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Q9NVD7

- PARVA_HUMAN

UniProt

Q9NVD7 - PARVA_HUMAN

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Protein

Alpha-parvin

Gene
PARVA, MXRA2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells to endothelial cells during blood vessel development By similarity. Plays a role in the reorganization of the actin cytoskeleton, formation of lamellipodia and ciliogenesis. Plays a role in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration.4 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. actin cytoskeleton reorganization Source: InterPro
  2. actin-mediated cell contraction Source: UniProtKB
  3. cell junction assembly Source: Reactome
  4. cilium morphogenesis Source: UniProtKB
  5. establishment or maintenance of cell polarity Source: UniProtKB
  6. heterotypic cell-cell adhesion Source: UniProtKB
  7. outflow tract septum morphogenesis Source: UniProtKB
  8. regulation of cell shape Source: UniProtKB-KW
  9. smooth muscle cell chemotaxis Source: UniProtKB
  10. sprouting angiogenesis Source: UniProtKB
  11. substrate adhesion-dependent cell spreading Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Angiogenesis, Cell adhesion, Cell shape, Chemotaxis, Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_20649. Cell-extracellular matrix interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-parvin
Alternative name(s):
Actopaxin
CH-ILKBP
Calponin-like integrin-linked kinase-binding protein
Matrix-remodeling-associated protein 2
Gene namesi
Name:PARVA
Synonyms:MXRA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:14652. PARVA.

Subcellular locationi

Cell junctionfocal adhesion. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereZ line By similarity
Note: Constituent of focal adhesions. Associates with the actin cytoskeleton.3 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA32950.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 372371Alpha-parvinPRO_0000121580Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei8 – 81Phosphoserine By similarity
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei19 – 191Phosphoserine2 Publications
Modified residuei28 – 281Phosphoserine1 Publication
Modified residuei62 – 621Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NVD7.
PaxDbiQ9NVD7.
PRIDEiQ9NVD7.

PTM databases

PhosphoSiteiQ9NVD7.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in heart, skeletal muscle, kidney and liver.3 Publications

Gene expression databases

ArrayExpressiQ9NVD7.
BgeeiQ9NVD7.
CleanExiHS_PARVA.
GenevestigatoriQ9NVD7.

Organism-specific databases

HPAiHPA005964.

Interactioni

Subunit structurei

Interacts with TGFB1I1 By similarity. Interacts with ILK, LIMS1 and PXN (via LD motifs). Interacts with ARHGAP31. Interacts with the actin cytoskeleton.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ILKQ134187EBI-747655,EBI-747644

Protein-protein interaction databases

BioGridi120860. 20 interactions.
IntActiQ9NVD7. 11 interactions.
MINTiMINT-1465264.
STRINGi9606.ENSP00000334008.

Structurei

Secondary structure

1
372
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi249 – 2568
Helixi258 – 27619
Helixi277 – 2793
Turni286 – 2927
Helixi294 – 30310
Helixi310 – 3123
Helixi320 – 33617
Helixi346 – 3505
Helixi354 – 36815

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K2RNMR-A244-372[»]
2VZCX-ray1.05A/B242-372[»]
2VZDX-ray2.10A/B242-372[»]
2VZGX-ray1.80B242-372[»]
2VZIX-ray2.20B242-372[»]
3KMUX-ray1.80B248-372[»]
3KMWX-ray2.00B248-372[»]
3REPX-ray1.80B248-372[»]
ProteinModelPortaliQ9NVD7.
SMRiQ9NVD7. Positions 246-372.

Miscellaneous databases

EvolutionaryTraceiQ9NVD7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini95 – 201107CH 1Add
BLAST
Domaini262 – 369108CH 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni21 – 255Interaction with ARHGAP31

Sequence similaritiesi

Belongs to the parvin family.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG303418.
HOGENOMiHOG000247027.
HOVERGENiHBG053517.
InParanoidiQ9NVD7.
KOiK06275.
PhylomeDBiQ9NVD7.

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]
SMARTiSM00033. CH. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 2 hits.
PROSITEiPS50021. CH. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NVD7-1) [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

MATSPQKSPS VPKSPTPKSP PSRKKDDSFL GKLGGTLARR KKAKEVSELQ    50
EEGMNAINLP LSPIPFELDP EDTMLEENEV RTMVDPNSRS DPKLQELMKV 100
LIDWINDVLV GERIIVKDLA EDLYDGQVLQ KLFEKLESEK LNVAEVTQSE 150
IAQKQKLQTV LEKINETLKL PPRSIKWNVD SVHAKSLVAI LHLLVALSQY 200
FRAPIRLPDH VSIQVVVVQK REGILQSRQI QEEITGNTEA LSGRHERDAF 250
DTLFDHAPDK LNVVKKTLIT FVNKHLNKLN LEVTELETQF ADGVYLVLLM 300
GLLEGYFVPL HSFFLTPDSF EQKVLNVSFA FELMQDGGLE KPKPRPEDIV 350
NCDLKSTLRV LYNLFTKYRN VE 372
Length:372
Mass (Da):42,244
Last modified:October 1, 2000 - v1
Checksum:iF48BB5B1E83F8CEF
GO
Isoform 2 (identifier: Q9NVD7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-182: EKLESEKLNV...RSIKWNVDSV → GRRVECCNGC...KCVEHGITAQ
     183-372: Missing.

Note: No experimental confirmation available.

Show »
Length:182
Mass (Da):20,625
Checksum:iB7D6685D209E628F
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei134 – 18249EKLES…NVDSV → GRRVECCNGCVFNCRWLDHL LVARRSYSQFTVAYLEMDYK CVEHGITAQ in isoform 2. VSP_008884Add
BLAST
Alternative sequencei183 – 372190Missing in isoform 2. VSP_008885Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111V → A in AAH14535. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF237771 mRNA. Translation: AAG27173.1.
AF325830 mRNA. Translation: AAK49911.1.
AK001655 mRNA. Translation: BAA91815.1.
AK022316 mRNA. Translation: BAB14009.1.
BC016713 mRNA. Translation: AAH16713.1.
BC014535 mRNA. Translation: AAH14535.1.
RefSeqiNP_060692.2. NM_018222.4.
UniGeneiHs.432914.

Genome annotation databases

EnsembliENST00000550549; ENSP00000447198; ENSG00000197702. [Q9NVD7-1]
GeneIDi55742.
KEGGihsa:55742.
UCSCiuc001mkh.3. human. [Q9NVD7-2]

Polymorphism databases

DMDMi20139236.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF237771 mRNA. Translation: AAG27173.1 .
AF325830 mRNA. Translation: AAK49911.1 .
AK001655 mRNA. Translation: BAA91815.1 .
AK022316 mRNA. Translation: BAB14009.1 .
BC016713 mRNA. Translation: AAH16713.1 .
BC014535 mRNA. Translation: AAH14535.1 .
RefSeqi NP_060692.2. NM_018222.4.
UniGenei Hs.432914.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K2R NMR - A 244-372 [» ]
2VZC X-ray 1.05 A/B 242-372 [» ]
2VZD X-ray 2.10 A/B 242-372 [» ]
2VZG X-ray 1.80 B 242-372 [» ]
2VZI X-ray 2.20 B 242-372 [» ]
3KMU X-ray 1.80 B 248-372 [» ]
3KMW X-ray 2.00 B 248-372 [» ]
3REP X-ray 1.80 B 248-372 [» ]
ProteinModelPortali Q9NVD7.
SMRi Q9NVD7. Positions 246-372.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120860. 20 interactions.
IntActi Q9NVD7. 11 interactions.
MINTi MINT-1465264.
STRINGi 9606.ENSP00000334008.

PTM databases

PhosphoSitei Q9NVD7.

Polymorphism databases

DMDMi 20139236.

Proteomic databases

MaxQBi Q9NVD7.
PaxDbi Q9NVD7.
PRIDEi Q9NVD7.

Protocols and materials databases

DNASUi 55742.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000550549 ; ENSP00000447198 ; ENSG00000197702 . [Q9NVD7-1 ]
GeneIDi 55742.
KEGGi hsa:55742.
UCSCi uc001mkh.3. human. [Q9NVD7-2 ]

Organism-specific databases

CTDi 55742.
GeneCardsi GC11P012398.
HGNCi HGNC:14652. PARVA.
HPAi HPA005964.
MIMi 608120. gene.
neXtProti NX_Q9NVD7.
PharmGKBi PA32950.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG303418.
HOGENOMi HOG000247027.
HOVERGENi HBG053517.
InParanoidi Q9NVD7.
KOi K06275.
PhylomeDBi Q9NVD7.

Enzyme and pathway databases

Reactomei REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_20617. Localization of the PINCH-ILK-PARVIN complex to focal adhesions.
REACT_20649. Cell-extracellular matrix interactions.

Miscellaneous databases

ChiTaRSi PARVA. human.
EvolutionaryTracei Q9NVD7.
GeneWikii PARVA.
GenomeRNAii 55742.
NextBioi 60703.
PROi Q9NVD7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9NVD7.
Bgeei Q9NVD7.
CleanExi HS_PARVA.
Genevestigatori Q9NVD7.

Family and domain databases

Gene3Di 1.10.418.10. 2 hits.
InterProi IPR001715. CH-domain.
IPR028433. Parvin.
[Graphical view ]
PANTHERi PTHR12114. PTHR12114. 1 hit.
Pfami PF00307. CH. 2 hits.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 2 hits.
PROSITEi PS50021. CH. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading."
    Tu Y., Huang Y., Zhang Y., Hua Y., Wu C.
    J. Cell Biol. 153:585-598(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ILK; LIMS1 AND WITH ACTIN CYTOSKELETON, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. "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] (ISOFORMS 1 AND 2).
    Tissue: Mammary gland.
  4. "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] (ISOFORM 1).
    Tissue: Brain.
  5. "Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes."
    Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.
    Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 118-131.
    Tissue: Adipocyte.
  6. "Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion."
    Nikolopoulos S.N., Turner C.E.
    J. Cell Biol. 151:1435-1448(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  7. "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.
  8. "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.
  9. "CdGAP associates with actopaxin to regulate integrin-dependent changes in cell morphology and motility."
    LaLonde D.P., Grubinger M., Lamarche-Vane N., Turner C.E.
    Curr. Biol. 16:1375-1385(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARHGAP31.
  10. "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-28 AND SER-62, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Functional genomic screen for modulators of ciliogenesis and cilium length."
    Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
    Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "LNK (SH2B3) is a key regulator of integrin signaling in endothelial cells and targets alpha-parvin to control cell adhesion and migration."
    Devalliere J., Chatelais M., Fitau J., Gerard N., Hulin P., Velazquez L., Turner C.E., Charreau B.
    FASEB J. 26:2592-2606(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly."
    Wang X., Fukuda K., Byeon I.J., Velyvis A., Wu C., Gronenborn A., Qin J.
    J. Biol. Chem. 283:21113-21119(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 244-372 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
  17. "Structural analysis of the interactions between paxillin LD motifs and alpha-parvin."
    Lorenz S., Vakonakis I., Lowe E.D., Campbell I.D., Noble M.E., Hoellerer M.K.
    Structure 16:1521-1531(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 242-372 IN COMPLEX WITH PXN, INTERACTION WITH PXN.
  18. "The pseudoactive site of ILK is essential for its binding to alpha-parvin and localization to focal adhesions."
    Fukuda K., Gupta S., Chen K., Wu C., Qin J.
    Mol. Cell 36:819-830(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 248-372 IN COMPLEX WITH ILK, INTERACTION WITH ILK.

Entry informationi

Entry nameiPARVA_HUMAN
AccessioniPrimary (citable) accession number: Q9NVD7
Secondary accession number(s): Q96C85, Q9HA48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: September 3, 2014
This is version 127 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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