Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Arfaptin-1

Gene

ARFIP1

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

Functioni

Putative target protein of ADP-ribosylation factor.

GO - Molecular functioni

  1. phosphatidylinositol-4-phosphate binding Source: FlyBase

GO - Biological processi

  1. intracellular protein transport Source: MGI
  2. regulation of Arp2/3 complex-mediated actin nucleation Source: GO_Central
  3. regulation of protein secretion Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Arfaptin-1
Alternative name(s):
ADP-ribosylation factor-interacting protein 1
Gene namesi
Name:ARFIP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:21496. ARFIP1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: MGI
  2. Golgi membrane Source: UniProtKB
  3. trans-Golgi network membrane Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134920621.

Polymorphism and mutation databases

DMDMi21264399.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 373372Arfaptin-1PRO_0000064665Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei5 – 51Phosphoserine1 Publication
Modified residuei36 – 361Phosphoserine1 Publication
Modified residuei39 – 391Phosphoserine1 Publication
Modified residuei69 – 691Phosphoserine2 Publications
Modified residuei79 – 791Phosphoserine1 Publication
Modified residuei132 – 1321Phosphoserine2 Publications
Modified residuei361 – 3611Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP53367.
PaxDbiP53367.
PRIDEiP53367.

PTM databases

PhosphoSiteiP53367.

Expressioni

Tissue specificityi

Ubiquitously expressed. Higher levels in liver, pancreas, placenta, skeletal muscle and heart.

Gene expression databases

BgeeiP53367.
CleanExiHS_ARFIP1.
ExpressionAtlasiP53367. baseline and differential.
GenevestigatoriP53367.

Organism-specific databases

HPAiCAB005080.
HPA037375.
HPA063759.

Interactioni

Subunit structurei

Interacts with non-myristoylated GTP-bound ARF3, but not to GDP-bound ARF3, and also to ARF1. Binds with lower affinity to ARF5 and with very little affinity to ARF6.1 Publication

Protein-protein interaction databases

BioGridi118084. 21 interactions.
IntActiP53367. 3 interactions.
MINTiMINT-3019815.
STRINGi9606.ENSP00000296557.

Structurei

3D structure databases

ProteinModelPortaliP53367.
SMRiP53367. Positions 151-351.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini153 – 353201AHPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 AH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG302946.
GeneTreeiENSGT00500000044828.
HOGENOMiHOG000236308.
HOVERGENiHBG050564.
InParanoidiP53367.
OMAiFQVHKEK.
OrthoDBiEOG7VQJD9.
PhylomeDBiP53367.
TreeFamiTF314945.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR010504. AH_dom.
IPR030793. Arfaptin-1.
IPR030798. Arfaptin_fam.
[Graphical view]
PANTHERiPTHR12141. PTHR12141. 1 hit.
PTHR12141:SF4. PTHR12141:SF4. 1 hit.
PfamiPF06456. Arfaptin. 1 hit.
[Graphical view]
SMARTiSM01015. Arfaptin. 1 hit.
[Graphical view]
PROSITEiPS50870. AH. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform B (identifier: P53367-1) [UniParc]FASTAAdd to basket

Also known as: 1b

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
MAQESPKNSA AEIPVTSNGE VDDSREHSFN RDLKHSLPSG LGLSETQITS
60 70 80 90 100
HGFDNTKEGV IEAGAFQGSP APPLPSVMSP SRVAASRLAQ QGSDLIVPAG
110 120 130 140 150
GQRTQTKSGP VILADEIKNP AMEKLELVRK WSLNTYKCTR QIISEKLGRG
160 170 180 190 200
SRTVDLELEA QIDILRDNKK KYENILKLAQ TLSTQLFQMV HTQRQLGDAF
210 220 230 240 250
ADLSLKSLEL HEEFGYNADT QKLLAKNGET LLGAINFFIA SVNTLVNKTI
260 270 280 290 300
EDTLMTVKQY ESARIEYDAY RTDLEELNLG PRDANTLPKI EQSQHLFQAH
310 320 330 340 350
KEKYDKMRND VSVKLKFLEE NKVKVLHNQL VLFHNAIAAY FAGNQKQLEQ
360 370
TLKQFHIKLK TPGVDAPSWL EEQ
Length:373
Mass (Da):41,738
Last modified:May 27, 2002 - v2
Checksum:i7A315D0E67DECDBF
GO
Isoform A (identifier: P53367-2) [UniParc]FASTAAdd to basket

Also known as: 1a

The sequence of this isoform differs from the canonical sequence as follows:
     69-100: Missing.

Show »
Length:341
Mass (Da):38,599
Checksum:i94675E3FF3FB9D08
GO
Isoform 3 (identifier: P53367-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     32-211: Missing.

Note: No experimental confirmation available.

Show »
Length:193
Mass (Da):22,055
Checksum:iA8203E8608316921
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei32 – 211180Missing in isoform 3. 1 PublicationVSP_057425Add
BLAST
Alternative sequencei69 – 10032Missing in isoform A. 3 PublicationsVSP_004088Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52521 mRNA. Translation: AAA97923.1.
AF124489 mRNA. Translation: AAD29390.1.
AK290472 mRNA. Translation: BAF83161.1.
AK299600 mRNA. Translation: BAG61531.1.
AC099339 Genomic DNA. No translation available.
AC106882 Genomic DNA. No translation available.
AC113155 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04968.1.
CH471056 Genomic DNA. Translation: EAX04969.1.
BC103759 mRNA. Translation: AAI03760.1.
BC105114 mRNA. Translation: AAI05115.1.
BC105116 mRNA. Translation: AAI05117.1.
BC143675 mRNA. Translation: AAI43676.1.
CCDSiCCDS34080.1. [P53367-1]
CCDS3780.1. [P53367-2]
PIRiG02515.
RefSeqiNP_001020764.1. NM_001025593.2. [P53367-2]
NP_001020766.1. NM_001025595.2. [P53367-1]
NP_001274360.1. NM_001287431.1. [P53367-1]
NP_001274361.1. NM_001287432.1. [P53367-1]
NP_001274362.1. NM_001287433.1. [P53367-2]
NP_055262.1. NM_014447.3. [P53367-2]
UniGeneiHs.416089.

Genome annotation databases

EnsembliENST00000353617; ENSP00000296557; ENSG00000164144. [P53367-1]
ENST00000356064; ENSP00000348360; ENSG00000164144. [P53367-2]
ENST00000405727; ENSP00000384189; ENSG00000164144. [P53367-2]
ENST00000429148; ENSP00000396653; ENSG00000164144. [P53367-3]
ENST00000451320; ENSP00000395083; ENSG00000164144. [P53367-1]
ENST00000618090; ENSP00000479111; ENSG00000164144. [P53367-2]
GeneIDi27236.
KEGGihsa:27236.
UCSCiuc003imz.3. human. [P53367-1]
uc003ina.3. human. [P53367-2]
uc011cij.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52521 mRNA. Translation: AAA97923.1.
AF124489 mRNA. Translation: AAD29390.1.
AK290472 mRNA. Translation: BAF83161.1.
AK299600 mRNA. Translation: BAG61531.1.
AC099339 Genomic DNA. No translation available.
AC106882 Genomic DNA. No translation available.
AC113155 Genomic DNA. No translation available.
CH471056 Genomic DNA. Translation: EAX04968.1.
CH471056 Genomic DNA. Translation: EAX04969.1.
BC103759 mRNA. Translation: AAI03760.1.
BC105114 mRNA. Translation: AAI05115.1.
BC105116 mRNA. Translation: AAI05117.1.
BC143675 mRNA. Translation: AAI43676.1.
CCDSiCCDS34080.1. [P53367-1]
CCDS3780.1. [P53367-2]
PIRiG02515.
RefSeqiNP_001020764.1. NM_001025593.2. [P53367-2]
NP_001020766.1. NM_001025595.2. [P53367-1]
NP_001274360.1. NM_001287431.1. [P53367-1]
NP_001274361.1. NM_001287432.1. [P53367-1]
NP_001274362.1. NM_001287433.1. [P53367-2]
NP_055262.1. NM_014447.3. [P53367-2]
UniGeneiHs.416089.

3D structure databases

ProteinModelPortaliP53367.
SMRiP53367. Positions 151-351.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118084. 21 interactions.
IntActiP53367. 3 interactions.
MINTiMINT-3019815.
STRINGi9606.ENSP00000296557.

PTM databases

PhosphoSiteiP53367.

Polymorphism and mutation databases

DMDMi21264399.

Proteomic databases

MaxQBiP53367.
PaxDbiP53367.
PRIDEiP53367.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000353617; ENSP00000296557; ENSG00000164144. [P53367-1]
ENST00000356064; ENSP00000348360; ENSG00000164144. [P53367-2]
ENST00000405727; ENSP00000384189; ENSG00000164144. [P53367-2]
ENST00000429148; ENSP00000396653; ENSG00000164144. [P53367-3]
ENST00000451320; ENSP00000395083; ENSG00000164144. [P53367-1]
ENST00000618090; ENSP00000479111; ENSG00000164144. [P53367-2]
GeneIDi27236.
KEGGihsa:27236.
UCSCiuc003imz.3. human. [P53367-1]
uc003ina.3. human. [P53367-2]
uc011cij.2. human.

Organism-specific databases

CTDi27236.
GeneCardsiGC04P153701.
HGNCiHGNC:21496. ARFIP1.
HPAiCAB005080.
HPA037375.
HPA063759.
MIMi605928. gene.
neXtProtiNX_P53367.
PharmGKBiPA134920621.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG302946.
GeneTreeiENSGT00500000044828.
HOGENOMiHOG000236308.
HOVERGENiHBG050564.
InParanoidiP53367.
OMAiFQVHKEK.
OrthoDBiEOG7VQJD9.
PhylomeDBiP53367.
TreeFamiTF314945.

Miscellaneous databases

ChiTaRSiARFIP1. human.
GeneWikiiARFIP1.
GenomeRNAii27236.
NextBioi35474578.
PROiP53367.
SOURCEiSearch...

Gene expression databases

BgeeiP53367.
CleanExiHS_ARFIP1.
ExpressionAtlasiP53367. baseline and differential.
GenevestigatoriP53367.

Family and domain databases

Gene3Di1.20.1270.60. 1 hit.
InterProiIPR027267. AH/BAR-dom.
IPR010504. AH_dom.
IPR030793. Arfaptin-1.
IPR030798. Arfaptin_fam.
[Graphical view]
PANTHERiPTHR12141. PTHR12141. 1 hit.
PTHR12141:SF4. PTHR12141:SF4. 1 hit.
PfamiPF06456. Arfaptin. 1 hit.
[Graphical view]
SMARTiSM01015. Arfaptin. 1 hit.
[Graphical view]
PROSITEiPS50870. AH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes."
    Kanoh H., Williger B.-T., Exton J.H.
    J. Biol. Chem. 272:5421-5429(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
  2. "Arfaptin-1b, a long splice variant of arfaptin-1."
    Premont R.T., Lefkowitz R.J.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
    Tissue: Liver.
  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 A AND 3).
    Tissue: Brain.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 A AND B).
    Tissue: Brain and Uterus.
  7. "Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D."
    Williger B.-T., Provost J.J., Ho W.-T., Milstine J., Exton J.H.
    FEBS Lett. 454:85-89(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARF1; ARF3; ARF5 AND ARF6.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69 AND SER-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-69 AND SER-79, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiARFP1_HUMAN
AccessioniPrimary (citable) accession number: P53367
Secondary accession number(s): B4DS69
, Q2M2X4, Q3SYL4, Q9Y2X6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 27, 2002
Last modified: April 29, 2015
This is version 122 of the entry and version 2 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 4
    Human chromosome 4: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.