPEFLYDLL QLPKGVEPPA EEELSKGGKK KYLPPTSRKD PKFEELQKVL MEWINATLLP 

        70         80         90        100        110        120 
EHIVVRSLEE DMFDGLILHH LFQRLAALKL EAEDIALTAT SQKHKLTVVL EAVNRSLQLE 

       130        140        150        160        170        180 
EWQAKWSVES IFNKDLLSTL HLLVALAKRF QPDLSLPTNV QVEVITIEST KSGLKSEKLV 

       190        200        210        220        230        240 
EQLTEYSTDK DEPPKDVFDE LFKLAPEKVN AVKEAIVNFV NQKLDRLGLS VQNLDTQFAD 

       250        260        270        280        290        300 
GVILLLLIGQ LEGFFLHLKE FYLTPNSPAE MLHNVTLALE LLKDEGLLSC PVSPEDIVNK 

       310        320        330 
DAKSTLRVLY GLFCKHTQKA HRDRTPHGAP N 

« Hide

Isoform 2 [UniParc].

Checksum: D9BCB325BE989A1A
Show »

FASTA27331,042
Isoform 3 [UniParc].

Checksum: 8B738B944A464753
Show »

FASTA18721,439

References

« Hide 'large scale' references
[1]"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: 11171322] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1).
[2]"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: 12529303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
Tissue: Fetal brain.
[3]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"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: 10591208] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain, Lung and Testis.
[6]"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: 11722847] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF237772 mRNA. Translation: AAG27174.1.
AL590887 mRNA. Translation: CAC37414.1.
AL355092 mRNA. Translation: CAB90188.1.
CR456480 mRNA. Translation: CAG30366.1.
AL031595 Genomic DNA. Translation: CAI22314.1.
BC034406 mRNA. Translation: AAH34406.1.
IPIIPI00005512.
IPI00215934.
IPI00552212.
RefSeqNP_001131077.1. NM_001137605.1.
NP_001131078.1. NM_001137606.1.
NP_071424.1. NM_022141.5.
UniGeneHs.658995.

3D structure databases

ProteinModelPortalQ9HBI0.
SMRQ9HBI0. Positions 47-151, 192-320.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9HBI0. 2 interactions.
MINTMINT-6944620.
STRINGQ9HBI0.

PTM databases

PhosphoSiteQ9HBI0.

Polymorphism databases

DMDM20143882.

Proteomic databases

PRIDEQ9HBI0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000415224; ENSP00000416761; ENSG00000138964.
ENST00000422871; ENSP00000391453; ENSG00000138964.
ENST00000444313; ENSP00000391583; ENSG00000138964.
ENST00000448527; ENSP00000388613; ENSG00000138964.
GeneID64098.
KEGGhsa:64098.
UCSCuc003bep.1. human.

Organism-specific databases

CTD64098.
GeneCardsGC22P044568.
H-InvDBHIX0016565.
HIX0016566.
HGNCHGNC:14654. PARVG.
HPAHPA031834.
MIM608122. gene.
neXtProtNX_Q9HBI0.
PharmGKBPA32952.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG13055.
GeneTreeENSGT00390000009673.
HOGENOMHBG447386.
HOVERGENHBG053517.
InParanoidQ9HBI0.
OMARSLEEDM.
OrthoDBEOG4N04FC.
PhylomeDBQ9HBI0.

Gene expression databases

ArrayExpressQ9HBI0.
BgeeQ9HBI0.
CleanExHS_PARVG.
GenevestigatorQ9HBI0.
GermOnlineENSG00000138964. Homo sapiens.

Family and domain databases

InterProIPR001715. CH-domain.
[Graphical view]
Gene3DG3DSA:1.10.418.10. Calponin-homology. 2 hits.
KOK06275.
PfamPF00307. CH. 2 hits.
[Graphical view]
SMARTSM00033. CH. 1 hit.
[Graphical view]
SUPFAMSSF47576. Calponin-homology. 1 hit.
PROSITEPS50021. CH. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio65928.
SOURCESearch...

Entry information

Entry namePARVG_HUMAN
AccessionPrimary (citable) accession number: Q9HBI0
Secondary accession number(s): Q9BQX5, Q9NSG1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: March 1, 2001
Last modified: January 25, 2012
This is version 87 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

Human chromosome 22

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families