Q9HBI0 (PARVG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gamma-parvin

Gene names

Name:

PARVG

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	331 AA.
Sequence status	Complete.
Protein existence	Evidence 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 junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cytoplasm › cytoskeleton 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 process	Cell adhesion
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Actin-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell-matrix adhesion Traceable author statement Ref.1. Source: UniProtKB
Cellular component	cytoplasm 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 function	actin 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 331	331	Gamma-parvin		PRO_0000121585
Regions
	Domain	44 – 151	108	CH 1
	Domain	210 – 317	108	CH 2
Natural variations
	Alternative sequence	187	1	S → R in isoform 3.		VSP_012953
	Alternative sequence	188 – 331	144	Missing in isoform 3.		VSP_012954
	Alternative sequence	272 – 273	2	LH → IS in isoform 2.		VSP_004540
	Alternative sequence	274 – 331	58	Missing in isoform 2.		VSP_004541

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 392BFCDD0B7D86A4	FASTA	331	37,485
	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
	Isoform 2 [UniParc]. Checksum: D9BCB325BE989A1A	FASTA	273	31,042
	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 GVILLLLIGQ LEGFFLHLKE FYLTPNSPAE MIS
	Isoform 3 [UniParc]. Checksum: 8B738B944A464753	FASTA	187	21,439
	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 EQLTEYR

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00005512. IPI00215934. IPI00552212.
RefSeq	NP_001131077.1. NM_001137605.1. NP_001131078.1. NM_001137606.1. NP_071424.1. NM_022141.5.
UniGene	Hs.658995.
3D structure databases
ProteinModelPortal	Q9HBI0.
SMR	Q9HBI0. Positions 47-151, 192-320.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9HBI0. 2 interactions.
MINT	MINT-6944620.
STRING	Q9HBI0.
PTM databases
PhosphoSite	Q9HBI0.
Polymorphism databases
DMDM	20143882.
Proteomic databases
PRIDE	Q9HBI0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000415224; ENSP00000416761; ENSG00000138964. ENST00000422871; ENSP00000391453; ENSG00000138964. ENST00000444313; ENSP00000391583; ENSG00000138964. ENST00000448527; ENSP00000388613; ENSG00000138964.
GeneID	64098.
KEGG	hsa:64098.
UCSC	uc003bep.1. human.
Organism-specific databases
CTD	64098.
GeneCards	GC22P044568.
H-InvDB	HIX0016565. HIX0016566.
HGNC	HGNC:14654. PARVG.
HPA	HPA031834.
MIM	608122. gene.
neXtProt	NX_Q9HBI0.
PharmGKB	PA32952.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG13055.
GeneTree	ENSGT00390000009673.
HOGENOM	HBG447386.
HOVERGEN	HBG053517.
InParanoid	Q9HBI0.
OMA	RSLEEDM.
OrthoDB	EOG4N04FC.
PhylomeDB	Q9HBI0.
Gene expression databases
ArrayExpress	Q9HBI0.
Bgee	Q9HBI0.
CleanEx	HS_PARVG.
Genevestigator	Q9HBI0.
GermOnline	ENSG00000138964. Homo sapiens.
Family and domain databases
InterPro	IPR001715. CH-domain. [Graphical view]
Gene3D	G3DSA:1.10.418.10. Calponin-homology. 2 hits.
KO	K06275.
Pfam	PF00307. CH. 2 hits. [Graphical view]
SMART	SM00033. CH. 1 hit. [Graphical view]
SUPFAM	SSF47576. Calponin-homology. 1 hit.
PROSITE	PS50021. CH. 2 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	65928.
SOURCE	Search...

Entry information

Entry name

PARVG_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.