Q9HBI1 (PARVB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Beta-parvin

Alternative name(s):
Affixin

Gene names

Name:	PARVB
ORF Names:	CGI-56

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Protein existence	Evidence 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.18
Subcellular location	Cell junction › focal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm › cytoskeleton. Cell projection › lamellipodium. Cytoplasm › myofibril › sarcomere. Cytoplasm › myofibril › sarcomere › Z 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.18
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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin cytoskeleton reorganization Inferred from mutant phenotype Ref.11. Source: UniProtKB cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell junction assembly Traceable author statement. Source: Reactome establishment or maintenance of cell polarity regulating cell shape Inferred from mutant phenotype Ref.11. Source: UniProtKB lamellipodium assembly Inferred from mutant phenotype Ref.15. Source: UniProtKB
Cellular_component	Z disc Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome focal adhesion Inferred from direct assay Ref.18. Source: UniProtKB lamellipodium Inferred from direct assay Ref.15. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 364

364

Beta-parvin

PRO_0000121583

Regions

Domain

87 – 194

108

CH 1

Domain

254 – 361

108

CH 2

Amino acid modifications

Modified residue

54

1

Phosphoserine Ref.16

Natural variations

Alternative sequence

1 – 38

38

MSSAP…RAREV → M in isoform 3.

VSP_045555

Alternative sequence

1 – 37

37

MSSAP…RRARE → MHHVFKDHQRGEKRGFLSPE NKNCRRLELRRGCSCSWGLC SQALMASLAGSLLPGSDRSG VETSEYAQGG in isoform 2.

VSP_041336

Natural variant

52

1

P → R.
Corresponds to variant rs34476853 [ dbSNP | Ensembl ].

VAR_034369

Natural variant

58

1

V → A. Ref.1 Ref.5 Ref.8 Ref.16
Corresponds to variant rs1983609 [ dbSNP | Ensembl ].

VAR_017242

Experimental info

Mutagenesis

256

1

V → Q: Abolishes interaction with PXN. Ref.18

Mutagenesis

299

1

F → D: Abolishes interaction with ILK. Abolishes location at focal adhesion sites. Ref.18

Sequence conflict

27

1

G → V in AAD34051. Ref.4

Sequence conflict

59

1

D → M in AAD34051. Ref.4

Sequence conflict

349

1

T → P in AAD34051. Ref.4

Isoform 2:

Sequence conflict

4

1

V → G in BG743702. Ref.8

Secondary structure

1

.

.

.

.

.

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.

.

.

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.

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.

364

Helix Strand Turn

Details...

Helix

243 – 246

4

Helix

250 – 252

3

Helix

254 – 268

15

Helix

269 – 271

3

Turn

278 – 284

7

Helix

286 – 295

10

Helix

302 – 304

3

Helix

312 – 328

17

Helix

338 – 342

5

Helix

346 – 360

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 4BA4B50C83083DC7	FASTA	364	41,714
	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
	Isoform 2 [UniParc]. Checksum: BA4335437824E465	FASTA	397	45,183
	10 20 30 40 50 60 MHHVFKDHQR GEKRGFLSPE NKNCRRLELR RGCSCSWGLC SQALMASLAG SLLPGSDRSG 70 80 90 100 110 120 VETSEYAQGG VSDLQEEGKN AINSPMSPAL VDVHPEDTQL EENEERTMID PTSKEDPKFK 130 140 150 160 170 180 ELVKVLLDWI NDVLVEERII VKQLEEDLYD GQVLQKLLEK LAGCKLNVAE VTQSEIGQKQ 190 200 210 220 230 240 KLQTVLEAVH DLLRPRGWAL RWSVDSIHGK NLVAILHLLV SLAMHFRAPI RLPEHVTVQV 250 260 270 280 290 300 VVVRKREGLL HSSHISEELT TTTEMMMGRF ERDAFDTLFD HAPDKLSVVK KSLITFVNKH 310 320 330 340 350 360 LNKLNLEVTE LETQFADGVY LVLLMGLLED YFVPLHHFYL TPESFDQKVH NVSFAFELML 370 380 390 DGGLKKPKAR PEDVVNLDLK STLRVLYNLF TKYKNVE
	Isoform 3 [UniParc]. Checksum: BD4A2F8D5ECD7768	FASTA	327	37,538
	10 20 30 40 50 60 MSDLQEEGKN AINSPMSPAL VDVHPEDTQL EENEERTMID PTSKEDPKFK ELVKVLLDWI 70 80 90 100 110 120 NDVLVEERII VKQLEEDLYD GQVLQKLLEK LAGCKLNVAE VTQSEIGQKQ KLQTVLEAVH 130 140 150 160 170 180 DLLRPRGWAL RWSVDSIHGK NLVAILHLLV SLAMHFRAPI RLPEHVTVQV VVVRKREGLL 190 200 210 220 230 240 HSSHISEELT TTTEMMMGRF ERDAFDTLFD HAPDKLSVVK KSLITFVNKH LNKLNLEVTE 250 260 270 280 290 300 LETQFADGVY LVLLMGLLED YFVPLHHFYL TPESFDQKVH NVSFAFELML DGGLKKPKAR 310 320 PEDVVNLDLK STLRVLYNLF TKYKNVE

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. 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]	"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.

IPI

IPI00043083.
IPI00382605.
IPI00879834.

RefSeq

NP_001003828.1. NM_001003828.2.
NP_001230314.1. NM_001243385.1.
NP_001230315.1. NM_001243386.1.
NP_037459.2. NM_013327.4.

UniGene

Hs.475074.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4EDL	X-ray	2.10	A/B/C/D/E/F	235-364	[»]
4EDM	X-ray	2.00	A/B	235-364	[»]
4EDN	X-ray	2.90	A/B/C/D/E/F/G/H/I/J	235-364	[»]

ProteinModelPortal

Q9HBI1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9HBI1. 1 interaction.

MINT

MINT-6178745.

PTM databases

PhosphoSite

Q9HBI1.

Polymorphism databases

DMDM

20139178.

Proteomic databases

PaxDb

Q9HBI1.

PRIDE

Q9HBI1.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338758; ENSP00000342492; ENSG00000188677.
ENST00000404989; ENSP00000384353; ENSG00000188677.
ENST00000406477; ENSP00000384515; ENSG00000188677.

GeneID

29780.

KEGG

hsa:29780.

UCSC

uc003bem.3. human.
uc003ben.3. human.

Organism-specific databases

CTD

29780.

GeneCards

GC22P044395.

HGNC

HGNC:14653. PARVB.

MIM

608121. gene.

neXtProt

NX_Q9HBI1.

PharmGKB

PA32951.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG303418.

HOVERGEN

HBG053517.

KO

K06275.

OMA

NLFTNYK.

OrthoDB

EOG4VX25H.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.

Gene expression databases

ArrayExpress

Q9HBI1.

Bgee

Q9HBI1.

CleanEx

HS_PARVB.

Genevestigator

Q9HBI1.

GermOnline

ENSG00000188677. Homo sapiens.

Family and domain databases

Gene3D

1.10.418.10. 2 hits.

InterPro

IPR001715. CH-domain.
[Graphical view]

Pfam

PF00307. CH. 2 hits.
[Graphical view]

SMART

SM00033. CH. 2 hits.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.

PROSITE

PS50021. CH. 2 hits.
[Graphical view]

ProtoNet

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Other

GenomeRNAi

29780.

NextBio

52306.

SOURCE

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Entry information

Entry name

PARVB_HUMAN

Accession

Primary (citable) accession number: Q9HBI1
Secondary accession number(s): B0QYM8 , 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:	May 1, 2013
This is version 113 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.