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Q86UA6

- RIP_HUMAN

UniProt

Q86UA6 - RIP_HUMAN

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Protein

RPA-interacting protein

Gene

RPAIN

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

Functioni

Mediates the import of RPA complex into the nucleus, possibly via some interaction with importin beta. Isoform 2 is sumoylated and mediates the localization of RPA complex into the PML body of the nucleus, thereby participating in RPA function in DNA metabolism.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri137 – 21276RIP-typeAdd
BLAST

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. protein complex binding Source: MGI

GO - Biological processi

  1. DNA-dependent DNA replication Source: MGI
  2. DNA recombination Source: MGI
  3. DNA repair Source: MGI
  4. protein import into nucleus Source: MGI
  5. response to UV Source: MGI
Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
RPA-interacting protein
Short name:
hRIP
Gene namesi
Name:RPAIN
Synonyms:RIP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:28641. RPAIN.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleolus Source: HPA
  3. nucleus Source: HPA
  4. PML body Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141K → R: Abolishes sumoylation; when associated with N-103; R-121 and R-142. 1 Publication
Mutagenesisi121 – 1211K → R: Induces a strong decrease in sumoylation; when associated with N-103. Abolishes sumoylation; when associated with N-103; R-114 and R-142. 1 Publication
Mutagenesisi142 – 1421K → R: Abolishes sumoylation; when associated with N-103; R-114 and R-121. 1 Publication

Organism-specific databases

PharmGKBiPA145007849.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 219219RPA-interacting proteinPRO_0000076299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki103 – 103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); in isoform 2Curated
Cross-linki121 – 121Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); in isoform 2Curated

Post-translational modificationi

Isoform 2 is sumoylated. Sumoylation is required for localization in the nuclear PML body and transport of RPA complex in PML body. Upon UV irradiation and during S phase, it is desumoylated, releasing RPA complex that is translocated to sites of DNA damage. Sumoylation takes place at different Lys residues.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ86UA6.
PaxDbiQ86UA6.
PRIDEiQ86UA6.

PTM databases

PhosphoSiteiQ86UA6.

Expressioni

Tissue specificityi

Widely expressed. Expressed in pancreas, kidney, muscle, liver, lung, placenta, brain, heart, leukocytes, colon, intestine, ovary, testis, prostate, thymus and spleen.1 Publication

Gene expression databases

BgeeiQ86UA6.
CleanExiHS_RPAIN.
ExpressionAtlasiQ86UA6. baseline and differential.
GenevestigatoriQ86UA6.

Organism-specific databases

HPAiHPA023924.
HPA031526.

Interactioni

Subunit structurei

Interacts with the RPA1 subunit of RPA complex.1 Publication

Protein-protein interaction databases

BioGridi123995. 8 interactions.
IntActiQ86UA6. 4 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ86UA6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 18017Mediates nuclear exportAdd
BLAST

Sequence similaritiesi

Contains 1 RIP-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri137 – 21276RIP-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG46030.
GeneTreeiENSGT00390000006416.
HOVERGENiHBG082800.
InParanoidiQ86UA6.
OrthoDBiEOG7673BZ.
PhylomeDBiQ86UA6.
TreeFamiTF326215.

Family and domain databases

InterProiIPR028156. RIP.
IPR028159. RPA_interact_C_dom.
IPR028155. RPA_interact_central.
IPR028158. RPA_interact_N_dom.
[Graphical view]
PANTHERiPTHR31742. PTHR31742. 1 hit.
PfamiPF14768. RPA_interact_C. 1 hit.
PF14767. RPA_interact_M. 1 hit.
PF14766. RPA_interact_N. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

This entry describes 9 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86UA6-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha, hRIPalpha

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
MAESLRSPRR SLYKLVGSPP WKEAFRQRCL ERMRNSRDRL LNRYRQAGSS
60 70 80 90 100
GPGNSQNSFL VQEVMEEEWN ALQSVENCPE DLAQLEELID MAVLEEIQQE
110 120 130 140 150
LIKQEQSIIS EYEKSLQFDE KCLSIMLAEW EANPLICPVC TKYNLRITSG
160 170 180 190 200
VVVCQCGLSI PSHSSELTEQ KLRACLEGSI NEHSAHCPHT PEFSVTGGTE
210
EKSSLLMSCL ACDTWAVIL

Note: Major isoform with isoform 2.

Length:219
Mass (Da):24,784
Last modified:June 1, 2003 - v1
Checksum:i4AF573893850704E
GO
Isoform 2 (identifier: Q86UA6-2) [UniParc]FASTAAdd to Basket

Also known as: Beta, hRIPbeta

The sequence of this isoform differs from the canonical sequence as follows:
     164-210: Missing.

Note: Major isoform with isoform 1.

Show »
Length:172
Mass (Da):19,727
Checksum:i0B6AA34C1429D384
GO
Isoform 3 (identifier: Q86UA6-3) [UniParc]FASTAAdd to Basket

Also known as: Gamma2

The sequence of this isoform differs from the canonical sequence as follows:
     143-219: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. May be due to an intron retention.

Show »
Length:142
Mass (Da):16,525
Checksum:iB08C00B3708D8E58
GO
Isoform 4 (identifier: Q86UA6-4) [UniParc]FASTAAdd to Basket

Also known as: Gamma1

The sequence of this isoform differs from the canonical sequence as follows:
     142-145: KYNL → NLLS
     146-219: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:145
Mass (Da):16,824
Checksum:iA7977D77FC00B370
GO
Isoform 5 (identifier: Q86UA6-5) [UniParc]FASTAAdd to Basket

Also known as: Delta2

The sequence of this isoform differs from the canonical sequence as follows:
     105-106: EQ → VF
     107-219: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:106
Mass (Da):12,399
Checksum:i184280661713B68C
GO
Isoform 6 (identifier: Q86UA6-6) [UniParc]FASTAAdd to Basket

Also known as: Delta3

The sequence of this isoform differs from the canonical sequence as follows:
     105-106: EQ → GL
     107-219: Missing.

Show »
Length:106
Mass (Da):12,323
Checksum:i16B830661713B68C
GO
Isoform 7 (identifier: Q86UA6-7) [UniParc]FASTAAdd to Basket

Also known as: Delta1, Delta 4

The sequence of this isoform differs from the canonical sequence as follows:
     105-107: EQS → GTT
     108-219: Missing.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Show »
Length:107
Mass (Da):12,412
Checksum:iA2803830661713B6
GO
Isoform 8 (identifier: Q86UA6-8) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     211-219: ACDTWAVIL → VSVSWDPLCGKRDLWLVLFPP

Note: No experimental confirmation available.

Show »
Length:231
Mass (Da):26,221
Checksum:i224CC8977EF906E9
GO
Isoform 9 (identifier: Q86UA6-9) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     143-219: YNLRITSGVV...LACDTWAVIL → PVILGL

Note: No experimental confirmation available.

Show »
Length:148
Mass (Da):17,118
Checksum:i67DFE6F2628D308C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031K → N Common polymorphism; results in a decrease in sumoylation. 3 Publications
Corresponds to variant rs12761 [ dbSNP | Ensembl ].
VAR_023947

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei105 – 1073EQS → GTT in isoform 7. 2 PublicationsVSP_016402
Alternative sequencei105 – 1062EQ → VF in isoform 5. 2 PublicationsVSP_016403
Alternative sequencei105 – 1062EQ → GL in isoform 6. 3 PublicationsVSP_016404
Alternative sequencei107 – 219113Missing in isoform 5 and isoform 6. 3 PublicationsVSP_016405Add
BLAST
Alternative sequencei108 – 219112Missing in isoform 7. 2 PublicationsVSP_016406Add
BLAST
Alternative sequencei142 – 1454KYNL → NLLS in isoform 4. 3 PublicationsVSP_016407
Alternative sequencei143 – 21977Missing in isoform 3. 2 PublicationsVSP_016408Add
BLAST
Alternative sequencei143 – 21977YNLRI…WAVIL → PVILGL in isoform 9. CuratedVSP_046795Add
BLAST
Alternative sequencei146 – 21974Missing in isoform 4. 3 PublicationsVSP_016409Add
BLAST
Alternative sequencei164 – 21047Missing in isoform 2. 2 PublicationsVSP_016410Add
BLAST
Alternative sequencei211 – 2199ACDTWAVIL → VSVSWDPLCGKRDLWLVLFP P in isoform 8. 1 PublicationVSP_045356

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY775314 mRNA. Translation: AAX14368.1.
AY775315 mRNA. Translation: AAX14369.1.
AY775316 mRNA. Translation: AAX14370.1.
AY775317 mRNA. Translation: AAX14371.1.
AY775318 mRNA. Translation: AAX14372.1.
AY775319 mRNA. Translation: AAX14373.1.
AY775320 mRNA. Translation: AAX14374.1.
AY775321 mRNA. Translation: AAX14375.1.
AY775323 mRNA. Translation: AAX14377.1.
AY680654 mRNA. Translation: AAT80872.1.
AY680655 mRNA. Translation: AAT80873.1.
AY680656 mRNA. Translation: AAT80874.1.
AY680657 mRNA. Translation: AAT80875.1.
AY680658 mRNA. Translation: AAT80876.1.
AY680659 mRNA. Translation: AAT80877.1.
AY680660 mRNA. Translation: AAT80878.1.
AK295394 mRNA. Translation: BAG58348.1.
AK300409 mRNA. Translation: BAG62139.1.
AC004148 Genomic DNA. No translation available.
BC004451 mRNA. Translation: AAH04451.1.
BC046349 mRNA. Translation: AAH46349.1.
BC051849 mRNA. Translation: AAH51849.1.
CCDSiCCDS32536.1. [Q86UA6-1]
CCDS54075.1. [Q86UA6-8]
CCDS54076.1. [Q86UA6-2]
CCDS54077.1. [Q86UA6-9]
CCDS54079.1. [Q86UA6-6]
RefSeqiNP_001028174.2. NM_001033002.3.
NP_001153715.1. NM_001160243.1.
NP_001153716.1. NM_001160244.1.
NP_001153718.1. NM_001160246.1.
NP_001153738.1. NM_001160266.1.
UniGeneiHs.462086.
Hs.555866.

Genome annotation databases

EnsembliENST00000536255; ENSP00000439939; ENSG00000129197.
ENST00000539417; ENSP00000446453; ENSG00000129197.
GeneIDi84268.
KEGGihsa:84268.

Polymorphism databases

DMDMi74727468.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY775314 mRNA. Translation: AAX14368.1 .
AY775315 mRNA. Translation: AAX14369.1 .
AY775316 mRNA. Translation: AAX14370.1 .
AY775317 mRNA. Translation: AAX14371.1 .
AY775318 mRNA. Translation: AAX14372.1 .
AY775319 mRNA. Translation: AAX14373.1 .
AY775320 mRNA. Translation: AAX14374.1 .
AY775321 mRNA. Translation: AAX14375.1 .
AY775323 mRNA. Translation: AAX14377.1 .
AY680654 mRNA. Translation: AAT80872.1 .
AY680655 mRNA. Translation: AAT80873.1 .
AY680656 mRNA. Translation: AAT80874.1 .
AY680657 mRNA. Translation: AAT80875.1 .
AY680658 mRNA. Translation: AAT80876.1 .
AY680659 mRNA. Translation: AAT80877.1 .
AY680660 mRNA. Translation: AAT80878.1 .
AK295394 mRNA. Translation: BAG58348.1 .
AK300409 mRNA. Translation: BAG62139.1 .
AC004148 Genomic DNA. No translation available.
BC004451 mRNA. Translation: AAH04451.1 .
BC046349 mRNA. Translation: AAH46349.1 .
BC051849 mRNA. Translation: AAH51849.1 .
CCDSi CCDS32536.1. [Q86UA6-1 ]
CCDS54075.1. [Q86UA6-8 ]
CCDS54076.1. [Q86UA6-2 ]
CCDS54077.1. [Q86UA6-9 ]
CCDS54079.1. [Q86UA6-6 ]
RefSeqi NP_001028174.2. NM_001033002.3.
NP_001153715.1. NM_001160243.1.
NP_001153716.1. NM_001160244.1.
NP_001153718.1. NM_001160246.1.
NP_001153738.1. NM_001160266.1.
UniGenei Hs.462086.
Hs.555866.

3D structure databases

ProteinModelPortali Q86UA6.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123995. 8 interactions.
IntActi Q86UA6. 4 interactions.

PTM databases

PhosphoSitei Q86UA6.

Polymorphism databases

DMDMi 74727468.

Proteomic databases

MaxQBi Q86UA6.
PaxDbi Q86UA6.
PRIDEi Q86UA6.

Protocols and materials databases

DNASUi 84268.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000536255 ; ENSP00000439939 ; ENSG00000129197 .
ENST00000539417 ; ENSP00000446453 ; ENSG00000129197 .
GeneIDi 84268.
KEGGi hsa:84268.

Organism-specific databases

CTDi 84268.
GeneCardsi GC17P005263.
H-InvDB HIX0013468.
HGNCi HGNC:28641. RPAIN.
HPAi HPA023924.
HPA031526.
neXtProti NX_Q86UA6.
PharmGKBi PA145007849.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46030.
GeneTreei ENSGT00390000006416.
HOVERGENi HBG082800.
InParanoidi Q86UA6.
OrthoDBi EOG7673BZ.
PhylomeDBi Q86UA6.
TreeFami TF326215.

Miscellaneous databases

ChiTaRSi RPAIN. human.
GeneWikii RPAIN.
GenomeRNAii 84268.
NextBioi 35534920.
PROi Q86UA6.

Gene expression databases

Bgeei Q86UA6.
CleanExi HS_RPAIN.
ExpressionAtlasi Q86UA6. baseline and differential.
Genevestigatori Q86UA6.

Family and domain databases

InterProi IPR028156. RIP.
IPR028159. RPA_interact_C_dom.
IPR028155. RPA_interact_central.
IPR028158. RPA_interact_N_dom.
[Graphical view ]
PANTHERi PTHR31742. PTHR31742. 1 hit.
Pfami PF14768. RPA_interact_C. 1 hit.
PF14767. RPA_interact_M. 1 hit.
PF14766. RPA_interact_N. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification, expression pattern, and subcellular location of human RIP isoforms."
    Chen J.-Z., Huang S.-D., Ji C.-N., Pang R.-Y., Xie Y., Xue J.-L.
    DNA Cell Biol. 24:464-469(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6 AND 7), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Sumoylation of the novel protein hRIPbeta is involved in replication protein A deposition in PML nuclear bodies."
    Park J., Seo T., Kim H., Choe J.
    Mol. Cell. Biol. 25:8202-8214(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4; 5; 6 AND 7), FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-103 AND LYS-121, INTERACTION WITH RPA1, MUTAGENESIS OF LYS-114; LYS-121 AND LYS-142, VARIANT ASN-103.
  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 3 AND 8), VARIANT ASN-103.
    Tissue: Corpus callosum and Placenta.
  4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 6), VARIANT ASN-103.
    Tissue: Eye.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRIP_HUMAN
AccessioniPrimary (citable) accession number: Q86UA6
Secondary accession number(s): B4DI36
, B4DTX7, E9PES3, J3KNH8, Q4G2Y0, Q4G2Y5, Q4G2Y8, Q6B4V9, Q6B4W0, Q6B4W1, Q6B4W4, Q86X49, Q9BT00
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 95 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3